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

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).

An alkaline and surfactant-tolerant lipase from Trichoderma lentiforme ACCC30425 with high application potential in the detergent industry

“…In addition, the lipase activity is also related to the size and orientation of the channel. For example, the lipase from Aspergillus niger having a narrow and curved channel shows relatively low activity, while those from Ophiostoma piceae , Nectria haematococca and Trichoderma reesei have straightforward and wider channels and much higher activities (Barriuso et al 2016 ).…”

LIP4 gene expression from Candida viswanathii strain

“…True lipases display a hydrophobic lid structure on active-site that regulate the activity mechanism in the presence of interface oil-water, which rearranges its position leaving an open gate to the active center. Then, the position of the lid marks the difference between the open (active) or closed (inactive) forms of these proteins [21,22]. On the other hand, Fikers et al [23] and Lotti et al [24] reported the repression of lipase production caused by glucose from culture both.…”

Kinetic studies of partially purified lipase from marine actinomycete streptomyces acrimycini ngp 1

“…In reality, a criteria used to recognize these two kinds of catalysts, i.e., actuation by the nearness of an interface, additionally called "interfacial initiation," was discovered unacceptable for the arrangement of such proteins as a few lipases didn't show such marvel. Prominent cases of this phenomenon are Lip4 from Candida rugosa (Barriuso et al, 2016) and Candida antarctica B (Zisis et al, 2016). In addition, lipase and esterase accord themes portrayed by PROSITE database (Hulo et al, 2006).…”