Ong, Chong-Boon and Ibrahim, Darah and Kassim, Mohd Jain Noordin Mohd (2024) The Tannase from red yeast Rhodotorula glutinis: Purification and characterization. Biocatalysis and Biotransformation, 42 (2). pp. 110-117. ISSN 1024-2422, DOI https://doi.org/10.1080/10242422.2022.2136523.
Full text not available from this repository.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.
| Item Type: | Article |
|---|---|
| Funders: | Universiti Sains Malaysia |
| Uncontrolled Keywords: | Tannase; Rhodotorula glutinis; Red yeast; Purification; Characterization |
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
| Divisions: | Universiti Malaya |
| Depositing User: | Ms. Juhaida Abd Rahim |
| Date Deposited: | 13 Aug 2024 03:08 |
| Last Modified: | 13 Aug 2024 03:08 |
| URI: | http://eprints.um.edu.my/id/eprint/46093 |
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