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从鲣鱼()骨中分离鉴定一种抗氧化胶原蛋白肽。 (注:原文括号处内容缺失)

Isolation and identification of an antioxidant collagen peptide from skipjack tuna () bone.

作者信息

Ding Ding, Du Bowei, Zhang Chao, Zaman Fakhar, Huang Yaqin

机构信息

Beijing Laboratory of Biomedical Materials, Beijing Key Laboratory of Electrochemical Process and Technology for Materials, Beijing University of Chemical Technology Beijing 100029 People's Republic of China

出版信息

RSC Adv. 2019 Aug 28;9(46):27032-27041. doi: 10.1039/c9ra04665h. eCollection 2019 Aug 23.

DOI:10.1039/c9ra04665h
PMID:35528566
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9070664/
Abstract

To date, many researchers have developed active components that are derived from seafood processing for the purposes of healthcare. Here, an antioxidant collagen peptide was obtained from skipjack tuna () bone by using a combination of trypsin and chymotrypsin as the catalyst. The amino acid sequence of the peptide was identified as Ser-Ser-Gly-Pro-Pro-Val-Pro-Gly-Pro-Met-Gly-Pro-Met-Gly-Pro-Arg (SSGPPVPGPMGPMGPR) by liquid chromatography-electrospray ionization quadrupole time-of-flight mass spectrometry (LC-ESI-QTOF-MS) analysis. We found that the as-prepared collagen peptide can efficiently scavenge DPPH radical (IC 3.149 mM), superoxide anion radical (IC 3.803 mM) and ABTS radical (IC 9.489 mM). In addition, it has been found that the methionine (Met) residue in the collagen peptide could provide a precise active site during the scavenging of DPPH radicals by Fourier transform infrared spectroscopy (FTIR) analysis and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry analysis. These results suggest that the peptide can find wide uses in the food, cosmetic and pharmaceutical industries.

摘要

迄今为止,许多研究人员为了医疗保健目的,开发了源自海产品加工的活性成分。在此,通过使用胰蛋白酶和糜蛋白酶的组合作为催化剂,从鲣鱼()骨中获得了一种抗氧化胶原蛋白肽。通过液相色谱 - 电喷雾电离四极杆飞行时间质谱(LC - ESI - QTOF - MS)分析,该肽的氨基酸序列被鉴定为Ser - Ser - Gly - Pro - Pro - Val - Pro - Gly - Pro - Met - Gly - Pro - Met - Gly - Pro - Arg(SSGPPVPGPMGPMGPR)。我们发现所制备的胶原蛋白肽能够有效清除DPPH自由基(IC 3.149 mM)、超氧阴离子自由基(IC 3.803 mM)和ABTS自由基(IC 9.489 mM)。此外,通过傅里叶变换红外光谱(FTIR)分析和基质辅助激光解吸/电离飞行时间(MALDI - TOF)质谱分析发现,胶原蛋白肽中的甲硫氨酸(Met)残基在清除DPPH自由基过程中可提供一个精确的活性位点。这些结果表明,该肽在食品、化妆品和制药行业具有广泛的应用前景。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/ee4ea0571d08/c9ra04665h-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/fe97276d9c5b/c9ra04665h-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/0c2d24a22727/c9ra04665h-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/768f1d926c08/c9ra04665h-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/8429ba34d2a2/c9ra04665h-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/a9e7a6c01e66/c9ra04665h-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/ee4ea0571d08/c9ra04665h-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/fe97276d9c5b/c9ra04665h-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/0c2d24a22727/c9ra04665h-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/768f1d926c08/c9ra04665h-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/8429ba34d2a2/c9ra04665h-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/a9e7a6c01e66/c9ra04665h-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d6a/9070664/ee4ea0571d08/c9ra04665h-f6.jpg

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