Some Properties of Extracellular Acetylxylan Esterase Produced by the Yeast Rhodotorula mucilaginosa.

Autor: Lee H; Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A OR6., To RJ, Latta RK, Biely P, Schneider H
Jazyk: angličtina
Zdroj: Applied and environmental microbiology [Appl Environ Microbiol] 1987 Dec; Vol. 53 (12), pp. 2831-4.
DOI: 10.1128/aem.53.12.2831-2834.1987
Abstrakt: The red yeast Rhodotorula mucilaginosa produced an esterase that accumulated in the culture supernatant on induction with triacetin. The enzyme was specific for substrates bearing an O-acetyl group, but was relatively nonspecific for the rest of the molecule, which could consist of a phenol, a monosaccharide, a polysaccharide, or an aliphatic alcohol. The esterase was more active against acetylxylan and glucose beta-d-pentaacetate than were a number of esterases from plant and animal sources, when activities on 4-nitrophenyl acetate were compared. The enzyme exhibited Michaelis-Menten kinetics and was active over a broad pH range (5.5 to 9.2), with an optimum between pH 8 and 10. In addition, the enzyme retained its activity for 2 h at 55 degrees C. The yeast that produced the enzyme did not produce xylanase and, hence, is of interest for the production of acetylxylan esterase that is free of xylanolytic activity.
Databáze: MEDLINE