The Tannase from red yeast Rhodotorula glutinis: Purification and characterization
Document Type
Article
Publication Date
3-1-2024
Abstract
The tannase enzyme was successfully purified to homogeneity from the culture broth of red yeast strain Rhodotorula glutinis DB2 in a three-tandem step involving ultrafiltration (5 kDa and 100 kDa systems), Sephadex G-200 gel filtration chromatography, and DEAE Sepharose CL-4B anion exchange chromatography. The purified tannase appeared to be homogeneous on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The purified tannase had a specific activity of 3.33 U mg(-1), with a 1.3% recovery and overall purification of 302-fold. The molecular mass of the tannase estimated by SDS-PAGE was about 73 kDa. The tannase had an optimum pH of 6.0 and an optimum temperature of 40 degrees C. The most stable pH was 7.0, and the enzyme was stable up to 40 degrees C. One mmol L-1 of Fe3+, Sr2+, Na+, and Pb2+ were found to promote tannase activity, whilst 1.0 mmol L-1 of Ba2+, Ca2+, Mg2+, Zn2+, Hg+, Ag+, Co2+, Fe2+, Mn2+, Cu2+, Cd-2+, Al3+, K+, Ni2+, and Li+ inhibited tannase activity.
Keywords
Tannase, Rhodotorula glutinis, Red yeast, Purification, Characterization
Divisions
universiti
Funders
Universiti Sains Malaysia
Publication Title
Biocatalysis and Biotransformation
Volume
42
Issue
2
Publisher
Taylor and Francis Ltd.
Publisher Location
2-4 PARK SQUARE, MILTON PARK, ABINGDON OR14 4RN, OXON, ENGLAND