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乳业科学与技术 ›› 2016, Vol. 39 ›› Issue (5): 1-6.DOI: 10.15922/j.cnki.jdst.2016.05.001

• 基础研究 •    下一篇

Paenibacillus spp.BD3526金属蛋白酶对乳蛋白水解位点分析

杭锋, 洪青, 王钦博   

  1. 光明乳业股份有限公司乳业研究院,上海乳业生物工程技术研究中心,乳业生物技术国家重点实验室,上海 200436
  • 出版日期:2016-09-01 发布日期:2022-02-08
  • 基金资助:
    上海市科委青年科技启明星人才计划项目(14QB1400200,16DZ2280600); “十二五”国家科技支撑计划项目(2013BAD18B02)

Analysis of Cleavage Sites in Bovine Milk Proteins by Metalloproteinase (M4) from Paenibacillus spp.BD3526

HANG Feng, HONG Qing, WANG Qinbo   

  1. (State Key Laboratory of Dairy Biotechnology, Shanghai Engineering Research Center of Dairy Biotechnology, Dairy Research Institute, Bright Dairy & Food Co. Ltd., Shanghai 200436, China)
  • Online:2016-09-01 Published:2022-02-08

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摘要： 为了比较具有凝乳功能的Paenibacillus spp.BD3526来源的金属蛋白酶与基因重组凝乳酶对乳蛋白水解位点的差异,采用BD3526金属蛋白酶和凝乳酶对αs1-酪蛋白(casein,CN)、αs2-CN、β-乳球蛋白(lactoglobulin,Lg)和κ-CN进行酶解,分别对不同时间的酶解产物采用高效液相色谱与四极杆飞行时间串联质谱(high performance liquid chromatography of quadrupole time of flight-tandem mass spectrometry,HPLC-Q-TOF-MS/MS)进行分析.结果表明:BD3526金属蛋白酶与凝乳酶在对乳蛋白的水解位点上具有较高的相似性,前者对αs1-CN、αs2-CN、β-Lg和κ-CN水解能力较后者弱,对P1为K(Lys)、R(Arg)且P1'为T(Thr)、F(Phe)和Y(Tyr)间的肽键水解特异性很高,并主要水解K-T (Lys-Thr)、K-F (Lys-Phe)、R-F(Arg-Phe)、R-Y(Arg-Tyr)肽键,水解生成的肽具有血管紧张素转换酶(angiotensin converting enzyme,ACE)抑制、抗菌、免疫调节等功能.

关键词: Paenibacillus spp.；金属蛋白酶；乳蛋白；水解位点

Abstract: In order to find the difference between the cleavage sites in bovine milk proteins by metalloproteinase from Paenibacillus spp. BD3526 and chymosin, the peptides generated from αs1-, αs2- and κ-casein and β-lactoglobulin (β-Lg) digested by the enzymes were analyzed by high performance liquid chromatography coupled with quadruple-timeof- flight mass spectrometer (HPLC-Q-TOF-MS-MS). The results indicated that the cleavage sites in bovine milk proteins by metalloproteinase and chymosin shared high similarity and both of these enzymes specifically cleaved the Lys-Thr, Lys-Phe, Arg- Phe and Arg-Tyr peptide bonds to generate peptides with ACE inhibitory, antimicrobial and immunomodulating activities.

Key words: Paenibacillus spp.; metalloproteinase; casein; cleavage site

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