Optimization of α-amylase immobilization in calcium alginate beads

ERTAN F., YAĞAR H., Balkan B.

Preparative Biochemistry and Biotechnology, cilt.37, sa.3, ss.195-204, 2007 (SCI-Expanded, Scopus) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 37 Sayı: 3
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1080/10826060701386679
  • Dergi Adı: Preparative Biochemistry and Biotechnology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.195-204
  • Anahtar Kelimeler: α-Amylase, Alginate, Aspergillus sclerotiorum, Entrapment, SSF, Starch hydrolysis
  • Trakya Üniversitesi Adresli: Evet

Özet

α-Amylase enzyme was produced by Aspergillus sclerotiorum under SSF conditions, and immobilized in calcium alginate beads. Effects of immobilization conditions, such as alginate concentration, CaCl2 concentration, amount of loading enzyme, bead size, and amount of beads, on enzymatic activity were investigated. Optimum alginate and CaCl2 concentration were found to be 3% (w/v). Using a loading enzyme concentration of 140 U mL-1, and bead (diameter 3 mm) amount of 0.5 g, maximum enzyme activity was observed. Beads prepared at optimum immobilization conditions were suitable for up to 7 repeated uses, losing only 35% of their initial activity. Among the various starches tested, the highest enzyme activity (96.2%) was determined in soluble potato starch hydrolysis for 120 min at 40°C. Copyright © Taylor & Francis Group, LLC.