Xiaoying Zhang , Yuyang Huang , Ruxin Ma , Yuqing Tang , Yang Li , Shuang Zhang
{"title":"德尔布鲁氏乳杆菌产大豆蛋白水解物的结构特性及抗氧化活性。保加利亚细胞包膜蛋白酶","authors":"Xiaoying Zhang , Yuyang Huang , Ruxin Ma , Yuqing Tang , Yang Li , Shuang Zhang","doi":"10.1016/j.foodchem.2023.135392","DOIUrl":null,"url":null,"abstract":"<div><p>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 <em>Lactobacillus delbrueckii</em> subsp<em>. bulgaricus.</em> CEP hydrolysis increased the β-sheet and red-shifted the fluorescence peak, while decreasing the α-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 IC<sub>50s</sub> value of ABTS<sup>•+</sup> 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.</p></div>","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":null,"pages":null},"PeriodicalIF":8.5000,"publicationDate":"2023-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"6","resultStr":"{\"title\":\"Structural properties and antioxidant activities of soybean protein hydrolysates produced by Lactobacillus delbrueckii subsp. bulgaricus cell envelope proteinase\",\"authors\":\"Xiaoying Zhang , Yuyang Huang , Ruxin Ma , Yuqing Tang , Yang Li , Shuang Zhang\",\"doi\":\"10.1016/j.foodchem.2023.135392\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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 <em>Lactobacillus delbrueckii</em> subsp<em>. bulgaricus.</em> CEP hydrolysis increased the β-sheet and red-shifted the fluorescence peak, while decreasing the α-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 IC<sub>50s</sub> value of ABTS<sup>•+</sup> 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.</p></div>\",\"PeriodicalId\":318,\"journal\":{\"name\":\"Food Chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":8.5000,\"publicationDate\":\"2023-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0308814623000080\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0308814623000080","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Structural properties and antioxidant activities of soybean protein hydrolysates produced by Lactobacillus delbrueckii subsp. bulgaricus cell envelope proteinase
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 β-sheet and red-shifted the fluorescence peak, while decreasing the α-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•+ 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.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.