Enzymatic biodiesel: Challenges and opportunities

This review describes how the versatile Candida rugosa lipases (CRL) have extended the frontiers of biotechnology. As evidenced by the current literature, CRL claims more applications than any other biocatalyst. This review comprises a detailed discussion on the molecular biology of CRL, its versatile catalytic reactions, broad specificities and diverse immobilization strategies. It also discusses its role in the food and flavour industry, the production of ice cream and single cell protein, biocatalytic resolution of life-saving pharmaceuticals, carbohydrate esters and amino acid derivatives unobtainable by conventional chemical synthesis, potent biocide making, biosensor modulations, eco-friendly approach and bioremediation, biosurfactants in detergent making, and recently, cosmetics and perfumery. ? 1998 John Wiley & Sons, Ltd.

Candida rugosa Lipases: Molecular Biology and Versatility in Biotechnology

(1999). Detection and Measurement of Microbial Lipase Activity: A Review. Critical Reviews in Food Science and Nutrition: Vol. 39, No. 2, pp. 165-187.

Detection and measurement of microbial lipase activity: a review.

Cloning, expression and characterization of a cDNA encoding a lipase from Rhizopus delemar.

The complete purification and characterization of an extracellular lipase (acylglycerol acylhydrolase, EC 3.1.1.3) fromR. delemar is described. The final product was homogeneous as judged by electrophoresis in denaturing polyacrylamide gels and by isoelectric focusing, and was shown by means of an activity stain to be lipolytic. The purified enzyme had a monomer molecular weight of 30,300, an isoelectric point of 8.6, and approximately one monosaccharide moiety per molecule.N-Terminal sequence data (28 residues) and the amino acid composition of the lipase indicated that it corresponds to the product of a lipase-encoding cDNA previously isolated fromR. delemar. Optimal activity occurred between pH 8.0 and 8.5. The activity and stability of the enzyme were maximum at 30°C. Divalent cations were required for activity, with barium, calcium and manganese conferring maximum activity. Activation by calcium was maximal at and above 10 mM. The lipase was not inactivated by reducing agents, sodium fluoride or phenylmethlsufonyl fluoride. It was resistant toN-ethylmaleimide, and inactivated byp-chloromercuribenzoic acid in a manner which was not reversed by cysteine.

Purification and characterization of an extracellular lipase from the fungusRhizopus delemar

Revue bibliographique sur l'activite lipolytique des microorganismes (bacteries, moisissures notamment) et la specificite des lipases vis-a-vis du substrat. Applications technologiques

H. Sztajer

Papers

Microbial lipases in biotechnology