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Immobilisation of Aspergillus oryzae α-amylase and Aspergillus niger glucoamylase enzymes as cross-linked enzyme aggregates

A. Sercan Sahutoglu and Cahit Akgul

Department of Chemistry, Faculty of Sciences and Arts, Canakkale Onsekiz Mart University 17200, Canakkale, Turkey

 

E-mail: sercansahutoglu@comu.edu.tr

Abstract: Cross-linked enzyme aggregates (CLEA) of Aspergillus oryzea α-amylase (AoAA) and Aspergillus niger glucoamylase (AnGA) were prepared using glutaraldehyde and dextran polyaldehyde as crosslinkers. The maximum activity recoveries for glutaraldehyde cross-linking were 21.8 % and 41.2 %, respectively. The addition of a proteic feeder (bovine serum albumin) exhibited a negative effect on the activity recoveries for both enzymes. Dextran polyaldehyde was used as a cross-linking agent instead of glutaraldehyde to reduce the activity losses. As a result, an activity recovery of 60.0 % was obtained for Aspergillus oryzea α-amylase. On the other hand, no activity recovery was observed for Aspergillus niger glucoamylase due to the latter enzyme’s affinity for dextran.

Keywords: immobilisation – glucoamylase – α-amylase – glutaraldehyde – dextran polyaldehyde – crosslinked enzyme aggregates (CLEAs)

Full paper is available at www.springerlink.com.

DOI: 10.1515/chempap-2015-0031

 

Chemical Papers 69 (3) 433–439 (2015)

Wednesday, July 24, 2024

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