Purification and Some Properties of Lipase Produced byPseudomonas fragi22.39 B

Catalytic potential of a poly(AAc‐co‐HPMA‐cl MBAm)‐matrix‐immobilized lipase from a thermotolerant Pseudomonas aeruginosa MTCC‐4713

“…The presence of ionizable salts of metals as well as nonmetals is likely to cause structural perturbation(s) at the catalytic site of lipase. Interestingly, both divalent‐ (such as Ca 2+ , Ba 2+ , Mg 2+ , Mn 2+ , and Hg 2+ ) as well as monovalent cations (Na + and K + ) are strong modulators of microbial lipase activity 15, 38–45. In the present study, cations of some of the metals (Hg 2+ , Al 3+ , and Fe 3+ ) as well as a nonmetal (NH 4 + ) were found to modulate lipase activity of P. aeruginosa .…”

Biogeneration of ethyl valerate by whole cells of Pseudomonas fragi CRDA 037 in aqueous medium

“…The optimal pH for the biotransformation of valeric acid and ethanol by whole cells of P. fragi was estimated to range from pH 8 to pH 9. Stead (1986) indicated that the pH optima of lipases from different strains of P. fiagi were in the range of pH 7.0 to pH 8.9 whereas Nishio et al (1987) reported that the maximal activity was at pH 9. The overall of these results indicated that the optimal range of pH for esterifying activity of whole cells of P. fragi is similar to that for the hydrolytic activity of lipase.…”

Cloning and Nucleotide Sequence of Thermostable Lipase Gene fromPseudomonas fluorescensSIK W1

“…Several thermostable lipases from thermostable fungi such as Humicola lanuginosa 34 ) and from the genus Pseudomonas such as P. fluorescens,35) Pseudomonas sp. KWI-56,36) and P. fragi 37 ) have been reported. The use of the thermostable microbial lipases in the oleochemical industry may provide advantages of decreased fluid viscosity and increased lipid solubility at high temperature.…”