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Characterization of β-glucosidases from Hanseniaspora sp. and Pichia anomala with potentially aroma-enhancing capabilities in juice and wine

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Abstract

The properties of intracellular β-glucosidases produced from two yeast isolates identified as Hanseniaspora sp. BC9 and Pichia anomala MDD24 were characterized. β-Glucosidase from Hanseniaspora sp. BC9 was not inhibited by both 20% w/v fructose and 20% w/v sucrose and was slightly inhibited by glucose (> 40% relative β-glucosidase activity with 10% w/v glucose). β-Glucosidase from P. anomala MDD24 was inhibited by glucose, fructose and sucrose. In the presence of 4–12% v/v ethanol, β-glucosidase from P. anomala MDD24 was stimulated in range 110–130% relative activity whereas β-glucosidase from Hanseniaspora sp. BC9 was substantially inhibited in the presence of ethanol. Finally, juice and wine of the Muscat-type grape variety, Traminette, were selected to determine sugar-bound volatile aroma release, particularly terpenes, by the activity of those β-glucosidases. The results showed that high concentration of free aroma compounds were detected from Traminette juice treated with β-glucosidase from Hanseniaspora sp. BC9 and Traminette wine treated with β-glucosidase from P. anomala MDD24. The preliminary results with proposed an application of these enzymes in commercial wine production lead to more efficient of β-glucosidase from Hanseniaspora sp. BC9 in releasing desirable aromas during an early stage of alcoholic fermentation while β-glucosidase from P. anomala MDD24 is suitable at the final stage of alcoholic fermentation.

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Acknowledgments

The authors would like to acknowledge the support from the Agro-Industry Consortium Commission, Commission on Higher Education, Ministry of Education, Thailand.

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Correspondence to Kanit Vichitphan.

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Swangkeaw, J., Vichitphan, S., Butzke, C.E. et al. Characterization of β-glucosidases from Hanseniaspora sp. and Pichia anomala with potentially aroma-enhancing capabilities in juice and wine. World J Microbiol Biotechnol 27, 423–430 (2011). https://doi.org/10.1007/s11274-010-0474-8

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  • DOI: https://doi.org/10.1007/s11274-010-0474-8

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