Journal
BIOCATALYSIS AND BIOTRANSFORMATION
Volume 31, Issue 6, Pages 329-334Publisher
INFORMA HEALTHCARE
DOI: 10.3109/10242422.2013.858711
Keywords
alpha-L-rhamnosidase; Aspergillus terreus; immobilization; polyvinyl alcohol gel; isoquercitrin
Funding
- European Union [266025]
- Slovak Research and Development Agency [DO7RP-0042-11]
- Ministry of Education of the Czech Republic [7E11010]
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Recombinant alpha-L-rhamnosidase from Aspergillus terreus expressed in Pichia pastoris was immobilized in LentiKats (R) lens-shaped polyvinylalcohol (PVA) capsules with an activity of 7 U g(-1), which was 21% of its original activity. Immobilization did not significantly affect the pH and temperature profile of alpha-L-rhamnosidase, K-M increased by a factor of 3.4 whereas V-max decreased more than 10-fold. No decrease in activity was observed after 27 repeated batch runs of rutin derhamnosylation. The enzyme proved to have an excellent storage stability (136 days) in 60 g L-1 ethanol with no change in its activity.
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