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来自……的蛋白酶抑制剂的筛选、纯化及特性分析

Screening, Purification and Characterization of Protease Inhibitor from .

作者信息

Mohan Manju, Kozhithodi Shireen, Nayarisseri Anuraj, Elyas Kothanam Kuzhiyil

机构信息

Department of Biotechnology, University of Calicut - 673635, Kerala, India.

In silico Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, Madhya Pradesh, India.

出版信息

Bioinformation. 2018 Jun 30;14(6):285-293. doi: 10.6026/97320630014285. eCollection 2018.

DOI:10.6026/97320630014285
PMID:30237674
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6137568/
Abstract

Plants are rich in protease inhibitors (PI) and trypsin inhibitors are the most common. Therefore, it is of interest to screen PI from plant sources. We report the screening, purification and characterization of PI from Capsicum frutescenes. The partially purified PI showed bands corresponding to 21 KDa and was further confirmed using reverse zymography. The enzyme was stable at temperatures below 60°C and a wide range of pH with 65 folds purification. The effect of magnesium ions oxidizing and reducing agents on PI is reported. The large-scale isolation and purification of PI from Capsicum frutescenes is of commercial interest.

摘要

植物富含蛋白酶抑制剂(PI),其中胰蛋白酶抑制剂最为常见。因此,从植物来源筛选PI具有重要意义。我们报道了从辣椒中筛选、纯化和鉴定PI的过程。部分纯化的PI显示出对应于21 kDa的条带,并通过反向酶谱法进一步确认。该酶在60°C以下的温度和较宽的pH范围内稳定,纯化倍数为65倍。报道了镁离子、氧化剂和还原剂对PI的影响。从辣椒中大规模分离和纯化PI具有商业价值。

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