Protein & Peptide Letters

Author(s): Mahjabeen Saleem, Muhammad Saleem Akhtar, Riffat Yasmin, Mahreen Zahid, Nadeem Nawazish Malik, Munazza Afzal and Muhammad Ibrahim Rajoka

DOI: 10.2174/092986608784246560

Production, Purification and Characterization of β-1,4-Endoglucanase from a Novel Bacterial Strain CTP-09 of a Bacillus sp.

Page: [402 - 410] Pages: 9

  • * (Excluding Mailing and Handling)

Abstract

Bacillus strain CTP-09 yielded maximum productivity (1120 IU/L.h) of extracellular endoglucanase (CMCase) on 0.5% cellobiose after 10 h fermentation at 55° C. The purified enzyme is mono-meric in nature and exhibits stability up to 80° C and over a pH range (6.0-9.0). Activation energy, enthalpy and entropy of catalysis, and inactivation indicated that this CMCase is highly thermos-table. Purified enzyme possessed high power of defibrillation of textile and was minutely inhibited by anionic detergent and oxidizing agent comparable with inhibition by commercial enzyme. This polypeptide could be exploited for mass production and application in local industries.

Keywords: Bacillus sp., endoglucanase, enthalpy, entropy, kinetics, thermodynamics, turn over number