alpha-chymotrypsin has been researched along with stachyose* in 1 studies
1 other study(ies) available for alpha-chymotrypsin and stachyose
| Article | Year |
|---|---|
A protease-resistant α-galactosidase from Pleurotus djamor with broad pH stability and good hydrolytic activity toward raffinose family oligosaccharides.
An acidic α-galactosidase designated as PDGI (Pleurotus djamor α-galactosidase) was purified to homogeneity with 290-fold purification and a specific activity of 52.18 units/mg by means of ion exchange chromatography and gel filtration chromatography. PDGI is a monomeric protein exhibiting a molecular mass of 60kDa in SDS-PAGE and gel filtration. The optimum pH and temperature of the enzyme with pNPGal as substrate were 5.0 and 53.5°C, respectively. It displayed great pH stability within the pH range 3.0-10.0. Besides, the enzyme harbored remarkable resistance to acid protease and varying degrees of tolerance to other proteases: trypsin>collagenase Type-I>α-chymotrypsin neutral protease>proteinaseK. It was strongly inhibited by K Topics: alpha-Galactosidase; Amino Acid Sequence; Chymotrypsin; Enzyme Stability; Fungal Proteins; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Metals; Molecular Weight; Oligosaccharides; Pleurotus; Raffinose; Substrate Specificity | 2017 |