Color Variants of Aureobasidium pullulans Overproduce Xylanase with Extremely High Specific Activity
- 1 November 1986
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 52 (5) , 1026-1030
- https://doi.org/10.1128/aem.52.5.1026-1030.1986
Abstract
Xylanase activity from naturally occurring color variants of Aureobasidium pullulans was associated with extracellular monomeric proteins of 20 to 21 kilodaltons. Xylanase represented nearly half the total extracellular protein, with a yield of up to 0.3 g of xylanase per liter. The specific activity of partially purified xylanase exceeded 2,000 IU/mg. Xylanase from typically pigmented strains appeared similar to that from color variants with respect to molecular weight, pH and temperature optima, and specific activity of purified (but not crude) enzyme. However, xylanase from typical strains made up only about 1.0% of total extracellular protein. Xylanase from strains of Cryptococcus albidus was associated with abundant proteins of about 43 kilodaltons and showed much lower specific activity.This publication has 13 references indexed in Scilit:
- Silver staining of proteins in polyacrylamide gelsAnalytical Biochemistry, 1981
- Substrate-Binding Site of Endo-1,4-beta-Xylanase of the Yeast Cryptococcus albidusEuropean Journal of Biochemistry, 1981
- Mechanisms of Substrate Digestion by Endo-1,4-beta-Xylanase of Cryptococcus albidus. Lysozyme-Type Pattern of ActionEuropean Journal of Biochemistry, 1981
- Induction and Inducers of Endo‐1,4‐β‐xylanase in the Yeast Cryptococcus albidusEuropean Journal of Biochemistry, 1980
- Xylan‐Degrading Enzymes of the Yeast Cryptococcus albidusEuropean Journal of Biochemistry, 1980
- Xylan-degrading activity in yeasts: Growth on xylose, xylan and hemicellulosesFolia Microbiologica, 1978
- Hemicellulases: Their Occurrence, Purification, Properties, and Mode of ActionAdvances in Carbohydrate Chemistry and Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gelsBiochemical and Biophysical Research Communications, 1967
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951