Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition

Characterization of smallest active monomeric penicillin V acylase from new source: A yeast, Rhodotorula aurantiaca (NCIM 3425)

“…Presence of enzyme in water organic cosolvent mixture may affect its catalytic properties and stability [26]. Results obtained by us from the effect of organic solvents on PVA activity are different from the results described by Arroyo et al [11,12]. They have demonstrated activation of extracellular penicillin V acylase from S. lavendulae in presence of organic solvents such as alcohols and aprotic polar solvents however it is not true in case of Ra-PVA.…”

“…Penicillin V acylase has been purified from B. sphaericus, E. aroideae, B. subtilis and S. lavendulae and the biochemical properties such as molecular weight, optimum pH, optimum temperature, Michaelis Menten constant (K m ) and inhibition kinetics are studied for various PVA preparations [6][7][8][9][10]. Penicillin V acylase from S. lavendulae has been extensively studied by Torres and Arroyo [10][11][12].…”

Low temperature effect on production of ampicillin and cephalexin in ethylene glycol medium with immobilized penicillin acylase

“…Polyols are especially suitable, since they strongly depress water activity and increase enzyme stability, those effects being correlated with the number of hydroxyl groups in the polyol moiety [16,22,23]. In the enzymatic synthesis of ampicillin and cephalexin with immobilized penicillin acylase, ethylene glycol (EG) and 1,2-propanediol (PD) were selected as the best among several poloyols tested [20,24].…”

Overexpression of Penicillin V Acylase from Streptomyces lavendulae and Elucidation of Its Catalytic Residues

“…PVA from Streptomyces lavendulae ATCC 13664 (SlPVA) is an extracellular enzyme which has been exhaustively characterized (7)(8)(9)(10) and immobilized (11,12) due to its ability to hydrolyze very efficiently PV and other natural aliphatic penicillins that contaminate PV and usually reduce 6-APA yield at the end of the process. The broad substrate specificity of SlPVA allows this enzyme to hydrolyze several penicillins with aliphatic acyl chains, e.g., 3-hexenoyl-penicillin (penicillin F [PF]), hexanoyl-penicillin (penicillin dihydro-F [PdF]), and octanoyl-penicillin (penicillin K [PK]), as the catalytic constant for PK was even higher than that for PV (13).…”