BIOL 203 |
| Comparative study of enzymatic properties for native fungal glycosidases revealed some interesting regularities: pH-optima for both alpha- and beta-series of glycosidases from Penicillium canescens and Aspergillus oryzae increase in approximately same order, possibly indicating similarities in the structure of active centers: mannosidase < galactosidase < arabinofuranosidase < fucosidase < glucosidase. The ratio of Michaelis constants [MCR = KM(lactose) / KM(NPG)] with two substrates (lactose and NPG) is approximately constant for certain groups of enzymes. It equals 35±3 and 10±1.5 for the mould and the yeast enzymes respectively. MCR may be interpreted as a relative substrate affinity. Noteworthy, KM for beta-galactosidase is always approximately two times greater than KM for alpha-galactosidase from the same producer. The enzyme preparations were immobilized on modified and non-modified porous silica gel by adsorption and/or covalent binding, and gave highly productive catalysts for the lactose hydrolysis. |
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Enzymes
4:30 PM-6:30 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster
Division of Biological Chemistry |