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, cilt.16, sa.6, ss.6690-6701, 2011 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 16 Sayı: 6
  • Basım Tarihi: 2011
  • Dergi Adı: ROMANIAN BIOTECHNOLOGICAL LETTERS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.6690-6701
  • Anahtar Kelimeler: alpha-amylase, Bacillus amyloliquefaciens, calcium alginate, immobilization, optimization, thin layer chromatography, ALGINATE BEADS, STARCH, HYDROLYSIS, LIPASE, OPTIMIZATION, PURIFICATION, ENTRAPMENT, STABILITY, MATRIX
  • Bursa Uludağ Üniversitesi Adresli: Evet

Özet

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.