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Published:
Feb 21, 2014Keywords:
Thiamine thiaminase Anaphe venata kinetics properties
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How to Cite
Okonji, R., Bamitale, K., & Balogun, R. (2014). Biochemical properties of thiaminase from <i>Anaphe venata</i> Burtler. African Journal of Biotechnology, 11(20), 4543–4550. https://doi.org/10.4314/ajb.v11i20.
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Main Article Content
Biochemical properties of thiaminase from Anaphe venata Burtler
Abstract
Anaphe venata contain a high level activity of thiaminase enzyme. The enzyme was partially purified through Biogel P-200 gel filtration chromatography. The proximate analysis of A. venata showed a high protein content of 28.00%, crude fibre content of 6.37 and crude fat content of 14.26. The native molecular weight of the enzyme was found to be 85,000 daltons. The overall results indicates that thiaminase from A. venata prefers thiamine as substrate with a Km value of 0.35 mM as compared to 24.51 mM of aniline. A pH optima of 6.0 was obtained for the enzyme. The temperature optimum was found to be 60°C with activation energy values of 5.01 and 12.5 Kcal.
Key words: Thiamine, thiaminase, Anaphe venata, kinetics properties.
Key words: Thiamine, thiaminase, Anaphe venata, kinetics properties.
