Immobilization of alpha-amylase onto cyclic carbonate bearing hybrid material

Turunc O., KAHRAMAN M. V., Akdemir Z. S., KAYAMAN APOHAN N., Gungor A.

FOOD CHEMISTRY, vol.112, no.4, pp.992-997, 2009 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 112 Issue: 4
  • Publication Date: 2009
  • Doi Number: 10.1016/j.foodchem.2008.07.024
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.992-997
  • Keywords: alpha-Amylase, Enzyme immobilization, Cyclic carbonate, Sol gel, UV curing, COVALENT IMMOBILIZATION, ALKALINE-PHOSPHATASE, VINYLENE CARBONATE, ENZYME-ACTIVITY, STABILITY, HYDROLYSIS, BEADS, IMPROVEMENT, CARRIERS, RESIN
  • Marmara University Affiliated: Yes

Abstract

Under ambient conditions, 4-((3-trimethoxysilyl)propoxy)methyl)1,3-dioxolan-2-one was synthesized from 3-glycidyloxypropyl trimethoxysilane. Methacrylate and cyclic carbonate functional hybrid matrix was prepared by sol-gel method. alpha-Amylase was covalently bounded onto the matrix via cyclic carbonate functionality. Immobilization yield was found as 34.4 +/- 2.6 mg per gram of hybrid matrix. The maximum activity was observed at pH 6.5. Immobilization did not change the pH-dependency of the enzyme. The immobilized enzyme had a higher activity at elevated temperature (50-80 degrees C) than the free one. Immobilized enzyme exhibited 80% activity after 20 runs and 69% after 30 runs. Free enzyme lost its activity completely within 15 days. Immobilized enzyme lost only 30% of its activity in 25 days. V-max values for the free and immobilized enzymes were calculated as 58 x 10(-3) and 5.2 x 10(-3) mg/ml min(-1), respectively. (C) 2008 Elsevier Ltd. All rights reserved.