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


CHEMICAL PAPERS, vol.69, no.3, pp.433-439, 2015 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 69 Issue: 3
  • Publication Date: 2015
  • Doi Number: 10.1515/chempap-2015-0031
  • Journal Name: CHEMICAL PAPERS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.433-439
  • Keywords: immobilisation, glucoamylase, alpha-amylase, glutaraldehyde, dextran polyaldehyde, crosslinked enzyme aggregates (CLEAs)
  • Çanakkale Onsekiz Mart University Affiliated: Yes


Cross-linked enzyme aggregates (CLEA) of Aspergillus oryzea a-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 a-amylase. On the other hand, no activity recovery was observed for Aspergillus niger glucoamylase due to the latter enzymes affinity for dextran.(C) 2014 Institute of Chemistry, Slovak Academy of Sciences