Invertase and urease activities in the carotenogenic yeast Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma)

• Published in: Bioresource technology Vol. 82; no. 1; pp. 79 - 85
• Main Authors: Persike, Daniele S, Bonfim, Tânia M.B, Santos, Maria H.R, Lyng, Sabrina M.O, Chiarello, Marileusa D, Fontana, José D
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.03.2002; Elsevier Science
• Subjects: Affinity chromatography; beta-Fructofuranosidase; Biological and medical sciences; Biotechnology; carbon; Cell Division - physiology; cell growth; Cell-bound; cellobiose; Cellobiose - metabolism; Chromatography, Affinity; Electrophoresis; Enzyme engineering; Enzyme Induction; Enzyme Inhibitors - pharmacology; Fermentation; Fundamental and applied biological sciences. Psychology; glass; Glycoside Hydrolases - antagonists & inhibitors; Glycoside Hydrolases - metabolism; Invertase; Methods. Procedures. Technologies; pearls; Phaffia rhodozyma; Production of selected enzymes; Sonication; Substrate Specificity; sucrose; Sucrose - metabolism; Temperature; ultrasonic treatment; Urea - metabolism; Urease; Urease - antagonists & inhibitors; Urease - metabolism; Xanthophyllomyces dendrorhous; yeasts; Yeasts - enzymology; Yeasts - metabolism; Sonication; Xanthophyllomyces dendrorhous; Affinity chromatography; Invertase; Cell-bound; Phaffia rhodozyma; Electrophoresis; Urease; Yeast; Enzyme; Gel electrophoresis; Xanthophyll; β-Fructofuranosidase; Ultrasonic treatment; Fungi; Organic pigment; Enzymatic activity; Biochemical reaction; Cellobiose; Glycosidases; Microorganism culture; Hydrolases; Fungi Imperfecti; Carotenoid; O-Glycosidases; Thallophyta
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/S0960-8524(01)00121-3

Invertase and urease are enzyme entities highly associated with the cells of the astaxanthin-producer yeast Xanthophyllomyces dendrorhous ( Phaffia rhodozyma) during any stage of its cell growth cycle. In this study cellobiose was a more efficient carbon source than sucrose or its hexose counterparts for invertase expression. Extensive ultrasonication or abrasion with glass pearls were required in order to promote enzyme release. In contrast to the yeast whose growth declines above 27 °C, the released enzymes displayed a higher optimum temperature range when assayed in vitro. Isoforms from both enzymes could be resolved either by FPLC on DEAE-Sepharose or by an affinity approach on immobilized Concanavalin. The zymogram for invertase showed a p I somewhat less acidic than that of the similar enzyme from S. cerevisiae.