title: Resolution of DL-Phenylglycine by Penicillin G acylase.
abstract: The parameters for complete hydrolysis of L-phenyl acetyl phenylglycine (L-PAPG) using immobilized penicillin G acylase (IMEPGA) were investigated. IMEPGA exhibited maximum activity at pH 8.5 and 50 degrees C. The apparent Km value observed was 10 mM. Quantitative hydrolysis (>97%) of the L-PAPG was achieved within 45 min, at pH 7.8 and 37 degrees C, when 0.5% (w/v) of DL-PAPG was used and the concentration of IMEPGA was 133 IU/gm of DL-PAPG. The IMEPGA was used for 50 cycles.
authors.affiliation: Hindustan Antibiotics Ltd., Pimpri, Pune 411 018, India.
authors.forename: R S
authors.initials: RS
authors.lastname: Kulkarni
authors.forename: U R
authors.initials: UR
authors.lastname: Kalkote
mesh_terms: D004800:Enzymes, Immobilized / Q000378:metabolism*; D005998:Glycine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010399:Penicillin Amidase / Q000302:isolation & purification / Q000378:metabolism*; D011108:Polymers / Q000737:chemistry*; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D011108:Polymers; C008852:2-phenylglycine; D010399:Penicillin Amidase; D005998:Glycine