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Biotechnology Advances
Vol. 34 (5), 2016, Pages: 874–885

Structural traits and catalytic versatility of the lipases from the Candida rugosa-like family: A review

Jorge Barriuso, María Eugenia Vaquero, Alicia Prieto, María Jesús Martínez

Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain.

Abstract

Lipases and sterol esterases are enzymes with broad biotechnological applications, which catalyze the hydrolysis or synthesis of long-chain acylglycerols and sterol esters, respectively. In this paper, we review the current knowledge on the so-called Candida rugosa-like family of enzymes, whose members display in most cases affinity against the two substrates mentioned above. The family includes proteins with the α/β-hydrolase folding, sharing conserved motifs in their sequences, and common structural features. We will go through their production and purification, relate their described structures and catalytic activity, and discuss the influence of the hydrophobic character of these lipases on their aggregation state and activity. On the basis of the few crystal structures available, the role of each of the functional areas in catalysis will be analyzed. Considering the particular characteristics of this group, we propose their classification as “Versatile Lipases” (EC 3.1.1.x).

Keywords: Lipase; Sterol-esterase; Candida rugosa; Biocatalysts; Hydrophobic enzymes.

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