The server is under maintenance between 08:00 to 12:00 (GMT+08:00), and please visit later.
We apologize for any inconvenience caused
Login  | Sign Up  |  Oriprobe Inc. Feed
China/Asia On Demand
Journal Articles
Laws/Policies/Regulations
Companies/Products
Bookmark and Share
Analysis of Cleavage Sites in Bovine Milk Proteins by Metalloproteinase (M4) from Paenibacillus spp.BD3526
Author(s): 
Pages: 1-6
Year: Issue:  5
Journal: Journal of Dairy Science and Technology

Keyword:  metalloproteinasecaseincleavage site;
Abstract: 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.
Related Articles
No related articles found