Structural properties and antioxidant activities of soybean protein hydrolysates produced by Lactobacillus delbrueckii subsp. bulgaricus cell envelope proteinase

被引:34
作者
Zhang, Xiaoying [1 ]
Huang, Yuyang [3 ]
Ma, Ruxin [1 ]
Tang, Yuqing [1 ]
Li, Yang [1 ]
Zhang, Shuang [1 ,2 ]
机构
[1] Northeast Agr Univ, Coll Food Sci, Harbin 150030, Peoples R China
[2] Northeast Agr Univ, Key Lab Dairy Sci, Minist Educ, Harbin 150030, Peoples R China
[3] Harbin Univ Commerce, Coll Food Engn, Harbin 150006, Peoples R China
关键词
Soybean protein isolate; Lactobacillus delbrueckii subsp; bulgaricus; Cell envelope proteinase; Structural properties; Antioxidant activity; LC-MS; MS; FUNCTIONAL-PROPERTIES; ENZYMATIC-HYDROLYSIS; PEPTIDES; PEA;
D O I
10.1016/j.foodchem.2023.135392
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
In this work, we investigated the structural and biological properties of soybean protein isolate (SPI) after 0-8 h hydrolyzation with cell envelope proteinase (CEP) extracted from Lactobacillus delbrueckii subsp. bulgaricus. CEP hydrolysis increased the beta-sheet and red-shifted the fluorescence peak, while decreasing the alpha-helix, indicating the unfolding of soybean proteins. Increased surface hydrophobicity and fluorescence of the soybean protein hydrolysates were correlated with the increased hydrophobic amino acid (from 209.67 to 217.6 mg/100 g). CEP tended to hydrolyze the N-and C-terminal regions of sequences dominated by Gly and Leu, which enhanced the antioxidant activity of the SPHs (lowest IC50s value of ABTS center dot+ and hydroxyl radical scavenging activity were 0.324 +/- 0.006 mg/mL and 0.365 +/- 0.001 mg/mL after 4 h hydrolysis). Comparison with the database of bioactive peptides suggested various potential biological activities, including antioxidant activity, angiotensin-converting enzyme inhibitory activity and dipeptidyl peptidase-IV inhibitory activity. The study findings have theoretical significance for the development of CEP hydrolysis and novel bioactive soybean peptides.
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页数:9
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