A facile approach to the isolation of proteins in Ferula asafoetida and their enzyme stabilizing, anti-microbial and anti-oxidant activity

摘要

The objective of the present study was to identify the proteome pattern, isolate and study the functions of selective proteins from Ferula asafoetida root exudate using chromatographic techniques. The root exudate proteins were fractionated using ion-exchange and gel filtration chromatography. A range of bioactive protein fractions were then separated in sufficient quantity which is the focus of this study. Based on studies, here we report three main proteins with molecular weights 14 kDa, 27 kDa, and 39 kDa. The biological and pharmacological activities of both purified and unpurified proteins obtained were extensively studied to understand their significance. The study revelaed that 27 kDa protein interestingly stabilized trypsin activity in 24 h of time and retained about 64% of the enzyme activity. Analyses confirmed 40 C and pH 8.0 are the optimum temperature and pH respectively. The 39 kDa protein remarkably increased the activity of chymotrypsin and the 14 kDa protein showed anti-bacterial activity against Pseudomonas aeruginosa. Invariably all of the three purified proteins showed enhanced anti-oxidant activity. In conclusion, results here obtained suggested that the primary metabolites (proteins) in asafoetida are mainly responsible for its versatile biological and pharmacological activities. (C) 2017 Elsevier B.V. All rights reserved.