A phytate-degrading enzyme (myo-inositol hexakisphosphate phosphohydrolase) has been puriยฎed about 5,400-fold from germinated oat seedlings to apparent homogeneity. The molecular mass of the native monomeric enzyme was estimated to be about 67 kDa. Optimal pH for degradation of phytate was 5.0 and t
Rapid purification and characterization of a novel heparin degrading enzyme from Acinetobacter calcoaceticus
โ Scribed by Jaspreet Banga; C.K.M. Tripathi
- Publisher
- Elsevier
- Year
- 2009
- Tongue
- English
- Weight
- 359 KB
- Volume
- 26
- Category
- Article
- ISSN
- 1871-6784
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Degradation of the proteoglycan matrix is considered an essential step in the process of calcification in the growth plate. This laboratory has just described the presence of a protease in human growth plate cartilage that degrades proteoglycan at neutral pH. We report here the isolation, partial pu