Free and immobilized glucose isomerase from Streptomyces phaeochromogenes.
Properties were determined of the glucose isomerase from Streptomyces phaeochromogenes NRRL B-3559. The enzyme exhibited a temperature optimum of 80 C and a pH optimum of about 8. The effect of various buffers on activity of the enzyme and the optimum pH were studied. Michaelis constants for glucose and Mg(2+) were 0.25 and 0.025 m, respectively. Co(2+) enhanced enzyme activity. A functional polyacrylamide-entrapped glucose isomerase was prepared. The conditions for entrapment and use of the bound enzyme were examined.
D000179:Acrylates; D002021:Buffers; D011232:Chemical Precipitation; D003035:Cobalt / Q000494:pharmacology; D005632:Fructose / Q000096:biosynthesis; D005782:Gels; D005947:Glucose / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007535:Isomerases / Q000302:isolation & purification / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D010710:Phosphates; D000644:Quaternary Ammonium Compounds; D013302:Streptomyces / Q000201:enzymology* / Q000378:metabolism; D013431:Sulfates; D013696:Temperature; D014325:Tromethamine
D000179:Acrylates; D002021:Buffers; D005782:Gels; D010710:Phosphates; D000644:Quaternary Ammonium Compounds; D013431:Sulfates; D014325:Tromethamine; D005632:Fructose; D003035:Cobalt; D007535:Isomerases; D008274:Magnesium; D005947:Glucose