Immobilization of B. amyloliquefaciens ?-amylase and comparison of some of its enzymatic properties with the free form
Küçük Resim Yok
Tarih
2011
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Ars Docendi
Erişim Hakkı
info:eu-repo/semantics/closedAccess
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.
Açıklama
Anahtar Kelimeler
Alpha-Amylase, Bacillus Amyloliquefaciens, Calcium Alginate, Immobilization, Optimization, Thin Layer Chromatography, Alginate Beads, Starch, Hydrolysis, Lipase, Optimization, Purification, Entrapment, Stability, Matrix
Kaynak
Romanian Biotechnological Letters
WoS Q Değeri
Q4
Scopus Q Değeri
N/A
Cilt
16
Sayı
6
