Literature DB >> 27283635

Catalytic properties of maltogenic α-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles.

Antanas Straksys1, Tatjana Kochane2, Saulute Budriene3.   

Abstract

The immobilization of maltogenic α-amylase from Bacillus stearothermophilus (BsMa) onto novel porous poly(urethane urea) (PUU) microparticles synthesized from poly(vinyl alcohol) and isophorone diisocyanate was performed by covalent attachment to free isocyanate groups from PUU microparticles, or by physical adsorption of enzyme onto the surface of the carrier. The influence of structure, surface area and porosity of microparticles on the catalytic properties of immobilized BsMa was evaluated. The highest efficiency of immobilization of BsMa was found to be 72%. Optimal activity of immobilized BsMa was found to have increased by 10°C compared with the native enzyme. Influence of concentration of sodium chloride on activity of immobilized BsMa was evaluated. High storage and thermal stability and reusability for starch hydrolysis of immobilized enzyme were obtained. Immobilized BsMa has a great potential for biotechnology.
Copyright © 2016 Elsevier Ltd. All rights reserved.

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Keywords:  Covalent binding; Immobilization; Maltoghenic α-amylase; Poly(urethane urea) microparticles; Starch hydrolysis

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Year:  2016        PMID: 27283635     DOI: 10.1016/j.foodchem.2016.05.071

Source DB:  PubMed          Journal:  Food Chem        ISSN: 0308-8146            Impact factor:   7.514


  1 in total

1.  α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors.

Authors:  Ömür Acet; Tülden İnanan; Burcu Önal Acet; Emrah Dikici; Mehmet Odabaşı
Journal:  Appl Biochem Biotechnol       Date:  2021-03-29       Impact factor: 2.926

  1 in total

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