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Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by β-galactosidase from Aspergillus oryzae

Paper ID Volume ID Publish Year Pages File Format Full-Text
34335 45018 2015 7 PDF Available
Title
Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by β-galactosidase from Aspergillus oryzae
Abstract

•Salicin was efficient acceptor in β-galactosidase-catalyzed transgalactosylation.•Ion mobility mass spectrometry proved reaction was regioselective.•Product was formed via primary hydroxyl group of carbohydrate moiety.•The increase of product yield up to 30.8 mM was achieved using RSM.

In this study, enzymatic synthesis of galactoside of salicin, compound with potential physiological activity due to structural resemblance with galectin inhibitors, and analgesic and antipyretic properties of salicin, was performed using β-galactosidase from Aspergillus oryzae. It was determined, using HPLC and ion mobility mass spectrometry, that enzymatic synthesis was highly selective since only one isomer was formed via primary hydroxyl group on glucose moiety of salicin. The optimization of key experimental factors using response surface methodology enabled galactosyl salicin concentration up to 30.8 mM obtained at lactose concentration 40 mM, salicin concentration 110 mM, enzyme amount 360 IU and reaction time 12 h.

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Keywords
Salicin; β-Galactosidase; Transgalactosylation; Response surface methodology; Ion mobility
First Page Preview
Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by β-galactosidase from Aspergillus oryzae
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 50, Issue 5, May 2015, Pages 782–788
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering