Immobilization of B. amyloliquefaciens alpha-amylase and comparison of some of its enzymatic properties with the free form

DEMİRKAN E., Dincbas S., Sevinc N., ERTAN F.

ROMANIAN BIOTECHNOLOGICAL LETTERS, vol.16, no.6, pp.6690-6701, 2011 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 16 Issue: 6
  • Publication Date: 2011
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.6690-6701
  • Keywords: alpha-amylase, Bacillus amyloliquefaciens, calcium alginate, immobilization, optimization, thin layer chromatography, ALGINATE BEADS, STARCH, HYDROLYSIS, LIPASE, OPTIMIZATION, PURIFICATION, ENTRAPMENT, STABILITY, MATRIX
  • Bursa Uludag University Affiliated: Yes


The enzyme alpha-Amylase from Bacillus amyloliquefaciens was entrapped by drop-wise addition of an aqueous mixture of sodium alginate in the solution of a Ca2+ salt. Effects of immobilization conditions were investigated. Optimum alginate and CaCl2 concentrations were found to be 2% and 5% (w/v), respectively. The immobilization yield was 89%. Amylase activity increased with increasing enzyme loading on the beads. The best size and amount of beads for achieving enzyme activity were found to be 3 mm and 0.4 g, respectively. When coated with silicate, amylase-entrapped beads retained the highest catalytic activity. The highest operational stability was six reuses with 51% residual activity. Some properties of immobilized enzyme were determined, and compared with those of free enzyme. Product profile of the various raw starches has been determined by thin layer chromatography.