Purification and characterization of a glycerol oxidase from Penicillium sp. TS-622.
A novel extracellular glycerol oxidase was purified 39-fold from wheat bran culture of a soil-isolated Penicillium strain TS-622 with an overall yield of 3%. The addition of Triton X-100 into the extraction buffer improved the extraction yield by 90 times, indicating that the enzyme is bound to the cell surface. The molecular weight of this enzyme was 400,000 as determined by size-exclusion high-performance liquid chromatography. The optimum pH was from 6 to 7 and the optimum temperature was 45 degrees C. This enzyme showed high specificity toward dihydroxyacetone and glycerol. It was inhibited by KCN, NaN3, and hydroxylamine.
Lin
S F
SF
Department of Bioengineering, Tatung Institute of Technology, Taipei, Taiwan, Republic of China.
Chiou
C M
CM
Tsai
Y C
YC
D002851:Chromatography, High Pressure Liquid; D003470:Culture Media; D003902:Detergents / Q000494:pharmacology; D004098:Dihydroxyacetone / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D004795:Enzyme Stability; D005110:Extracellular Space / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000302:isolation & purification; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000302:isolation & purification*; D013696:Temperature
D003470:Culture Media; D003902:Detergents; D004791:Enzyme Inhibitors; D008565:Membrane Proteins; D008670:Metals; D013401:Sugar Alcohol Dehydrogenases; C036131:glycerol oxidase; D004098:Dihydroxyacetone