Comparison of some properties of free and immobilized α-amylase by Aspergillus sclerotiorum in calcium alginate gel beads

YAĞAR H., ERTAN F., Balkan B.

Preparative Biochemistry and Biotechnology, cilt.38, sa.1, ss.13-23, 2008 (SCI-Expanded, Scopus) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 38 Sayı: 1
  • Basım Tarihi: 2008
  • Doi Numarası: 10.1080/10826060701774304
  • Dergi Adı: Preparative Biochemistry and Biotechnology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.13-23
  • Anahtar Kelimeler: α-Amylase, Aspergillus sclerotiorum, Calcium alginate, Entrapment, Hydrolysis, Soluble starch
  • Trakya Üniversitesi Adresli: Evet

Özet

Some properties of immobilized α-amylase by Aspergillus sclerotiorum within calcium alginate gel beads were investigated and compared with soluble enzyme. Optimum pH and temperature were found to be 5.0 and 40°C, respectively, for both soluble and immobilized enzymes. The immobilized enzyme had a better Km value, but kcat/Km values were the same for both enzymes. Entrapment within calcium alginate gel beads improved, remarkably, the thermal and storage stability of α-amylase. The half life values of immobilized enzyme and soluble enzyme at 60°C were 164.2, and 26.2 min, respectively. The midpoint of thermal inactivation (Tm) shifted from 56°C (for soluble enzyme) to 65.4°C for immobilized enzyme. The percentages of soluble starch hydrolysis for soluble and immobilized α-amylase were determined to be 97.5 and 92.2% for 60 min, respectively. Copyright © Taylor & Francis Group, LLC.