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Updated: Jun 5, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
An alkali-thermotolerant extracellular protease from a newly isolated Streptomyces sp. DP2
Bijender K Bajaj1, Priyanka Sharma
1School of Biotechnology, University of Jammu, Jammu 180 006, India. bkbajaj1@rediffmail.com
Abstract:
Of six alkalitolerant, extracellular protease producing bacterial strains isolated, DP2 displayed maximum activity. This organism was designated as Streptomyces sp. DP2 and identified as Streptomyces ambofaciens. Maximum protease yield was observed after 48hours of submerged fermentation using various carbon and nitrogen sources. Fructose was found to be the best substrate for protease production, followed by maltose, lactose and wheat bran. Mustard cake is reported for the first time as the most ideal nitrogen source although soybean meal also gave comparable yield. The protease produced by Streptomyces sp. DP2 exhibited extensive activity over a broad pH range (4-12) with maximum activity at pH 8, and was active over a broad range of elevated temperatures (50-100°C), and possessed thermostability at 60-90°C for up to 1 hour. Enzyme activity was reduced by EDTA (25%), SDS (16%), and PMSF (6%). This novel alkaline protease has both alkali- and thermostability that may have industrial significance.
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