PURIFICATION AND CHARACTERIZATION OF AN ENDOGLUCANASE PRODUCED FROM Streptomyces sp. STRAINBPNG23

Authors

  • Azzeddine BETTACHE Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000)? Algeria
  • Copinet Estelle Laboratory of Industrial Microbiology, university of Reims Champagne-Ardenne, Reims (51687), France.
  • Zahra Azzouz Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000), Algeria.
  • Nawel Boucherba Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000), Algeria.
  • Celia Bouiche Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000), Algeria.
  • Samir Hamma Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000), Algeria.
  • Rima Maibeche Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000), Algeria.
  • Francis Duchiron Laboratory of Industrial Microbiology, university of Reims Champagne-Ardenne, Reims (51687), France.
  • Said Benallaoua Laboratory of Applied Microbiology, faculty of nature science and life, university of Bejaia (06000), Algeria.

DOI:

https://doi.org/10.15414/jmbfs.2020.10.2.284-288

Keywords:

Streptomyces, endoglucanase, purification, characterization, wheat bran

Abstract

Streptomyces sp. strain BPNG23 produces five endoglucanases: endo1, endo 2, endo 3, endo 4 and endo 5.The endo2 has been purified and characterized by two subsequent purification steps with ultrafiltration and anion exchange chromatography. The specific activity of the endoglucanase has been found to be 380.65 U/mg. The molecular weight to the endoglucanase 2 has been estimated with sodium dodecyl sulfate-polyacrylamide gel electrophoresis, revealing that this isoenzyme is a 66 KDa monomeric enzyme. It showed an optimum temperature and pH values respectively of 6.0 and 50 °C. It was thermostable, it exhibited a half-life time 6 h with a temperature of  50 °C, the enzyme was activated by several metal ions Mn+2, NH4+, Zn2+, Ca2+, Fe2+, Ni2+ and  Co2+. It presents a higher affinity towards carboxymethyl cellulose (CMC) with a Km of 6.37 mg/mL and Vmax of 0.056 μmol/mn. This the first of a study of purification and characterization of an endoglucanase produced by a newly isolated actinobacteria strain in Kabylia region (Algeria).

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Published

2020-10-16

Issue

Section

Biotechnology