title: Modification of L-asparaginase from Erwinia carotovora using human serum albumin.
abstract: L-Asparaginase from Erwinia carotovora was modified by coupling with human serum albumin. The complex retained 80% of the activity, shifted the pH optima to 7.0, and lowered the Km value by tenfold, but the temperature optima remained at 37 degrees C. It was also found to be heat-resistant.
authors.affiliation: Food Technology and Enzyme Engineering Division, Bhabha Atomic Research Centre, Bombay, India.
authors.forename: D P
authors.initials: DP
authors.lastname: Nerkar
authors.forename: M
authors.initials: M
authors.lastname: Gangadharan
mesh_terms: D001215:Asparaginase / Q000302:isolation & purification / Q000378:metabolism*; D004800:Enzymes, Immobilized; D004885:Erwinia / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012709:Serum Albumin / Q000378:metabolism*; D012995:Solubility; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D012709:Serum Albumin; D001215:Asparaginase