{"title":"Production of Hydrolyzed Collagen from Common Carp Cyprinus carpio L. Scales by Synergistic Enzyme Systems","authors":"Hala H. M. Al-Abadi, Wasan K. A. AI-Temimi","doi":"10.37077/25200860.2022.35.1.08","DOIUrl":null,"url":null,"abstract":"Fish skin, bones and scales are a good source of collagen, for the sake of exploitation these fish wastes of high commercial worth and convert them into food, therapeutic and pharmaceutical products. Therefore, the study included extracting collagen with acetic acid at a concentration 0.5 M and pepsin enzyme 0.1% from fish Cyprinus carpio scales and then producing hydrolyzed collagen protein. Chemical content of the scales was estimated from the percentage of moisture, protein, fat and ash, as it was found (55.36, 35.85, 2.47 and 5.99) %, respectively. The metallic elements represented by (Ca, P, Fe and Zn), they reached (153430, 1887.5, 71.455 and 48.045) µg.g-1. The collagen yield by the two methods mentioned above was 16.40% and 5.30%, respectively. Diagnosis of collagen extracted with acid using FT-IR technique and determination of the active groups in it, the presence of amides A, B, I, II and III was observed at frequencies 3413.39, 2924.52, 1653.66, 1548.56 and 1240 cm-1, respectively. Hydrolysed collagen was prepared using Collagenase enzyme followed by Pepsin enzyme, the highest degree of hydrolysis reached 43.56% after four hours. The electrophoresis of collagen extracted with acid and enzyme was carried out, as three bundles of collagen α1, α2 and β were obtained with weights (126, 100 and 180) KD, respectively.","PeriodicalId":8700,"journal":{"name":"Basrah Journal of Agricultural Sciences","volume":"27 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2022-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Basrah Journal of Agricultural Sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.37077/25200860.2022.35.1.08","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Agricultural and Biological Sciences","Score":null,"Total":0}
引用次数: 1
Abstract
Fish skin, bones and scales are a good source of collagen, for the sake of exploitation these fish wastes of high commercial worth and convert them into food, therapeutic and pharmaceutical products. Therefore, the study included extracting collagen with acetic acid at a concentration 0.5 M and pepsin enzyme 0.1% from fish Cyprinus carpio scales and then producing hydrolyzed collagen protein. Chemical content of the scales was estimated from the percentage of moisture, protein, fat and ash, as it was found (55.36, 35.85, 2.47 and 5.99) %, respectively. The metallic elements represented by (Ca, P, Fe and Zn), they reached (153430, 1887.5, 71.455 and 48.045) µg.g-1. The collagen yield by the two methods mentioned above was 16.40% and 5.30%, respectively. Diagnosis of collagen extracted with acid using FT-IR technique and determination of the active groups in it, the presence of amides A, B, I, II and III was observed at frequencies 3413.39, 2924.52, 1653.66, 1548.56 and 1240 cm-1, respectively. Hydrolysed collagen was prepared using Collagenase enzyme followed by Pepsin enzyme, the highest degree of hydrolysis reached 43.56% after four hours. The electrophoresis of collagen extracted with acid and enzyme was carried out, as three bundles of collagen α1, α2 and β were obtained with weights (126, 100 and 180) KD, respectively.