Applied Biochemistry and Biotechnology

, Volume 170, Issue 7, pp 1713–1723

Expression and Displaying of β-Glucosidase from Streptomyces Coelicolor A3 in Escherichia coli

Article

DOI: 10.1007/s12010-013-0301-4

Cite this article as:
Gu, MZ., Wang, JC., Liu, WB. et al. Appl Biochem Biotechnol (2013) 170: 1713. doi:10.1007/s12010-013-0301-4

Abstract

Two genes encoding β-glucosidase from Streptomyces coelicolor A3(2) were cloned and expressed in Escherichia coli BL21 (DE3). Two recombinant enzymes (SC1059 and SC7558) were purified and characterized. The molecular mass of the purified SC1059 and SC7558 as determined by SDS-PAGE agrees with the calculated values (51.0 and 52.2 kDa, respectively). Optimal temperature and pH for the two enzymes were both at 35 °C and 6.0. SC7558 exhibited to be much more active than SC1059 under optimal conditions, and it was recombined with ice nucleation protein which could anchor on the surface of the cell. The optimal temperature and pH of the recombinant cells were 55 °C and 8.0, respectively. The resultant cells were to be used as material for immobilized β-glucosidase, which is convenient to catalyze substrates in various complicated conditions.

Keywords

β-GlucosidaseSurface displayingStreptomyces coelicolor

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor EngineeringEast China University of Science and TechnologyShanghaiChina