Determination of Amino acid Profile and Some Characteristics of Collagen Extracted from Skin and Bone of Luciobarbus esocinus (Heckel, 1843)

Mustafa Göçer, Y. Yanar, M. Aydın
{"title":"Determination of Amino acid Profile and Some Characteristics of Collagen Extracted from Skin and Bone of Luciobarbus esocinus (Heckel, 1843)","authors":"Mustafa Göçer, Y. Yanar, M. Aydın","doi":"10.17216/limnofish.1213720","DOIUrl":null,"url":null,"abstract":"Acid soluble collagens (ASC) from bone (ASC-B) and skin (ASC-S) of mangar (Luciobarbus esocinus (Heckel, 1843) were extracted, characterized, and their amino acid profiles were determined. To best of our knowledge, the current study is the first research that used this species as a source of collagen. Both ASC-S and ASC-B from mangar skin and bone contained glycine as the major amino acid and high amounts of proline, hydroxyproline, alanine, and glutamic acid. On the basis of dry weight, yields of ASC-S and ASC-B were 9.38 and 3.71%, respectively. Furthermore, fourier transform infrared spectroscopy proved that both collagens were integrated and native. Additionally, the results of XRD demonstrated that both of the collagens reserved their helical structures. The screened collagens had prominent absorptions at 230 nm by UV-Vis spectra. Additionally, the SEM studies have shown that both ACS-S and ASC-B have porous and fibrous nature. According to the UV–Vis and FTIR results, extracted collagens were characterized as type I collagen based on their amino acid composition. According to the obtained results, the collagen isolated from mangar can potentially be an alternative source of vertebrate collagens for use in the diet and other industries such as medical and pharmaceutical industries.","PeriodicalId":31031,"journal":{"name":"Journal of Limnology and Freshwater Fisheries Research","volume":"1 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2023-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Limnology and Freshwater Fisheries Research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17216/limnofish.1213720","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1

Abstract

Acid soluble collagens (ASC) from bone (ASC-B) and skin (ASC-S) of mangar (Luciobarbus esocinus (Heckel, 1843) were extracted, characterized, and their amino acid profiles were determined. To best of our knowledge, the current study is the first research that used this species as a source of collagen. Both ASC-S and ASC-B from mangar skin and bone contained glycine as the major amino acid and high amounts of proline, hydroxyproline, alanine, and glutamic acid. On the basis of dry weight, yields of ASC-S and ASC-B were 9.38 and 3.71%, respectively. Furthermore, fourier transform infrared spectroscopy proved that both collagens were integrated and native. Additionally, the results of XRD demonstrated that both of the collagens reserved their helical structures. The screened collagens had prominent absorptions at 230 nm by UV-Vis spectra. Additionally, the SEM studies have shown that both ACS-S and ASC-B have porous and fibrous nature. According to the UV–Vis and FTIR results, extracted collagens were characterized as type I collagen based on their amino acid composition. According to the obtained results, the collagen isolated from mangar can potentially be an alternative source of vertebrate collagens for use in the diet and other industries such as medical and pharmaceutical industries.
esocinus Luciobarbus esocinus (Heckel, 1843)皮肤和骨骼中胶原蛋白氨基酸谱和某些特性的测定
本文对锰(Luciobarbus esocinus, Heckel, 1843)骨(ASC- b)和皮(ASC- s)的酸溶性胶原(ASC)进行了提取、表征和氨基酸谱分析。据我们所知,目前的研究是第一个使用这种物种作为胶原蛋白来源的研究。从锰皮和骨中提取的ASC-S和ASC-B均以甘氨酸为主要氨基酸,并含有大量脯氨酸、羟脯氨酸、丙氨酸和谷氨酸。按干重计算,ASC-S和ASC-B的产量分别为9.38%和3.71%。此外,傅里叶变换红外光谱证明了两种胶原蛋白的完整性和天然性。此外,XRD结果表明,两种胶原都保留了其螺旋结构。所筛选的胶原蛋白在230 nm处有明显的紫外-可见吸收。此外,SEM研究表明,ACS-S和ASC-B均具有多孔性和纤维性。根据UV-Vis和FTIR结果,提取的胶原蛋白根据其氨基酸组成特征为I型胶原蛋白。根据获得的结果,从锰中分离的胶原蛋白可能是脊椎动物胶原蛋白的替代来源,可用于饮食和其他行业,如医疗和制药行业。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
6
审稿时长
8 weeks
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信