{"title":"通过 Alcalase® 水解,鱼 I 型胶原蛋白肽中的活性羧基和游离α-氨基基团增加,从而表现出更高的抗菌和抗氧化活性","authors":"Sülhattin Yaşar, Hülya Şen Arslan, Kubra Akgul","doi":"10.1515/ijfe-2023-0303","DOIUrl":null,"url":null,"abstract":"\n This study aimed to generate low molecular weight peptides (LMWP) from fish collagen type I hydrolysed by increasing activity of Alcalase® from 0.0 to 12.0 (AU-A per 100 g) at 55 °C and 7.4 of pH for 3 h 40 min. The results showed that all enzyme activity levels caused 34–55 % reductions in protein recovery, 1.0–3.0 folds’ increase in free α-amino groups and 1.7–3.2 folds’ increase in carboxyl groups. Degree of hydrolysis ranged from 20 to 30 % with increasing enzyme activity. The number average molecular weight significantly reduced from 3200 g/mol in 0.0 AU-A per 100 g enzyme activity to 1151, 1398, 1175, 1040 and 1246 g/mol in 2.4, 4.8, 7.2, 9.6 and 12.0 AU-A per 100 g enzyme activities, respectively. Depending upon enzyme activity level, the produced LMWP with reactive carboxyl and amino end-groups exhibited 2.5- to 4.0-fold increases in antioxidant capacity and 1.0–3.5 log cfu/ml inhibition of four pathogen bacteria. Highest inhibition of 2.5 log cfu/ml in Escherichia coli was obtained from 2.4 AU-A per 100 g enzyme activity and 3.5 log cfu/ml in Listeria monocytogenes from 9.6 and 12.0 AU-A per 100 g enzyme activity levels. Infrared spectroscopy clearly identified reactive end-groups and showed remarkably differences in molar absorptivity of various molecular regions between non-enzyme and enzyme treated collagen type I molecule. A 9.6 and 12.0 AU-A per 100 g enzyme activity levels were found optimally effective to generate LMWP. In conclusion, LMWP exhibited high antioxidant and antibacterial activity due to increased functional reactive end-groups, and these bio-active peptides may have greater potentialities in various food and pharmaceutical applications.","PeriodicalId":13976,"journal":{"name":"International Journal of Food Engineering","volume":null,"pages":null},"PeriodicalIF":1.6000,"publicationDate":"2024-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Increased reactive carboxyl and free alfa-amino groups from fish type I collagen peptides by Alcalase® hydrolysis exhibit higher antibacterial and antioxidant activities\",\"authors\":\"Sülhattin Yaşar, Hülya Şen Arslan, Kubra Akgul\",\"doi\":\"10.1515/ijfe-2023-0303\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"\\n This study aimed to generate low molecular weight peptides (LMWP) from fish collagen type I hydrolysed by increasing activity of Alcalase® from 0.0 to 12.0 (AU-A per 100 g) at 55 °C and 7.4 of pH for 3 h 40 min. The results showed that all enzyme activity levels caused 34–55 % reductions in protein recovery, 1.0–3.0 folds’ increase in free α-amino groups and 1.7–3.2 folds’ increase in carboxyl groups. Degree of hydrolysis ranged from 20 to 30 % with increasing enzyme activity. The number average molecular weight significantly reduced from 3200 g/mol in 0.0 AU-A per 100 g enzyme activity to 1151, 1398, 1175, 1040 and 1246 g/mol in 2.4, 4.8, 7.2, 9.6 and 12.0 AU-A per 100 g enzyme activities, respectively. Depending upon enzyme activity level, the produced LMWP with reactive carboxyl and amino end-groups exhibited 2.5- to 4.0-fold increases in antioxidant capacity and 1.0–3.5 log cfu/ml inhibition of four pathogen bacteria. Highest inhibition of 2.5 log cfu/ml in Escherichia coli was obtained from 2.4 AU-A per 100 g enzyme activity and 3.5 log cfu/ml in Listeria monocytogenes from 9.6 and 12.0 AU-A per 100 g enzyme activity levels. Infrared spectroscopy clearly identified reactive end-groups and showed remarkably differences in molar absorptivity of various molecular regions between non-enzyme and enzyme treated collagen type I molecule. A 9.6 and 12.0 AU-A per 100 g enzyme activity levels were found optimally effective to generate LMWP. In conclusion, LMWP exhibited high antioxidant and antibacterial activity due to increased functional reactive end-groups, and these bio-active peptides may have greater potentialities in various food and pharmaceutical applications.\",\"PeriodicalId\":13976,\"journal\":{\"name\":\"International Journal of Food Engineering\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.6000,\"publicationDate\":\"2024-03-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Food Engineering\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1515/ijfe-2023-0303\",\"RegionNum\":4,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Food Engineering","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1515/ijfe-2023-0303","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Increased reactive carboxyl and free alfa-amino groups from fish type I collagen peptides by Alcalase® hydrolysis exhibit higher antibacterial and antioxidant activities
This study aimed to generate low molecular weight peptides (LMWP) from fish collagen type I hydrolysed by increasing activity of Alcalase® from 0.0 to 12.0 (AU-A per 100 g) at 55 °C and 7.4 of pH for 3 h 40 min. The results showed that all enzyme activity levels caused 34–55 % reductions in protein recovery, 1.0–3.0 folds’ increase in free α-amino groups and 1.7–3.2 folds’ increase in carboxyl groups. Degree of hydrolysis ranged from 20 to 30 % with increasing enzyme activity. The number average molecular weight significantly reduced from 3200 g/mol in 0.0 AU-A per 100 g enzyme activity to 1151, 1398, 1175, 1040 and 1246 g/mol in 2.4, 4.8, 7.2, 9.6 and 12.0 AU-A per 100 g enzyme activities, respectively. Depending upon enzyme activity level, the produced LMWP with reactive carboxyl and amino end-groups exhibited 2.5- to 4.0-fold increases in antioxidant capacity and 1.0–3.5 log cfu/ml inhibition of four pathogen bacteria. Highest inhibition of 2.5 log cfu/ml in Escherichia coli was obtained from 2.4 AU-A per 100 g enzyme activity and 3.5 log cfu/ml in Listeria monocytogenes from 9.6 and 12.0 AU-A per 100 g enzyme activity levels. Infrared spectroscopy clearly identified reactive end-groups and showed remarkably differences in molar absorptivity of various molecular regions between non-enzyme and enzyme treated collagen type I molecule. A 9.6 and 12.0 AU-A per 100 g enzyme activity levels were found optimally effective to generate LMWP. In conclusion, LMWP exhibited high antioxidant and antibacterial activity due to increased functional reactive end-groups, and these bio-active peptides may have greater potentialities in various food and pharmaceutical applications.
期刊介绍:
International Journal of Food Engineering is devoted to engineering disciplines related to processing foods. The areas of interest include heat, mass transfer and fluid flow in food processing; food microstructure development and characterization; application of artificial intelligence in food engineering research and in industry; food biotechnology; and mathematical modeling and software development for food processing purposes. Authors and editors come from top engineering programs around the world: the U.S., Canada, the U.K., and Western Europe, but also South America, Asia, Africa, and the Middle East.