文献类型：期刊文献

中文题名：油茶饼粕酪氨酸酶抑制肽制备与构效研究

英文题名：Preparation and Structure-Activity Relationship Study of Tyrosinase Inhibitory Peptides from Camellia oleifera Seed Cake

作者：吴苏喜[1] 石思琪[1,2] 方学智[2] 罗凡[2] 胡立松[2] 魏祯倩[2] 杜孟浩[2]

第一作者：吴苏喜

机构：[1]长沙理工大学食品与生物工程学院,长沙410114;[2]中国林业科学研究院亚热带林业研究所,杭州311400

年份：2025

卷号：40

期号：12

起止页码：88-95

中文期刊名：中国粮油学报

外文期刊名：Journal of the Chinese Cereals and Oils Association

收录：;北大核心:【北大核心2023】；

基金：浙江省领雁项目(2023C02045);长沙理工大学研究生科研创新项目(CSLGCX23129);2024年湖南省油茶产业科研示范项目(2024LYCY0009)。

语种：中文

中文关键词：油茶饼粕;油茶籽蛋白肽;抗氧化;酪氨酸酶抑制

外文关键词：Camellia oleifera seed cake;Camellia oleifera seed protein peptide;antioxidant;tyrosinase inhibition

分类号：TS229

摘要：以油茶饼粕蛋白为原料,采用碱性蛋白酶、中性蛋白酶和胃蛋白酶进行酶解处理。通过测定其2,2'-联氮双(3-乙基苯并噻唑啉-6-磺酸)二铵盐(ABTS+·)自由基清除能力、羟基自由基(·OH)清除能力以及酪氨酸酶活性抑制能力,评估酶解产物的抗氧化活性;利用膜分离技术对酶解产物进行分离,并利用高效液相色谱-串联质谱联用技术(LC-MS/MS)鉴定抗氧化活性组分的氨基酸序列。研究结果表明,油茶饼粕蛋白被中性蛋白酶处理4 h的产物经膜分离后,<3 ku组分具有较好的自由基清除能力和酪氨酸酶活性抑制能力,·OH清除率、ABTS+·清除率、酪氨酸酶活性抑制率分别为58.97%、34.44%、53.49%。该组分经氨基酸序列鉴定,结合PeptideRanker平台的生物活性、水溶性、毒性、致敏性预测和分子对接结合能对比得到3个肽段,通过分子对接分析FKL、LRM、MRW 3个肽段与酪氨酸酶之间可能存在非竞争性抑制的关系。
In this study,Camellia oleifera seed cake protein was selected as the raw material and subjected to enzymatic hydrolysis with alkaline protease,neutral protease,and pepsin.The antioxidant activity of the hydrolysates was evaluated by determining the 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)(ABTS+·)radical scavenging capacity,hydroxyl radical(·OH)scavenging capacity,and tyrosinase inhibitory activity.Subsequently,the hydrolysates were fractionated using membrane separation technology,and the amino acid sequences of the antioxidant-active components were identified by liquid chromatography-tandem mass spectrometry(LC-MS/MS).The results indicated that the<3 ku fraction obtained from 4-hour enzymatic hydrolysis with neutral protease exhibited superior radical scavenging capacity and tyrosinase inhibitory activity,with·OH scavenging rate,ABTS+·scavenging rate,and tyrosinase inhibition rate reaching 58.97%,34.44%,and 53.49%,respectively.After amino acid sequence identification,three peptides were screened out through comprehensive analysis,including bioactivity,solubility,toxicity,and allergenicity prediction via PeptideRanker,as well as binding energy comparison of molecular docking.Molecular docking analysis suggested that the a non-competitive inhibitory relationship might exist between the three peptides(FKL,LRM,and MRW)and tyrosinase.