Characterization of transglutaminase from Bacillus subtilis and its cross-linking function with a bovine serum albumin model,Food & Function

当前位置： X-MOL 学术 › Food Funct. › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Characterization of transglutaminase from Bacillus subtilis and its cross-linking function with a bovine serum albumin model
Food & Function ( IF 5.1 ) Pub Date : 2018-09-21 00:00:00 , DOI: 10.1039/c8fo01503a
Yihan Liu _{1,

2,

3,

4,

5} , Lin Huang _{1,

2,

3,

4,

5} , Dong Zheng _{1,

2,

3,

4,

5} , Yu Fu _{1,

2,

3,

4,

5} , Mengying Shan _{1,

2,

3,

4,

5} , Yanzhen Li _{1,

2,

3,

4,

5} , Zehua Xu _{1,

2,

3,

4,

5} , Leibo Jia _{1,

2,

3,

4,

5} , Wenhang Wang _{2,

5,

6,

7,

8} , Fuping Lu _{1,

2,

3,

4,

5}

Affiliation

Finding new crosslinking enzymes for enzyme-mediated protein conjugation is a great need in the food industry. In this research, the properties of Bacillus subtilis transglutaminase (BTG) were characterized in detail and its protein crosslinking functions with bovine serum albumin (BSA) as a model were studied. Compared to the commercial transglutaminase from Streptoverticillium mobaraense, BTG was more stable in a broad range of temperatures (30–60 °C) and pH values (pH 5.0–9.0), with its maximum enzymatic activity at 60 °C and pH 8.0. The protein function evaluation results demonstrated that the BTG-modified BSA showed better emulsifying and foaming properties (p < 0.05) compared with the native one. Additionally, significant improvements (p < 0.05) were observed in the rheological properties, water holding capacity, and textural properties of the BTG-treated BSA gels. With good thermal and pH stability and excellent crosslinking effects, BTG would be a potential enzyme for food structure engineering to improve the functional properties of food proteins and expand their applications.

中文翻译：

枯草芽孢杆菌 转谷氨酰胺酶的表征及其与牛血清白蛋白模型的交联功能

寻找新的用于酶介导的蛋白质缀合的交联酶是食品工业中的巨大需求。在这项研究中，枯草芽孢杆菌转谷氨酰胺酶（BTG）的特性进行了详细描述，并以牛血清白蛋白（BSA）为模型研究了其蛋白质的交联功能。与来自茂链链霉菌的商业转谷氨酰胺酶相比，BTG在宽广的温度范围（30–60°C）和pH值（pH 5.0–9.0）下更稳定，在60°C和pH 8.0时具有最大的酶促活性。蛋白质功能评估结果表明，与天然BSA相比，经BTG修饰的BSA具有更好的乳化和起泡性能（p <0.05）。此外，重大改进（p<0.05）在BTG处理的BSA凝胶的流变性质，持水量和质构性质方面观察到。BTG具有良好的热稳定性和pH稳定性以及出色的交联效果，将成为食品结构工程中潜在的酶，可改善食品蛋白质的功能特性并扩大其应用范围。

更新日期：2018-09-21

点击分享查看原文

点击收藏

阅读更多本刊最新论文本刊介绍/投稿指南11