Applied Biological Research
  • Year: 2014
  • Volume: 16
  • Issue: 1

Immobilization of α-amylase purified from Bacillus cereus MTCC 10205 by entrapment and adsorption on various support systems

Plant Biochemistry and Molecular Biology Laboratory, Department of Biochemistry, CCS Haryana Agricultural University, Hisar - 125 004, Haryana (India)

*E-mail: ajaydrdo@rediffmail.com

Online published on 29 May, 2014.

Abstract

Alpha-amylase from Bacillus cereus MTCC 10205 was immobilized by entrapment in alginate beads and carrageenan as well as via adsorption on charcoal. The immobilized enzyme had the pH optima 6.0 (in comparison to 5.5 of free enzyme), and temperature optima of 60°C (5°C higher than that of soluble enzyme). Thermostability of enzyme increased remarkably after immobilization. Storage stability and Km of the immobilized enzyme was higher than that of free form. Alginate entrapped enzyme could be stored at 4°C for one week without appreciable loss in activity, however carrageenan entrapped and charcoal adsorbed enzyme was stable only upto four days. The alginate entrapped α-amylase was found to have good operational utility (reused upto seven cycles) while carrageenan entrapped and charcoal adsorbed enzyme were reusable upto three cycles without appreciable loss in activity. Results of the study indicated that alginate entrapped enzyme had better thermostability and operational utility.

Keywords

Alginate, α-amylase, Bacillus cereus, carrageenan, charcoal, immobilization