Peptide name : Glycinin G5

Source/Organism : Soyabean (Soybean)

Linear/Cyclic : Linear

Chirality : Not found

Peptide length: 516

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-bacterial activitiy

Amino acid composition bar chart :

Molecular mass : 57955.4207 Dalton

Aliphatic index : 0.668

Instability index : 57.9402

Hydrophobicity (GRAVY) : -0.839

Isoelectric point : 5.5991

Charge (pH 7) : -13.1606

Aromaticity : 0.071

Molar extinction coefficient (cysteine, cystine): (44350, 44850)

Hydrophobic/hydrophilic ratio : 0.77931034

hydrophobic moment : -0.016

Missing amino acid : None

Most occurring amino acid : Q

Most occurring amino acid frequency : 45

Least occurring amino acid : W

Least occurring amino acid frequency : 4

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.3, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CS)NC(=O)CNC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccccc1)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)CNC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)CNC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)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1 : González-Montoya M, et al. Peptides derived from in vitro gastrointestinal digestion of germinated soybean proteins inhibit human colon cancer cells proliferation and inflammation. Food Chem. 2018; 242:75-82. doi: 10.1016/j.foodchem.2017.09.035

2 : Peng XQ, et al. Molecular Mechanism for Improving Emulsification Efficiency of Soy Glycinin by Glycation with Soy Soluble Polysaccharide. J Agric Food Chem. 2018; 66:12316-12326. doi: 10.1021/acs.jafc.8b03398

3 : Wang T, et al. Advances of research on glycinin and β-conglycinin: a review of two major soybean allergenic proteins. Crit Rev Food Sci Nutr. 2014; 54:850-62. doi: 10.1080/10408398.2011.613534

4 : Taliercio E and Kim SW. Epitopes from two soybean glycinin subunits are antigenic in pigs. J Sci Food Agric. 2013; 93:2927-32. doi: 10.1002/jsfa.6113

5 : Nielsen NC, et al. Characterization of the glycinin gene family in soybean. Plant Cell. 1989; 1:313-28. doi: 10.1105/tpc.1.3.313

6 : Prak K, et al. Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013; 69:937-41. doi: 10.1107/S1744309113019684

7 : Maruyama N, et al. A vacuolar sorting receptor-independent sorting mechanism for storage vacuoles in soybean seeds. Sci Rep. 2018; 8:1108. doi: 10.1038/s41598-017-18697-w

8 : Adachi M, et al. Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer. Proc Natl Acad Sci U S A. 2003; 100:7395-400. doi: 10.1073/pnas.0832158100

9 : Holzhauser T, et al. Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. J Allergy Clin Immunol. 2009; 123:452-8. doi: 10.1016/j.jaci.2008.09.034

10 : Sitohy MZ, et al. In vitro and in situ antimicrobial action and mechanism of glycinin and its basic subunit. Int J Food Microbiol. 2012; 154:19-29. doi: 10.1016/j.ijfoodmicro.2011.12.004

11 : He XT, et al. Thermal aggregation behaviour of soy protein: characteristics of different polypeptides and sub-units. J Sci Food Agric. 2016; 96:1121-31. doi: 10.1002/jsfa.7184

12 : Li YQ, et al. Effects of glycinin basic polypeptide on sensory and physicochemical properties of chilled pork. Food Sci Biotechnol. 2016; 25:803-809. doi: 10.1007/s10068-016-0135-2

13 : Zheng S, et al. Acidic polypeptides A_1a, A₃ and A₄ of Gly m 6 (glycinin) are allergenic for piglets. Vet Immunol Immunopathol. 2018; 202:147-152. doi: 10.1016/j.vetimm.2018.06.003

14 : Han F, et al. Effects of glycinin and β-conglycinin on growth performance and intestinal health in juvenile Chinese mitten crabs (Eriocheir sinensis). Fish Shellfish Immunol. 2019; 84:269-279. doi: 10.1016/j.fsi.2018.10.013

15 : Peng C, et al. Soybean Glycinin- and β-Conglycinin-Induced Intestinal Damage in Piglets via the p38/JNK/NF-κB Signaling Pathway. J Agric Food Chem. 2018; 66:9534-9541. doi: 10.1021/acs.jafc.8b03641

16 : González-Montoya M, et al. Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes. Int J Mol Sci. 2018; 19:(unknown pages). doi: 10.3390/ijms19102883

17 : Natarajan S, et al. Proteomic and genetic analysis of glycinin subunits of sixteen soybean genotypes. Plant Physiol Biochem. 2007; 45:436-44. doi: 10.1016/j.plaphy.2007.03.031

18 : Bu G, et al. The structural properties and antigenicity of soybean glycinin by glycation with xylose. J Sci Food Agric. 2017; 97:2256-2262. doi: 10.1002/jsfa.8036

19 : Fukazawa C, et al. Glycinin A3B4 mRNA. Cloning and sequencing of double-stranded cDNA complementary to a soybean storage protein. J Biol Chem. 1985; 260:6234-9.

20 : Renkema JM, et al. The effect of pH on heat denaturation and gel forming properties of soy proteins. J Biotechnol. 2000; 79:223-30. doi: 10.1016/s0168-1656(00)00239-x

21 : Zhao GP, et al. Antibacterial Actions of Glycinin Basic Peptide against Escherichia coli. J Agric Food Chem. 2017; 65:5173-5180. doi: 10.1021/acs.jafc.7b02295

22 : Tandang-Silvas MR, et al. Conservation and divergence on plant seed 11S globulins based on crystal structures. Biochim Biophys Acta. 2010; 1804:1432-42. doi: 10.1016/j.bbapap.2010.02.016

23 : Xiang N, et al. Methodology for identification of pore forming antimicrobial peptides from soy protein subunits β-conglycinin and glycinin. Peptides. 2016; 85:27-40. doi: 10.1016/j.peptides.2016.09.004

Paper title : Peptides derived from in vitro gastrointestinal digestion of germinated soybean proteins inhibit human colon cancer cells proliferation and inflammation.

Doi : https://doi.org/10.1016/j.foodchem.2017.09.035

Abstract : The aim was to investigate the potential of germinated soybean proteins asa source of peptides with anticancer and anti-inflammatory activities produced after simulated gastrointestinal digestion. Protein concentrate from germinated soybean was hydrolysed with pepsin/pancreatin and fractionated by ultrafiltration. Whole digest and fractions>10, 5-10, and<5kDa caused cytotoxicity to Caco-2, HT-29, HCT-116 human colon cancer cells, and reduced inflammatory response caused by lipopolysaccharide in macrophages RAW 264.7. Antiproliferative and anti-inflammatory effects were generally higher in 5-10kDa fractions. This fraction was further purified by semi-preparative chromatography and characterised by HPLC-MS/MS. The most potent fraction was mainly composed of β-conglycinin and glycinin fragments rich in glutamine. This is the first report on the anti-cancer and anti-inflammatory effects of newly isolated and identified peptides from germinated soybean released during gastrointestinal digestion. These findings highlight the potential of germination as a process to obtain functional foods or nutraceuticals for colon cancer prevention.

Paper title : Molecular Mechanism for Improving Emulsification Efficiency of Soy Glycinin by Glycation with Soy Soluble Polysaccharide.

Doi : https://doi.org/10.1021/acs.jafc.8b03398

Abstract : Glycation with carbohydrates has been considered to be an effective strategy to improve the emulsifying properties of plant storage globulins, but the knowledge is inconsistent and even contradictory. This work reported that the glycation with soy soluble polysaccharide (SSPS) progressively improved the emulsification efficiency of soy glycinin (SG) in a degree-of-glycation (DG)-dependent manner. The glycation occurred in both the acidic (A) and basic (B) polypeptides to a similar extent. The physicochemical and structural properties of glycated SG samples with different DG values of 0-35% were characterized. The emulsifying properties of unglycated and glycated SG were performed on the emulsions at an oil fraction of 0.3 and a protein concentration in the aqueous phase, produced using microfluidization as the emusification process. The glycation with increasing the DG led to a progressive decrease in solubility and surface hydrophobicity but remarkably increased the magnitude of ζ-potential. Dynamic latter scattering and spectroscopic results showed that the glycation resulted in a gradual dissociation of the 11S-form SG at the quaternary level (into different [AB] subunits), in a DG-dependent way, while their tertiary ([AB] subunits) and secondary structure were slightly affected. Besides the emulsification efficiency, the glycation progressively accelerated the droplet flocculation and facilitated the adsorption of the proteins at the interface and formation of bridged emulsions. The results demonstrated that the improvement of the emulsification efficiency of SG by the glycation with SSPS was largely attributed to the enhanced conformation flexibility at the [AB] subunit level as well as facilitated formation of bridged emulsions. It was also confirmed that once the glycated SG adsorbed at the interface, it would readily dissociated into subunits; the dissociated [AB] subunits exhibited an outstanding Pickering stabilization. The findings would be of importance for providing new knowledge about the molecular mechanism for the modification of emulsifying properties of oligomeric globulins by the glycation with polysaccharides.

Paper title : Advances of research on glycinin and β-conglycinin: a review of two major soybean allergenic proteins.

Doi : https://doi.org/10.1080/10408398.2011.613534

Abstract : Being an important crop, soybean is widely used in the world and plays a vital role in human and animal nutrition. However, it contains several antinutritional factors (ANFs) including soybean agglutinin, soybean protease inhibitors, soybean allergenic proteins, etc., that may result in poor food utilization, decreased growth performance, and even disease. Among these ANFs, soybean allergenic proteins can lead to allergic reactions in human and animals, which has become a public problem all over the world, but our knowledge on it is still inadequate. This paper aims to provide an update on the characteristics, detection or exploration methods, and in vivo research models of soybean allergenic proteins; especially glycinin and β-conglycinin are deeply discussed. Through this review, we may have a better understanding on the advances of research on these two soybean allergenic proteins. Besides, the ingredient processing used to reduce the allergenicity of soybean is also reviewed.

Paper title : Epitopes from two soybean glycinin subunits are antigenic in pigs.

Doi : https://doi.org/10.1002/jsfa.6113

Abstract : BACKGROUND: Glycinin is a seed storage protein in soybean (Glycine max) that is allergenic in pigs. Glycinin is a hexamer composed of subunits consisting of basic and acidic portions joined by disulfide bridges. There are five glycinin subunit isoforms designated Gy1-Gy5. The purpose of this study is to identify epitopes from selected glycinin subunits that are antigenic in pigs. RESULTS: Twenty-seven out of 30 pigs had antibodies against glycinin in their sera. Ten of these sera had immunoglobulin G (IgG) against the Gy4 (A5A4B3) or Gy1 (A1aBx) subunit. Three sera recognised overlapping regions between the two subunits tested, though no serum stained both A5A4B3 and A1aBx. Two sera stained a highly conserved region between A5A4B3 and A1aBx, though again neither serum stained both peptides. The basic part of the A1aBx subunit was not recognised by any of the sera tested even though immunoblot data indicated that the basic and acidic subunits of glycinin are nearly equally antigenic. CONCLUSION: Two antigenic regions of A5A4B3 and A1aBx were identified that bound antibodies in half of the sera that reacted with these two proteins. Half of the sera reacted with unique regions of A5A4B3 and A1aBx. The failure of the basic portion of A1aBx to bind pig antibodies may indicate that it is less antigenic than the basic portion of A5A4B3 and other glycinin subunits.

Paper title : Characterization of the glycinin gene family in soybean.

Doi : https://doi.org/10.1105/tpc.1.3.313

Abstract : We characterized the structure, organization, and expression of genes that encode the soybean glycinins, a family of storage proteins synthesized exclusively in seeds during embryogenesis. Five genes encode the predominant glycinin subunits found in soybeans, and they have each been cloned, sequenced, and compared. The five genes have diverged into two subfamilies that are designated as Group-I and Group-II glycinin genes. Each glycinin gene contains four exons and three introns like genes that encode related proteins in other legumes. Two other genes have been identified and designated as "glycinin-related" because they hybridize weakly with the five glycinin genes. Although not yet characterized, glycinin-related genes could encode other glycinin subunit families whose members accumulate in minor amounts in seeds. The three Group-I glycinin genes are organized into two chromosomal domains, each about 45 kilobase pairs in length. The two domains have a high degree of homology, and contain at least five genes each that are expressed either in embryos or in mature plant leaves. Gel blot studies with embryo mRNA, as well as transcription studies with 32P-RNA synthesized in vitro from purified embryo nuclei, indicate that glycinin and glycinin-related genes become transcriptionally activated in a coordinated fashion early in embryogenesis, and are repressed coordinately late in seed development. In addition to transcriptional control processes, posttranscriptional events also are involved in regulating glycinin and glycinin-related mRNA levels during embryogenesis.

Paper title : Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2.

Doi : https://doi.org/10.1107/S1744309113019684

Abstract : Glycinin is one of the most abundant storage-protein molecules in soybean seeds and is composed of five subunits (A1aB1b, A1bB2, A2B1a, A3B4 and A5A4B3). A1bB2 was purified from a mutant soybean cultivar containing glycinin composed of only A5A4B3 and A1bB2. At 281 K the protein formed hexagonal, rectangular and rod-shaped crystals in the first [0.1 M imidazole pH 8.0, 0.2 M MgCl₂, 35%(v/v) MPD], second [0.1 M sodium citrate pH 5.6, 0.2 M ammonium acetate, 30%(v/v) MPD] and third (0.1 M phosphate-citrate pH 4.2, 2.0 M ammonium sulfate) crystallization conditions, respectively. X-ray diffraction data were collected to resolutions of 1.85, 1.85 and 2.5 Å from crystals of the three different shapes. The crystals belonged to space groups P6₃22, P2₁ and P1, with unit-cell parameters a = b = 143.60, c = 84.54 Å, a = 114.54, b = 105.82, c = 116.67 Å, β = 94.99° and a = 94.45, b = 94.96, c = 100.66 Å, α = 107.02, β = 108.44, γ = 110.71°, respectively. One, six and six subunits of A1bB2 were estimated to be present in the respective asymmetric units. The three-dimensional structure of the A1bB2 hexamer is currently being determined.

Paper title : A vacuolar sorting receptor-independent sorting mechanism for storage vacuoles in soybean seeds.

Doi : https://doi.org/10.1038/s41598-017-18697-w

Abstract : The seed storage proteins of soybean (Glycine max) are composed mainly of glycinin (11S globulin) and β-conglycinin (7S globulin). The subunits of glycinin (A1aB1b, A1bB2, A2B1a, A3B4, and A5A4B3) are synthesized as a single polypeptide precursor. These precursors are assembled into trimers with a random combination of subunits in the endoplasmic reticulum, and are sorted to the protein storage vacuoles. Proteins destined for transport to protein storage vacuoles possess a vacuolar sorting determinant, and in this regard, the A1aB1b subunit contains a C-terminal peptide that is sufficient for its sorting to protein storage vacuoles. The A3B4 subunit, however, lacks a corresponding C-terminal sorting determinant. In this study, we found that, unlike the A1aB1b subunit, the A3B4 subunit does not bind to previously reported vacuolar sorting receptors. Despite this difference, we observed that the A3B4 subunit is sorted to protein storage vacuoles in a transgenic soybean line expressing the A3B4 subunit of glycinin. These results indicate that a protein storage vacuolar sorting mechanism that functions independently of the known vacuolar sorting receptors in seeds might be present in soybean seeds.

Paper title : Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer.

Doi : https://doi.org/10.1073/pnas.0832158100

Abstract : Most plant seeds contain 11S globulins as major storage proteins for their nutrition. Soybean glycinin belongs to the 11S globulin family and consists of five kinds of subunits. We determined the crystal structure of a homohexamer of the glycinin A3B4 subunit at 2.1-A resolution. The crystal structure shows that the hexamer has 32-point group symmetry formed by face-to-face stacking of two trimers. The interface buries the highly conserved interchain disulfide. Based on the structure, we propose that an ingenious face-to-face mechanism controls the hexamer formation of the 11S globulin by movement of a mobile disordered region to the side of the trimer after posttranslational processing. Electrostatic analysis of the faces suggests that the interchain disulfide-containing face has high positive potential at acidic pH, which induces dissociation of the hexamer into trimers that may be susceptible to proteinases after seed imbibition. This dissociation might result in the degradation and mobilization of 11S globulins as storage proteins in embryos during germination and seedling growth.

Paper title : Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy.

Doi : https://doi.org/10.1016/j.jaci.2008.09.034

Abstract : BACKGROUND: Soybean is considered an important allergenic food, but published data on soybean allergens are controversial. OBJECTIVE: We sought to identify relevant soybean allergens and correlate the IgE-binding pattern to clinical characteristics in European patients with confirmed soy allergy. METHODS: IgE-reactive proteins were identified from a soybean cDNA expression library, purified from natural soybean source, or expressed in Escherichia coli. The IgE reactivity in 30 sera from subjects with a positive double-blind, placebo-controlled soybean challenge (n = 25) or a convincing history of anaphylaxis to soy (n = 5) was analyzed by ELISA or CAP-FEIA. RESULTS: All subunits of Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) were IgE-reactive: 53% (16/30) of the study subjects had specific IgE to at least 1 major storage protein, 43% (13/30) to Gly m 5 , and 36% (11/30) to Gly m 6. Gly m 5 was IgE-reactive in 5 of 5 and Gly m 6 in 3 of 5 children. IgE-binding to Gly m 5 or Gly m 6 was found in 86% (6/7) subjects with anaphylaxis to soy and in 55% (6/11) of subjects with moderate but only 33% (4/12) of subjects with mild soy-related symptoms. The odds ratio (P < .05) for severe versus mild allergic reactions in subjects with specific IgE to Gly m 5 or Gly m6 was 12/1. CONCLUSION: Sensitization to the soybean allergens Gly m 5 or Gly m 6 is potentially indicative for severe allergic reactions to soy.

Paper title : In vitro and in situ antimicrobial action and mechanism of glycinin and its basic subunit.

Doi : https://doi.org/10.1016/j.ijfoodmicro.2011.12.004

Abstract : Glycinin, basic subunit and β-conglycinin were isolated from soybean protein isolate and tested for their antimicrobial action against pathogenic and spoilage bacteria as compared to penicillin. The three fractions exhibited antibacterial activities equivalent to or higher than penicillin in the next order; basic subunit>glycinin>β-conglycinin with MIC of 50, 100 and 1000 μg/mL, respectively. The IC(50%) values of the basic subunit, glycinin and β-conglycinin against Listeria\monocytogenes were 15, 16 and 695 μg/mL, against Bacillussubtilis were 17, 20, and 612 μg/mL, and against S. Enteritidis were 18, 21 and 526 μg/mL, respectively. Transmission electron microscopy images of L. monocytogenes and S. Enteritidis exhibited bigger sizes and separation of cell wall from cell membrane when treated with glycinin or basic subunit. Scanning electron microscopy of B. subtilis indicated signs of irregular wrinkled outer surface, fragmentation, adhesion and aggregation of damaged cells or cellular debris when treated with glycinin or the basic subunits but not with penicillin. All tested substances particularly the basic subunit showed increased concentration-dependent cell permeation assessed by crystal violet uptake. The antimicrobial action of glycinin and basic subunit was swifter than that of penicillin. The cell killing efficiency was in the following descending order; basic subunit>glycinin>penicillin>β-conglycinin and the susceptibility of the bacteria to the antimicrobial agents was in the next order: L. monocytogenes>B. Subtilis>S. Enteritidis. Adding glycinin and the basic subunit to pasteurized milk inoculated with the three bacteria; L. monocytogenes, B. Subtilis and S. Enteritidis (ca. 5 log CFU/mL) could inhibit their propagation after 16-20 days storage at 4 °C by 2.42-2.98, 4.25-4.77 and 2.57-3.01 log and by 3.22-3.78, 5.65-6.27 and 3.35-3.72 log CFU/mL, respectively.

Paper title : Thermal aggregation behaviour of soy protein: characteristics of different polypeptides and sub-units.

Doi : https://doi.org/10.1002/jsfa.7184

Abstract : BACKGROUND: Due to the differences in structure and composition of glycinin and β-conglycinin, they exhibit different characteristics during heat treatment. In present study, the thermal aggregation behaviour of glycinin, β-conglycinin and their isolated sub-units was investigated at pH 7.0. RESULTS: Acidic polypeptides, basic polypeptides, αα' and β sub-units of soy protein were denatured during the isolation process. The degree of aggregation of protein fractions after heat treatment was in the order: denatured basic polypeptides > native glycinin > denatured β sub-unit > native β-conglycinin > denatured acidic polypeptides > denatured αα' sub-units. Glycinin, β-conglycinin, acidic polypeptides and αα'/β sub-units exhibited different changing trends of surface hydrophobicity with increasing temperature. The αα' sub-units showed higher ability to suppress thermal aggregation of basic polypeptides than β sub-units during heat treatment. The β sub-units were shown to form soluble aggregates with glycinin after heating. CONCLUSION: The interaction mechanism of αα' and β sub-units heated with basic polypeptides was proposed. For the β sub-units-basic polypeptides mixed system, more hydrophobic chains were binding together and buried inside during heat treatment, which resulted in lower surface hydrophobicity. The αα' sub-units-basic polypeptides mixed system was considered to be a stable system with higher surface hydrophobicity after being heated.

Paper title : Effects of glycinin basic polypeptide on sensory and physicochemical properties of chilled pork.

Doi : https://doi.org/10.1007/s10068-016-0135-2

Abstract : Effects of glycinin basic polypeptide (GBP) on sensory and physicochemical properties of pork during chilled storage were investigated. Pork treated with GBP was analyzed periodically for sensory properties, pH, total volatile base nitrogen (TVB-N), α-thiobarbituric acid (TBA), and total viable count (TVC) values. Compared with controls, TBA values of pork treated with GBP did not change. TVB-N, pH, and TVC values of pork showed reductions with increasing concentrations of GBP during 8 days of storage. However, there were increases in sensory scores. TVC values of treated pork showed a positive linear relationship with both pH and TVB-N values. GBP at 0.16 and 0.20% efficiently inhibited bacterial growth, and enhanced chilled pork sensory scores. Therefore, GBP has potential as a pork biological preservative for extension of shelf life during chilled storage.

Paper title : Acidic polypeptides A_1a, A₃ and A₄ of Gly m 6 (glycinin) are allergenic for piglets.

Doi : https://doi.org/10.1016/j.vetimm.2018.06.003

Abstract : Gly m 6 (glycinin) is one of the major antigenic proteins in soybeans responsible for transient hypersensitivity to soybean meal in weaned piglets. The globulin is a hexamer consisting of subunits containing basic and acidic polypeptides. Multiple acidic polypeptides have long been demonstrated to be allergens for humans and play a key role in the overall allergenicity of Gly m 6. To date, knowledge on the allergenicity of the acidic polypeptides for piglets is very limited. The purpose of this study was to identify the acidic polypeptides that were allergenic for piglets and to characterize these acidic polypeptides by ELISA, western blot, skin prick and basophile histamine release test. The IgG and IgE antibody binding capacities of the acidic polypeptides of Gly m 6 were determined using ELISA and western blot analysis with sera from Gly m 6 sensitized piglets. Skin prick test and basophile histamine release test were conducted to measure the effector cell response to the polypeptides. Specific IgG and IgE antibodies against A_1a, A₃ and A₄ of Gly m 6 were identified in the sera of Gly m 6 sensitized piglets. Meanwhile, positive skin prick test and specific histamine release responses were also induced by the acidic polypeptide A_1a, A₃ and A₄ of Gly m 6 from the basophiles of Gly m 6 sensitized piglets. The results demonstrate that the acidic polypeptide A_1a, A₃ and A₄ of Gly m 6 are allergenic for piglets.

Paper title : Effects of glycinin and β-conglycinin on growth performance and intestinal health in juvenile Chinese mitten crabs (Eriocheir sinensis).

Doi : https://doi.org/10.1016/j.fsi.2018.10.013

Abstract : This study investigates the effects of two soybean antigens (glycinin and β-conglycinin) as an antinutritional substance in the diet on the growth, digestive ability, intestinal health and microbiota of juvenile Chinese mitten crabs (Eriocheir sinensis). The isonitrogenous and isolipidic diets contained two soybean antigens at two levels each (70 and 140 g/kg β-conglycinin, 80 and 160 g/kg glycinin) and a control diet without β-conglycinin or glycinin supplementation, and were used respectively to feed juvenile E. sinensis for seven weeks. Dietary inclusion of either glycinin or β-conglycinin significantly reduced crab survival and weight gain. The crabs fed diets containing soybean antigens had higher malondialdehyde concentrations and lower catalase activities in the intestine than those in the control. The activities of trypsin and amylase in the intestine were suppressed by dietary β-conglycinin and glycinin. Dietary glycinin or β-conglycinin impaired the immunity and morphological structure of intestine, especially the peritrophic membrane. The mRNA expression of constitutive and inducible immune responsive genes (lipopolysaccharide-induced TNF-α factor and interleukin-2 enhancer-binding factor 2) increased while the mRNA expression of the main genes related to the structural integrity peritrophic membrane (peritrophin-like gene and peritrophic 2) significantly decreased in the groups with soybean antigen addition. Soybean antigen could also change the intestinal microbial community. The abundance of pathogenic bacteria (Ochrobactrum, Burkholderia and Pseudomonas) increased significantly in both soybean antigen groups. Although pathogenic bacteria Vibrio were up-regulated in the glycinin group, the abundance of Dysgonomonas that degraded lignocellulose and ameliorated the gut environment decreased in the glycinin group. This study indicates that existence of soybean antigens (glycinin or β-conglycinin) could induce gut inflammation, reshape the community of gut microbiota, and cause digestive dysfunction, ultimately leading to impaired growth in crabs.

Paper title : Soybean Glycinin- and β-Conglycinin-Induced Intestinal Damage in Piglets via the p38/JNK/NF-κB Signaling Pathway.

Doi : https://doi.org/10.1021/acs.jafc.8b03641

Abstract : β-Conglycinin (7S) and glycinin (11S) are known to induce a variety of hypersensitivity reactions involving the skin, intestinal tract, and respiratory tract. The present study aimed to identify the mechanism underlying the development of allergy to soybean antigen proteins, using piglets as an animal model. Weaned "Duroc × Landrace × Yorkshire" piglets were fed a diet supplemented with 7S or 11S to investigate the signaling pathway involved in intestinal damage in piglets. Results showed that serum nitric oxide (NO), tumor necrosis factor-α (TNF-α), and caspase-3 levels were significantly higher in 7S- and 11S-fed piglets compared to those in suckling or weaned ones. mRNA, protein, and phosphorylation levels of nuclear factor-kappa B (NF-κB), p38, and Jun N-terminal kinase (JNK) were higher in 7S- and 11S-fed piglets than in suckling and weaned ones. Overall, our results indicate that 7S and 11S damaged the intestinal function in piglets through their impact on NF-κB, JNK, and p38 expression.

Paper title : Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes.

Doi : https://doi.org/10.3390/ijms19102883

Abstract : Functional foods containing peptides offer the possibility to modulate the absorption of sugars and insulin levels to prevent diabetes. This study investigates the potential of germinated soybean peptides to modulate postprandial glycaemic response through inhibition of dipeptidyl peptidase IV (DPP-IV), salivary α-amylase, and intestinal α-glucosidases. A protein isolate from soybean sprouts was digested by pepsin and pancreatin. Protein digest and peptide fractions obtained by ultrafiltration (&lt;5, 5⁻10 and &gt;10 kDa) and subsequent semipreparative reverse phase liquid chromatography (F1, F2, F3, and F4) were screened for in vitro inhibition of DPP-IV, α-amylase, maltase, and sucrase activities. Protein digest inhibited DPP-IV (IC₅₀ = 1.49 mg/mL), α-amylase (IC₅₀ = 1.70 mg/mL), maltase, and sucrase activities of α-glucosidases (IC₅₀ = 3.73 and 2.90 mg/mL, respectively). Peptides of 5⁻10 and &gt;10 kDa were more effective at inhibiting DPP-IV (IC₅₀ = 0.91 and 1.18 mg/mL, respectively), while peptides of 5⁻10 and &lt;5 kDa showed a higher potency to inhibit α-amylase and α-glucosidases. Peptides in F1, F2, and F3 were mainly fragments from β-conglycinin, glycinin, and P34 thiol protease. The analysis of structural features of peptides in F1⁻F3 allowed the tentative identification of potential antidiabetic peptides. Germinated soybean protein showed a promising potential to be used as a nutraceutical or functional ingredient for diabetes prevention.

Paper title : Proteomic and genetic analysis of glycinin subunits of sixteen soybean genotypes.

Doi : https://doi.org/10.1016/j.plaphy.2007.03.031

Abstract : We investigated proteomic and genomic profiles of glycinin, a family of major storage proteins in 16 different soybean genotypes consisting of four groups including wild soybean (Glycine soja), unimproved cultivated soybean landraces from Asia (G. max), ancestors of N. American soybean (G. max), and modern soybean (G. max) genotypes. We observed considerable variation in all five glycinin subunits, G1, G2 G3, G4 and G5 using proteomics and genetic analysis. Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and mass spectrometry (MS) analysis showed that the wild genotypes had a range of 25-29 glycinin protein spots that included both acidic and basic polypeptides followed by the ancestors with 24-28, modern cultivars with 24-25, and landraces with 17-23 protein spots. Overall, the wild genotypes have a higher number of protein spots when compared to the other three genotypes. Major variation was observed in acidic polypeptides of G3, G4 and G5 compared to G1 and G2, and minor variation was observed in basic polypeptides of all subunits. Our data indicated that there are major variations of glycinin subunits between wild and cultivated genotypes rather than within the same groups. Based on Southern blot DNA analysis, we observed genetic polymorphisms in group I genes (G1, G2, and G3) between and within the four genotype groups, but not in group II genes (G4 and G5). This is the first study reporting the comparative analysis of glycinin in a diverse set of soybean genotypes using combined proteomic and genetic analysis.

Paper title : The structural properties and antigenicity of soybean glycinin by glycation with xylose.

Doi : https://doi.org/10.1002/jsfa.8036

Abstract : BACKGROUND: Soybean glycinin is considered a major allergenic protein, and glycation is widely used to reduce the allergenic potential of present allergens. Glycation of soybean glycinin with xylose at 55 °C for different lengths of time was investigated. The extent of Maillard reaction was reflected through the content changing of free amino groups, color analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alteration in the structural properties of glycinin was characterized by Fourier transform infrared spectroscopy, and antigenicity was evaluated by indirect competitive enzyme-linked immunosorbent assay. RESULTS: The changes in the color of glycinin-xylose samples and the reduction of free amino group content in proteins indicated that the Maillard reaction occurred. The degree of glycation increased in glycated samples with the increase in reaction time. Glycation induced the changes in the secondary structure of glycinin and the ordered structure of proteins increased during the glycation reaction. The antigenicity of glycinin was reduced with the increase in reaction time. After glycation for 12 h, the antigenicity of glycinin declined about 18% compared with native glycinin. CONCLUSION: The application of glycation may be an efficient method to reduce the antigenicity of soybean glycinin. © 2016 Society of Chemical Industry.

Paper title : Glycinin A3B4 mRNA. Cloning and sequencing of double-stranded cDNA complementary to a soybean storage protein.

Doi : https://doi.org/Not available

Abstract : The cDNA clones encoding the precursor form of glycinin A3B4 subunit have been identified from a library of soybean cotyledonary cDNA clones in the plasmid pBR322 by a combination of differential colony hybridizations, and then by immunoprecipitation of hybrid-selected translation product with A3-mono-specific antiserum. A recombinant plasmid, designated pGA3B41425, from one of six clones covering codons for the NH2-terminal region of the subunit was sequenced, and the amino acid sequence was inferred from the nucleotide sequence, which showed that the mRNA codes for a precursor protein of 516 amino acids. Analysis of this cDNA also showed that it contained 1786 nucleotides of mRNA sequence with a 5'-terminal nontranslated region of 46 nucleotides, a signal peptide region corresponding to 24 amino acids, an A3 acidic subunit region corresponding to 320 amino acids followed by a B4 basic subunit region corresponding to 172 amino acids, and a 3'-terminal nontranslated region of 192 nucleotides, which contained two characteristic AAUAAA sequences that ended 110 nucleotides and 26 nucleotides from a 3'-terminal poly(A) segment, respectively. Our results confirm that glycinin is synthesized as precursor polypeptides which undergo post-translational processing to form the nonrandom polypeptide pairs via disulfide bonds. The inferred amino acid sequence of the mature basic subunit, B4, was compared to that of the basic subunit of pea legumin, Leg Beta, which contained 185 amino acids. Using an alignment that permitted a maximum homology of amino acids, it was found that overall 42% of the amino acid positions are identical in both proteins. These results led us to conclude that both storage proteins have a common ancestor.

Paper title : The effect of pH on heat denaturation and gel forming properties of soy proteins.

Doi : https://doi.org/10.1016/s0168-1656(00)00239-x

Abstract : This study is focussed on the influence of pH on the gel forming properties of soy protein isolate and purified glycinin in relation to denaturation and aggregation. At pH 7.6 more fine-stranded gels were formed characterised by low G' values, and a smooth, slightly turbid appearance, whereas at pH 3.8 coarse gels were obtained with a high stiffness and a granulated, white appearance. Low G' values, as found at pH 7.6, correlate with a high solubility of glycinin and soy protein isolate (ca. 50%) after heating at low protein concentration. At pH 3.8 all protein precipitated upon heating, which correlates with relatively high G' values. The role of beta-conglycinin during gelation of SPI seems to be minor at pH 7.6, which is indicated by the fact that, in contrast to pH 3.8, notable gel formation did not start upon heat denaturation of beta-conglycinin. Furthermore, the mechanism of gel formation seems to be affected by pH, because at pH 7.6, in contrast to pH 3.8, the disulphide bridge between the acidic and the basic polypeptide of glycinin is broken upon heating.

Paper title : Antibacterial Actions of Glycinin Basic Peptide against Escherichia coli.

Doi : https://doi.org/10.1021/acs.jafc.7b02295

Abstract : Glycinin basic peptide (GBP) is an antibacterial ingredient that occurs naturally in the basic parts of soybean glycinin. The antibacterial actions of GBP against Escherichia coli ATCC 8739 were investigated in this study. The minimum inhibitory concentration of GBP against E. coli was 200 μg/mL. The exposure of E. coli cells to GBP induced significant cell damage and inactivated intracellular esterases (stressed and dead cells, 70.9% ± 0.04 for 200 μg/mL of GBP and 91.9% ± 0.06 for 400 μg/mL of GBP), as determined through dual staining in flow cytometry. GBP resulted in the exposure of phosphatidylserine in E. coli cells. The analyses of flow cytometry-manifested GBP treatment led to the shrinkage of the cell surface and the complication of cell granularity. The observations in transmission electron microscopy demonstrated that 400 μg/mL of GBP severely disrupted the membrane integrity, resulting in ruptures or pores in the membrane, outflows of intracellular contents, or aggregation of the cytoplasm. Release of alkaline phosphatase, lipopolysaccharide, and reducing sugar further verified that the membrane damage was due to GBP. In addition, GBP treatment changed the helicity and base staking of DNA, as determined by circular dichroism spectroscopy. These results showed that GBP had strong antibacterial activity against E. coli via membrane damage and DNA perturbation. Additionally, GBP exhibited no cytotoxicity on the viability of human embryonic kidney cells. Thus, GBP may be a promising candidate as a natural antibacterial agent.

Paper title : Conservation and divergence on plant seed 11S globulins based on crystal structures.

Doi : https://doi.org/10.1016/j.bbapap.2010.02.016

Abstract : The crystal structures of two pro-11S globulins namely: rapeseed procruciferin and pea prolegumin are presented here. We have extensively compared them with the other known structures of plant seed 11S and 7S globulins. In general, the disordered regions in the crystal structures among the 11S globulins correspond to their five variable regions. Variable region III of procruciferin is relatively short and is in a loop conformation. This region is highly disordered in other pro-11S globulin crystals. Local helical and strand variations also occur across the group despite general structure conservation. We showed how these variations may alter specific physicochemical, functional and physiological properties. Aliphatic hydrophobic residues on the molecular surface correlate well with Tm values of the globulins. We also considered other structural features that were reported to influence thermal stability but no definite conclusion was drawn since each factor has additive or subtractive effect. Comparison between proA3B4 and mature A3B4 revealed an increase in r.m.s.d. values near variable regions II and IV. Both regions are on the IE face. Secondary structure based alignment of 11S and 7S globulins revealed 16 identical residues. Based on proA3B4 sequence, Pro60, Gly128, Phe163, Phe208, Leu213, Leu227, Ile237, Pro382, Val404, Pro425 and Val 466 are involved in trimer formation and stabilization. Gly28, Gly74, Asp135, Gly349 and Gly397 are involved in correct globular folding.

Paper title : Methodology for identification of pore forming antimicrobial peptides from soy protein subunits β-conglycinin and glycinin.

Doi : https://doi.org/10.1016/j.peptides.2016.09.004

Abstract : Antimicrobial peptides (AMPs) inactivate microbial cells through pore formation in cell membrane. Because of their different mode of action compared to antibiotics, AMPs can be effectively used to combat drug resistant bacteria in human health. AMPs can also be used to replace antibiotics in animal feed and immobilized on food packaging films. In this research, we developed a methodology based on mechanistic evaluation of peptide-lipid bilayer interaction to identify AMPs from soy protein. Production of AMPs from soy protein is an attractive, cost-saving alternative for commercial consideration, because soy protein is an abundant and common protein resource. This methodology is also applicable for identification of AMPs from any protein. Initial screening of peptide segments from soy glycinin (11S) and soy β-conglycinin (7S) subunits was based on their hydrophobicity, hydrophobic moment and net charge. Delicate balance between hydrophilic and hydrophobic interactions is necessary for pore formation. High hydrophobicity decreases the peptide solubility in aqueous phase whereas high hydrophilicity limits binding of the peptide to the bilayer. Out of several candidates chosen from the initial screening, two peptides satisfied the criteria for antimicrobial activity, viz. (i) lipid-peptide binding in surface state and (ii) pore formation in transmembrane state of the aggregate. This method of identification of antimicrobial activity via molecular dynamics simulation was shown to be robust in that it is insensitive to the number of peptides employed in the simulation, initial peptide structure and force field. Their antimicrobial activity against Listeria monocytogenes and Escherichia coli was further confirmed by spot-on-lawn test.