Peptide name : Glycinin G2

Source/Organism : Soyabean (Soybean)

Linear/Cyclic : Linear

Chirality : Not found

Peptide length: 485

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 : 54390.1371 Dalton

Aliphatic index : 0.72

Instability index : 60.6031

Hydrophobicity (GRAVY) : -0.654

Isoelectric point : 5.462

Charge (pH 7) : -7.1561

Aromaticity : 0.076

Molar extinction coefficient (cysteine, cystine): (38390, 39015)

Hydrophobic/hydrophilic ratio : 0.87596899

hydrophobic moment : -0.161

Missing amino acid : None

Most occurring amino acid : Q

Most occurring amino acid frequency : 51

Least occurring amino acid : n

Least occurring amino acid frequency : 1

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)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccc(O)cc1)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](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)CNC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CS)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)C(C)C)[C@@H](C)O)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(=O)O)C(=O)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1 : 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

2 : Schmutz J, et al. Genome sequence of the palaeopolyploid soybean. Nature. 2010; 463:178-83. doi: 10.1038/nature08670

3 : 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

4 : 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

5 : Kitamura Y, et al. The complete nucleotide sequence of soybean glycinin A2B1a gene spanning to another glycinin gene A1aB1b. Nucleic Acids Res. 1990; 18:4245. doi: 10.1093/nar/18.14.4245

6 : 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

7 : 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

8 : 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

9 : 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

10 : 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

11 : 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

12 : 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

13 : 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

14 : Staswick PE, et al. The amino acid sequence of the A2B1a subunit of glycinin. J Biol Chem. 1984; 259:13424-30.

15 : Thanh VH, et al. The glycinin Gy2 gene from soybean. Nucleic Acids Res. 1989; 17:4387. doi: 10.1093/nar/17.11.4387

16 : 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

17 : 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

18 : 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

19 : 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

20 : Asakura T, et al. Global gene expression profiles in developing soybean seeds. Plant Physiol Biochem. 2012; 52:147-53. doi: 10.1016/j.plaphy.2011.12.007

21 : Fukazawa C, et al. Complete nucleotide sequence of the gene encoding a glycinin A2B1a subunit precursor of soybean. Nucleic Acids Res. 1987; 15:8117. doi: 10.1093/nar/15.19.8117

22 : Staswick PE, et al. Identification of the cystines which link the acidic and basic components of the glycinin subunits. J Biol Chem. 1984; 259:13431-5.

23 : 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

24 : Marco YA, et al. Cloning and structural analysis of DNA encoding an A2B1a subunit of glycinin. J Biol Chem. 1984; 259:13436-41.

25 : Shutov AD, et al. Limited proteolysis of beta-conglycinin and glycinin, the 7S and 11S storage globulins from soybean [Glycine max (L.) Merr.]. Structural and evolutionary implications. Eur J Biochem. 1996; 241:221-8. doi: 10.1111/j.1432-1033.1996.0221t.x

26 : 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

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 : Genome sequence of the palaeopolyploid soybean.

Doi : https://doi.org/10.1038/nature08670

Abstract : Soybean (Glycine max) is one of the most important crop plants for seed protein and oil content, and for its capacity to fix atmospheric nitrogen through symbioses with soil-borne microorganisms. We sequenced the 1.1-gigabase genome by a whole-genome shotgun approach and integrated it with physical and high-density genetic maps to create a chromosome-scale draft sequence assembly. We predict 46,430 protein-coding genes, 70% more than Arabidopsis and similar to the poplar genome which, like soybean, is an ancient polyploid (palaeopolyploid). About 78% of the predicted genes occur in chromosome ends, which comprise less than one-half of the genome but account for nearly all of the genetic recombination. Genome duplications occurred at approximately 59 and 13 million years ago, resulting in a highly duplicated genome with nearly 75% of the genes present in multiple copies. The two duplication events were followed by gene diversification and loss, and numerous chromosome rearrangements. An accurate soybean genome sequence will facilitate the identification of the genetic basis of many soybean traits, and accelerate the creation of improved soybean varieties.

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 : The complete nucleotide sequence of soybean glycinin A2B1a gene spanning to another glycinin gene A1aB1b.

Doi : https://doi.org/10.1093/nar/18.14.4245

Abstract : Not available

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 : 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 : The amino acid sequence of the A2B1a subunit of glycinin.

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

Abstract : The amino acid sequences of the acidic and basic components of the A2B1a subunit of glycinin, the major seed reserve protein of the soybean (Glycine max L. Merr.), were determined. They contain 278 and 180 amino acids, respectively, and have molecular weights of 31,600 +/- 100 and 19,900 +/- 100. The molecular weight of the acidic component is considerably less than that estimated by sodium dodecyl sulfate-gel electrophoresis (37,000). Sequence heterogeneity was detected at several positions scattered throughout the primary structures of both components, indicating that the preparation sequenced was composed of several nearly identical polypeptides. These data, in conjunction with a recently determined nucleotide sequence of the 3'-terminal two-thirds of the analogous glycinin subunit gene, illustrate the complexity of the gene family responsible for synthesis of glycinin subunits.

Paper title : The glycinin Gy2 gene from soybean.

Doi : https://doi.org/10.1093/nar/17.11.4387

Abstract : Not available

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 : Global gene expression profiles in developing soybean seeds.

Doi : https://doi.org/10.1016/j.plaphy.2011.12.007

Abstract : The gene expression profiles in soybean (Glycine max L.) seeds at 4 stages of development, namely, pod, 2-mm bean, 5-mm bean, and full-size bean, were examined by DNA microarray analysis. The total genes of each sample were classified into 4 clusters based on stage of development. Gene expression was strictly controlled by seed size, which coincides with the development stage. First, stage specific gene expression was examined. Many transcription factors were expressed in pod, 2-mm bean and 5-mm bean. In contrast, storage proteins were mainly expressed in full-size bean. Next, we extracted the genes that are differentially expressed genes (DEGs) that were extracted using the Rank products method of the Bioconductor software package. These DEGs were sorted into 8 groups using the hclust function according to gene expression patterns. Three of the groups across which the expression levels progressively increased included 100 genes, while 3 groups across which the levels decreased contained 47 genes. Storage proteins, seed-maturation proteins, some protease inhibitors, and the allergen Gly m Bd 28K were classified into the former groups. Lipoxygenase (LOX) family members were present in both the groups, indicating the multi-functionality with different expression patterns.

Paper title : Complete nucleotide sequence of the gene encoding a glycinin A2B1a subunit precursor of soybean.

Doi : https://doi.org/10.1093/nar/15.19.8117

Abstract : Not available

Paper title : Identification of the cystines which link the acidic and basic components of the glycinin subunits.

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

Abstract : The half-cystine residues involved in linking the acidic and basic polypeptides were determined for several glycinin subunits. The cystines were localized with specific cyanogen bromide fragments either by comparing the electrophoretic mobility of nonreduced and reduced fragments, or by co-purifying and then determining the NH2-terminal sequence of the covalently linked fragments. Residues involved in the disulfides were further identified by labeling them with [3H] iodoacetic acid. Only 1 cystine was found to be involved in linking the acidic and basic components of each subunit, and they were in analogous positions in each of the subunits studied. Potential sites for intrapolypeptide cystines were also identified.

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 : Cloning and structural analysis of DNA encoding an A2B1a subunit of glycinin.

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

Abstract : The partial DNA sequence of a glycinin gene in a genomic clone and a homologous cDNA clone were determined. They have nearly identical nucleotide sequences and encode the basic polypeptide and part of the acidic polypeptide for an A2B1a glycinin subunit. The protein primary structure deduced from the DNA sequence is in close agreement with the amino acid sequence of the subunit determined chemically and confirms assignment of part of the amino acid sequence in the basic component where we were able to establish an overlap using conventional approaches. The coding part of the basic subunit is interrupted by a 625-base pair A + T-rich intron whose boundaries correlate with the established consensus sequences for the exon-intron junctions. Comparison of the nucleotide sequence of the basic subunit of pea legumin gene with that of the gene for A2B1a subunit reveals 70% homology in coding regions, although there is considerably less in the 3'-flanking regions.

Paper title : Limited proteolysis of beta-conglycinin and glycinin, the 7S and 11S storage globulins from soybean [Glycine max (L.) Merr.]. Structural and evolutionary implications.

Doi : https://doi.org/10.1111/j.1432-1033.1996.0221t.x

Abstract : The G2 (A2B1a) glycinin subunit from soybean (Glycine max L. Merr.) was purified and renatured to the homohexameric holoprotein. This protein along with purified beta-conglycinin were subjected to limited proteolysis by trypsin. The generated polypeptide fragments were separated via SDS/PAGE and the amino acid sequence of the N-terminals was determined. Four cleavage points were detected in the alpha-chain A2 of glycinin as well as in the alpha'-chain of beta-conglycinin. From the known three-dimensional structure of 7S globulin and the hypothetical model of 7S globulin-like 11S globulin structure, it was possible to draw the conclusion that two distinct types of susceptible sites for proteolytic cleavage are characteristic of the subunits of both globulins. The first includes the sequences linking N- and C-terminal domains of both globulins and the sequence of N-terminal extensions of 70-kDa subunits from the vicilin-like 7S globulins. The second type includes the loop between beta-strands E and F of the N-terminal domain of 11S globulins and of the C-terminal domain of 7S globulins. A statistically significant similarity was found between the N-terminal extension of the alpha'-chain of beta-conglycinin and the interdomain linker regions of soybean glycinin and pea legumin. It is proposed that the three sequence regions which form the first type of susceptible sites are of similar structural function and might have evolved from the N-terminal segment of a putative single-domain ancestor.

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.