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Fermentation 2017, 3(1), 2; doi:10.3390/fermentation3010002

Purification and Properties of Yeast Proteases Secreted by Wickerhamomyces anomalus 227 and Metschnikovia pulcherrima 446 during Growth in a White Grape Juice

Institute for Microbiology and Wine Research, Johannes Gutenberg University of Mainz, Becherweg 15, D-55099 Mainz, Germany
Institute of Immunology, University Medical Centre of the Johannes Gutenberg University Mainz, Langenbeckstr. 1, D-55131 Mainz, Germany
Author to whom correspondence should be addressed.
Academic Editor: Ronnie G. Willaert
Received: 25 October 2016 / Revised: 19 December 2016 / Accepted: 19 December 2016 / Published: 26 December 2016
(This article belongs to the Special Issue Yeast Biotechnology)
View Full-Text   |   Download PDF [1785 KB, uploaded 26 December 2016]   |  


Aspartic proteases are of significant importance for medicine and biotechnology. In spite of sufficient evidence that many non-Saccharomyces yeasts produce extracellular proteases, previous research has focused on the enzymes of Candida species because of their role as virulence factors. Nowadays, there is also increasing interest for their applications in industrial processes, mainly because of their activities at low pH values. Here, we report the features of new acid proteases isolated from wine-relevant yeasts Metschnikovia pulcherrima and Wickerhamomyces anomalus. To our knowledge, this is the first detailed description of such an enzyme derived from strains of W. anomalus. Deviating to most former studies, we could demonstrate that the yeasts produce these enzymes in a natural substrate (grape juice) during the active growth phase. The enzymes were purified from concentrated grape juice by preparative isoelectric focusing. Biochemical data (maximum activity at ≈ pH 3.0, inhibition by pepstatin A) classify them as aspartic proteases. For W. anomalus 227, this assumption was confirmed by the protein sequence of WaAPR1 determined by LC-MS/MS. The sequence revealed a signal peptide for secretion, as well as a peptidase A1 domain with two aspartate residues in the active site. The enzyme has a calculated molecular mass of 47 kDa and an isolelectric point of 4.11. View Full-Text
Keywords: aspartic protease; Wickerhamomyces; Metschnikovia; grape juice; wine protein aspartic protease; Wickerhamomyces; Metschnikovia; grape juice; wine protein

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Schlander, M.; Distler, U.; Tenzer, S.; Thines, E.; Claus, H. Purification and Properties of Yeast Proteases Secreted by Wickerhamomyces anomalus 227 and Metschnikovia pulcherrima 446 during Growth in a White Grape Juice. Fermentation 2017, 3, 2.

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