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Purification, characterization, and antimicrobial activity of nontoxic trypsin inhibitor from Albizia amara Boiv.

Paper ID Volume ID Publish Year Pages File Format Full-Text
34261 45013 2016 16 PDF Available
Title
Purification, characterization, and antimicrobial activity of nontoxic trypsin inhibitor from Albizia amara Boiv.
Abstract

•A novel, nontoxic, proteinaceous trypsin inhibitor was reported from seeds of Albizia amara.•The purified proteinaceous protease inhibitor (API) is a thermo- and salt-stable 49-kDa protein.•API has antifungal activity against Alternaria alternata, Alternaria tenuissima, and Candida albicans.•API has antibacterial activity against Pseudomonas aeruginosa and Bacillus subtilis.•API has potential to inhibit trypsin, chymotrypsin, and proteinase-K.

The present investigation describes the purification, and characterization of a novel, thermostable, nontoxic, proteinaceous trypsin inhibitor extracted from seeds of Albizia amara Boiv. The proteinaceous protease inhibitor (API) was purified via acetone fractionation, ion-exchange chromatography (diethylaminoethyl (DEAE) cellulose), and gel permeation chromatography (GPC; Sephadex G-100). The apparent molecular weight of the API is 49 kDa and is identified as a serine protease inhibitor. The API remains active in a wide pH range (3.0–8.0), and showed thermal stability at 60 °C. The API inhibits trypsin by a mixed inhibitory mechanism with an inhibition constant (Ki) of 1.24 × 10−8 M using BApNA (Nα-benzoyl-dl-arginine-p-nitroanilide hydrochloride) as the substrate. The API also showed substantial activity in the presence of several metal ions, surfactant (Triton X-100), oxidizing agent (dimethyl sulfoxide; DMSO), and NaCl (5%). Moreover, API retained 85% trypsin inhibition activity upon storage at 4 °C over a period of 6 months. The antimicrobial effectiveness of the API against Pseudomonas aeruginosa, Bacillus subtilis, Alternaria alternata, Alternaria tenuissima, and Candida albicans reported in this study suggests its utility as a potential antimicrobial component.

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Keywords
Albizia amara; Proteinaceous protease inhibitor; Trypsin; Antimicrobial; Nontoxic; Phytopathogens
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Purification, characterization, and antimicrobial activity of nontoxic trypsin inhibitor from Albizia amara Boiv.
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 51, Issue 5, May 2016, Pages 659–674
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us