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鲭鱼蛋白质中抗氧化肽的纯化与鉴定

Purification and identification of antioxidative peptides from mackerel () protein.

作者信息

Wang Xueqin, Yu Huahua, Xing Ronge, Chen Xiaolin, Li Rongfeng, Li Kecheng, Liu Song, Li Pengcheng

机构信息

CAS Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences No. 7, Nanhai Road Qingdao 266071 China

Laboratory for Marine Drugs and Bioproducts, Qingdao National Laboratory for Marine Science and Technology No. 1, Wenhai Road Qingdao 266237 China.

出版信息

RSC Adv. 2018 Jun 5;8(37):20488-20498. doi: 10.1039/c8ra03350a.

DOI:10.1039/c8ra03350a
PMID:35542336
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9080898/
Abstract

This study reports the preparation, purification and identification of an antioxidative peptide from mackerel () protein. Neutrase was chosen as the optimum protease, with the highest cellular antioxidant activity of 53.65%. The optimal hydrolysate conditions for mackerel protein hydrolysates (MPH) according to response surface methodology were an enzyme concentration of 1203.2 U g, extraction time of 4.53 h, pH of 7.26, water/material ratio of 5.22 v/w and extraction temperature of 43.72 °C. MPH was separated using ultrafiltration membranes, and the fraction MPH-III with molecular weight below 3500 Da showed the highest cellular antioxidant activity. Five fractions were separated from MPH-III on a Sephadex G-25 column, and MPH-III-2, exhibiting the highest cellular antioxidant activity, was further separated with an XBridge® peptide BEH C18 column. The MPH-III-2-6 separated from RP-HPLC was further analysed by Thermo Scientific Q Exactive mass spectrometer, and the heptapeptide LDIQKEV (843.5 Da) and the octapeptide TAAIVNTA (759.4 Da) were identified. The results of this study offer a promising alternative to produce natural antioxidative peptides from fish protein hydrolysate, which may be utilized as functional ingredients in food systems.

摘要

本研究报道了一种从鲭鱼蛋白中制备、纯化和鉴定抗氧化肽的方法。选择中性蛋白酶作为最佳蛋白酶，其细胞抗氧化活性最高可达53.65%。根据响应面法，鲭鱼蛋白水解物（MPH）的最佳水解条件为：酶浓度1203.2 U/g、提取时间4.53 h、pH值7.26、水/物料比5.22 v/w、提取温度43.72℃。采用超滤膜对MPH进行分离，分子量低于3500 Da的MPH-III组分显示出最高的细胞抗氧化活性。在Sephadex G-25柱上从MPH-III中分离出5个组分，其中细胞抗氧化活性最高的MPH-III-2进一步用XBridge®肽BEH C18柱进行分离。采用Thermo Scientific Q Exactive质谱仪对从反相高效液相色谱（RP-HPLC）中分离得到的MPH-III-2-6进行进一步分析，鉴定出七肽LDIQKEV（843.5 Da）和八肽TAAIVNTA（759.4 Da）。本研究结果为从鱼蛋白水解物中生产天然抗氧化肽提供了一种有前景的替代方法，这些抗氧化肽可作为食品体系中的功能成分加以利用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/8461b2bd73b4/c8ra03350a-f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/cb33eba0264c/c8ra03350a-f1.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/20c18d4f60a1/c8ra03350a-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/1d5e271e4b8b/c8ra03350a-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/df290d825754/c8ra03350a-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/0e6af44e5823/c8ra03350a-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/1cc5c8275c22/c8ra03350a-f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/8461b2bd73b4/c8ra03350a-f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/cb33eba0264c/c8ra03350a-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/c37f67a812cb/c8ra03350a-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/a501f6df9757/c8ra03350a-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/20c18d4f60a1/c8ra03350a-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/1d5e271e4b8b/c8ra03350a-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/df290d825754/c8ra03350a-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/0e6af44e5823/c8ra03350a-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/1cc5c8275c22/c8ra03350a-f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9046/9080898/8461b2bd73b4/c8ra03350a-f9.jpg

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