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Substantial Improvement of Tryptic and Chymotryptic Hydrolysis of β-Lactoglobulin Pretreated with High Voltage Electrical Treatments
ACS Sustainable Chemistry & Engineering ( IF 8.4 ) Pub Date : 2020-09-03 , DOI: 10.1021/acssuschemeng.0c03904
Rock-Seth Agoua 1, 2 , Laurent Bazinet 1, 3 , Eugène Vorobiev 4 , Nabil Grimi 4 , Sergey Mikhaylin 1, 2, 3
Affiliation  

β-lactoglobulin (β-lg) is an important source of biologically and functionally active peptides that are of particular interest in agri-food, nutraceutical, and pharmaceutical industries. Enzymatic hydrolysis of proteins remains the most common mode of peptide production. However, efficient hydrolysis of proteins and particularly β-lg is difficult to perform due to their compact globular structure. Thus, the current study deals with green high-voltage electric treatments (HVET): pulsed electric fields and electric arc to pretreat β-lg and improve its proteolysis by trypsin and chymotrypsin. The results demonstrate substantial improvement of hydrolysis performance after the pretreatment of β-lg with HVET compared to the non-pretreated and preheated β-lg. Moreover, HVET led to the peptide release from β-lg even before the addition of proteases. Furthermore, pioneer studies of proteolysis kinetics and structural changes of β-lg molecules subjected to HVET allowed a better understanding of the mechanisms underlying hydrolysis improvement.

中文翻译:

高压电气处理预处理的β-乳球蛋白的胰蛋白酶和胰胰蛋白酶水解的显着改善

β-乳球蛋白(β-lg)是重要的生物和功能活性肽来源,在农业食品,营养保健品和制药行业中特别受到关注。蛋白质的酶水解仍然是最常见的肽生产方式。然而,由于其紧密的球状结构,蛋白质尤其是β-Ig的有效水解难以进行。因此,当前的研究涉及绿色高压电处理(HVET):脉冲电场和电弧预处理β-lg,并通过胰蛋白酶和胰凝乳蛋白酶改善其蛋白水解作用。结果表明,与未经预处理和预热的β-Ig相比,用HVET预处理β-Ig后的水解性能有了显着提高。而且,HVET甚至在添加蛋白酶之前也导致肽从β-1g释放。
更新日期:2020-10-05
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