Transglycosylation properties of a Kluyveromyces lactis enzyme preparation: Production of tyrosol β-fructoside using free and immobilized enzyme

Abstract

A variety of glycosides with interesting biological properties suitable for application in cosmetic and pharmaceutical industry can be found in nature. However, the demand exceeds the quantity and purity which can be obtained naturally and therefore enzymatic glycosylation has been of great interest in recent decades. In this study, crude Kluyveromyces lactis enzyme preparation Lactozym 3000 L was examined for the production of two phenolic glycosides – tyrosol β-fructoside and tyrosol β-galactoside. Its performance was compared to other commercial fungal and yeast enzyme preparations. It was found that the key enzyme, β-galactosidase is unsuitable for tyrosol β-galactoside production. However, one of the Lactozym 3000 L components, β-fructofuranosidase, performed very well in the tyrosol β-fructoside production from sucrose and tyrosol. Lactozym 3000 L was effectively immobilized onto activated carrier Lifetech ECR8309 via covalent binding of the enzyme, which is a promising method to reduce very high enzyme consumption in its free form. Potential of deep-eutectic solvents to enhance transfructosylation selectivity has been studied proving their interesting stabilization effect on Lactozym 3000 L β-fructofuranosidase.