Literature DB >> 17516249

Optimization of alpha-amylase immobilization in calcium alginate beads.

Figen Ertan1, Hulya Yagar, Bilal Balkan.   

Abstract

alpha-Amylase enzyme was produced by Aspergillus sclerotiorum under SSF conditions, and immobilized in calcium alginate beads. Effects of immobilization conditions, such as alginate concentration, CaCl(2) concentration, amount of loading enzyme, bead size, and amount of beads, on enzymatic activity were investigated. Optimum alginate and CaCl(2) 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 degrees C.

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Year:  2007        PMID: 17516249     DOI: 10.1080/10826060701386679

Source DB:  PubMed          Journal:  Prep Biochem Biotechnol        ISSN: 1082-6068            Impact factor:   2.162


  3 in total

1.  Saccharification of citrus wastes by immobilized polygalacturonase in an improved alginate matrix.

Authors:  Yuly A Ramírez-Tapias; Aldana S Lapasset Laumann; Claudia N Britos; Cintia W Rivero; Jorge A Trelles
Journal:  3 Biotech       Date:  2017-10-26       Impact factor: 2.406

2.  Entrapment of α-Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate.

Authors:  Manu Sharma; Vinay Sharma; Dipak K Majumdar
Journal:  Int Sch Res Notices       Date:  2014-09-15

3.  Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix.

Authors:  Muhammad Asif Nawaz; Haneef Ur Rehman; Zainab Bibi; Afsheen Aman; Shah Ali Ul Qader
Journal:  Biochem Biophys Rep       Date:  2015-10-08
  3 in total

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