Chitinase from leaves of sugar beet was purified by (NH4)2SO4 precipitation (20-60%) and fractionated on Sephadex G-120 followed by Sephadex G-200 column chromatography. A 18.9 fold purification of the enzyme with 14.0 ImU/mg specific activity was achieved. The yield of the purified chitinase was 43.4 mg protein (608 ImU) from 100g dry leaves tissues. The prepared enzyme was showing a single protein band on agarose gel electrophoresis. The purified enzyme had been shown to have a M, 64×103 Dalton on the basis of gel filtration on Sephadex G-200 column. Optimum chitinase activity on chitin was recorded in 0.1M acetate buffer, pH 4.5 at 40°C.
PDF Fulltext XML References Citation
How to cite this article
Sanaa T. El-Sayed, Ahmed M. Salem, Abeer N. Shehata and Etidal W. Jwanny, 2000. Chitinase from Leaves of Beta vulgaris and other Higher Plants. Pakistan Journal of Biological Sciences, 3: 250-256.
DOI: 10.3923/pjbs.2000.250.256
URL: https://scialert.net/abstract/?doi=pjbs.2000.250.256
DOI: 10.3923/pjbs.2000.250.256
URL: https://scialert.net/abstract/?doi=pjbs.2000.250.256