Citation: Jian-Hua Ren, Shun-Tang Guo. In vitro digestibility of soybean β-conglycinin hydrolysates[J]. Chinese Chemical Letters, ;2013, 24(07): 585-587. shu

In vitro digestibility of soybean β-conglycinin hydrolysates

Jian-Hua Ren ,
Shun-Tang Guo ^,

1.
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China

Corresponding author: Shun-Tang Guo,
Received Date: 5 February 2013
Available Online: 28 March 2013

The in vitro digestibility of alcalase enzymatic hydrolysates of β-conglycinin was studied. The results showed that the zeta potentials of β-conglycinin hydrolysates decreased and their electronegativity increased when digested with pepsin and trypsin. Furthermore, the content of peptides with molecular weight from 10 kDa to 20 kDa remained stable, while those with higher molecular weight (>20 kDa) decreased, and those with lower molecular weight (<10 kDa) increased. The proportion of highly hydrophobic peptides decreased in the process of the in vitro digestion, but no significant change in the surface hydrophobicity indices of digestion products was observed (P < 0.05). These results indicate that the β-conglycinin hydrolysates were degraded through in vitro digestion, but the degree of degradation was relatively low. Peptides with molecular weight from 10 kDa to 20 kDa in the β-conglycinin hydrolysates resisted the digestion by pepsin and trypsin and they remained stable during the in vitro digestion processes.
- β-Conglycinin hydrolysates,
- In vitro digestion,
- Digestibility
1. [1]
  [1] H.M. Chen, K. Muramoto, F. Yamauchi, Structural analysis of antioxidative peptides from soybean β-conglycinin, J. Agric. Food Chem. 43 (1995) 574-578.
2. [2]
  [2] C. Martinez-Villaluenga, V.P. Dia, M. Berhow, N.A. Bringe, E. Gonzalez de Mejia, Protein hydrolysates from beta-conglycinin enriched soybean genotypes inhibit lipid accumulation and inflammation in vitro, Mol. Nutr. Food Res. 53 (2009) 1007-1018.
3. [3]
  [3] T. Tsuruki, K. Kishi, M. Takahashi, M. Tanaka, T. Matsukawa, M. Yoshikawa, Soymetide, an immunostimulating peptide derived from soybean β-conglycinin, is an fMLP agonist, FEBS Lett. 540 (2003) 206-210.
4. [4]
  [4] B.C. Yang, X.M. Zhang, X.L. Bao, et al., Glycopeptide derived from soybean bconglycinin inhibits the adhesion of Escherichia coli and Salmonella to human intestinal cells, Food Res. Int. 41 (2008) 594-599.
5. [5]
  [5] B.C. Yang, Y. Lv, Y. Chen, et al., Inhibitory action of soybean β-conglycinin hydrolysates on Salmonella typhimurium translocation in Caco-2 epithelial cell monolayers, J. Agric. Food Chem. 56 (2008) 7522-7527.
6. [6]
  [6] S. Roufik, S.F. Gauthier, S.L. Turgeon, In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin, Int. Dairy J. 16 (2006) 294-302.
7. [7]
  [7] M.I. Mahmoud, W.T. Malone, C.T. Cordle, Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties, J. Food Sci. 57 (1992) 1223-1229.
1. [1]
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