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Purification And Characterization Of An Extracellular Chitinase From Rhizopus Oryzae, Wei-Ming Chen, Ching-San Chen, Shann-Tzong Jiang
Purification And Characterization Of An Extracellular Chitinase From Rhizopus Oryzae, Wei-Ming Chen, Ching-San Chen, Shann-Tzong Jiang
Journal of Marine Science and Technology
A chitinase with about 50 kDa of molecular mass from Rhizopus oryzae was purified to electrophoretical homogeneity after DEAE Sepharose and Sephacryl S-200 chromatographs, with specific activity of 165.2 U/mg, 19.7% recovery and 4.3-fold of purification. It had optimal pH and temperature at 5.5-6.0 and 60°C, respectively, and was stable at pH 5.0-8.5 and below 50°C. Ca2+, Sr2+, Ba2+, Mn2+, Co2+ and β-Me enhanced chitinase activity by 10-48% ,whereas Hg2+ and SDS strongly inhibited enzyme activity. This enzyme was identified that might be with both chitinolytic and amylolytic activity. According to the result of LC-MS/MS analysis, 4 identified amino acid …
Purification And Characterization Of Acidic Protease From Aspergillus Oryzae Bcrc 30118, Li-Jung Yin, Ya-Hui Chou, Shann-Tzong Jiang
Purification And Characterization Of Acidic Protease From Aspergillus Oryzae Bcrc 30118, Li-Jung Yin, Ya-Hui Chou, Shann-Tzong Jiang
Journal of Marine Science and Technology
The acidic protease was purified from 4-day cultivation of Aspergillus oryzae BCRC 30118 by DEAE Sephacel and Sephacryl S-200 HR chromatographs. The specific activity, yield and purification fold were 117.62 kU/mg, 15.1% and 6.6, respectively. The molecular weight (M) was 41.0 kDa, while the optimal pH and temperature were 3.0 and 60°C, respectively. It was stable at pH 3.0-6.0 and 4-35°C. However, it was inhibited by Fe2+, Hg2+, Fe3+ and pepstatin A, and slightly by leupeptin and TPCK. According to substrate specificity and inhibitor study, it was a cysteine protease with activation energy of 37.5 kcal/mol. Its Km, Vmax, Kcat …