Understanding Candida rugosa lipases: An overview

Marı́a, Pablo Domı́nguez de; Sánchez-Montero, J.M.; Sinisterra, J. V.; Alcántara, Andrés R.

doi:10.1016/j.biotechadv.2005.09.003

Cited by 207 publications

(93 citation statements)

References 138 publications

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“…However, it must be taken into account that, to the best of our knowledge, the proteins used in the aforementioned examples were commercial samples composed of a mixture of several isoenzymes in different proportions. Since modifications of the fermentation conditions lead to different lipase amounts and (iso)enzymatic profiles, reproducibility of the results could hence be challenging 26. On the other hand, CAL‐A wt is a well‐studied lipase with great potential in biocatalysis due to its high level of overexpression, stability and the possibility of immobilization 21,27.…”

Section: Resultsmentioning

confidence: 99%

Alteration of Chain Length Selectivity of Candida antarctica Lipase A by Semi‐Rational Design for the Enrichment of Erucic and Gondoic Fatty Acids

Zorn

Oroz‐Guinea

Brundiek³

et al. 2018

Adv Synth Catal

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Biotechnological strategies using renewable materials as starting substrates are a promising alternative to traditional oleochemical processes for the isolation of different fatty acids. Among them, long chain mono‐unsaturated fatty acids are especially interesting in industrial lipid modification, since they are precursors of several economically relevant products, including detergents, plastics and lubricants. Therefore, the aim of this study was to develop an enzymatic method in order to increase the percentage of long chain mono‐unsaturated fatty acids from Camelina and Crambe oil ethyl ester derivatives, by using selective lipases. Specifically, the focus was on the enrichment of gondoic (C20:1 cisΔ11) and erucic acid (C22:1 cisΔ13) from Camelina and Crambe oil derivatives, respectively. The pursuit of this goal entailed several steps, including: (i) the choice of a suitable lipase scaffold to serve as a protein engineering template (Candida antarctica lipase A); (ii) the identification of potential amino acid targets to disrupt the binding tunnel at the adequate location; (iii) the design, creation and high‐throughput screening of lipase mutant libraries; (iv) the study of the selectivity towards different chain length p‐nitrophenyl fatty acid esters of the best hits found, as well as the analysis of the contribution of each amino acid change and the outcome of combining several of the aforementioned residue alterations and, finally, (v) the selection and application of the most promising candidates for the fatty acid enrichment biocatalysis. As a result, enrichment of C22:1 from Crambe ethyl esters was achieved either, in the free fatty acid fraction (wt, 78%) or in the esterified fraction (variants V1, 77%; V9, 78% and V19, 74%). Concerning the enrichment of C20:1 when Camelina oil ethyl esters were used as substrate, the best variant was the single mutant V290W, which doubled its content in the esterified fraction from approximately 15% to 34%. A moderately lower increase was achieved by V9 and its two derived triple mutant variants V19 and V20 (27%).

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Section: Resultsmentioning

confidence: 99%

Alteration of Chain Length Selectivity of Candida antarctica Lipase A by Semi‐Rational Design for the Enrichment of Erucic and Gondoic Fatty Acids

Zorn

Oroz‐Guinea

Brundiek³

et al. 2018

Adv Synth Catal

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“…Many microbial extracellular lipases are used for industrial purposes as biocatalysts and Candida species are frequently used to produce hydrolytic enzymes for industrial use [38,39]. For example, C. antartica and C. rugosa secreted lipases are the most frequently used biocatalysts that are involved in detergent industry, biosensor modulation, and even biocatalytic resolution of pharmaceuticals such as antibiotics, virucids, probiotics and non-steroid anti-inflammatory drugs (NSAIDs) [38,40,41]. Thus, fungal secreted lipases are considered beneficial for biotechnological applications.…”

Section: Function Of Fungal Secreted Lipasesmentioning

confidence: 99%

Candida parapsilosis Secreted Lipase as an Important Virulence Factor

Tóth

Vágvölgyi

et al. 2017

CPPS

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Abstract:The prevalence of Candida parapsilosis, an opportunistic human pathogenic fungal species, is increasing at an alarming rate in the hospital environment. Patients at risk for C. parapsilosis infection include those with immunosuppression, such as individuals with cancer, AIDS, and low birth weight premature neonates as well as patients that had undergone abdominal surgery. Neonatal candidiasis caused by C. parapsilosis has been widely reported across the globe. Various reports have shown that, compared to other Candida species, certain C. parapsilosis clinical isolates were less susceptible to antifungals such as amphotericin B, fluconazole, and caspofungin. In addition, some studies have even reported multi-echinocandin or multi-azole resistant strains of C. parapsilosis. C. parapsilosis has several virulence factors that contribute to its capacity for host invasion and among these factors extracellular lipases have a major role in pathogenesis. In this review we have collected all the recent relevant studies that confirm the involvement of secreted lipases in C. parapsilosis pathogenesis, using both in vitro and in vivo models of infection. Of particular note, an available lipase deficient C. parapsilosis strain has been utilized to demonstrate that the lack of secreted lipases decreased virulence, reduced tissue damage, and was less able to survive within phagocytes or mice compared to the wild type. Since fungal secreted lipases have different characteristics than lipolytic enzymes present in humans, C. parapsilosis extracellular lipases may be potential targets for the development of novel antifungal drugs.

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“…Candida antarctica lipase A (CALA) ( 28,29 ) and Geotrichum candidum lipase ( 30 ) were reported to show sn -2 preference during the hydrolysis of TAGs. A review on CALA illustrates the increasing attention being paid to this unique biocatalyst and the many applications that have been developed, especially in the synthesis of structured TAGs ( 31 ). Sn -2-specifi c lipases are particularly interesting for tailoring the FAs at the internal position of structured TAGs.…”

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An ultraviolet spectrophotometric assay for the screening of sn-2-specific lipases using 1,3-O-dioleoyl-2-O-α-eleostearoyl-sn-glycerol as substrate

Mendoza

Rodríguez

Leclaire

et al. 2012

Journal of Lipid Research

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Lipases (triacylglycerol ester hydrolases, EC 3.1.1.3) are lipolytic carboxylester hydrolases that catalyze the hydrolysis of the ester bonds of long-chain triacylglycerols (TAGs). They are widely distributed in microorganisms, plants, and animals ( 1-3 ), where they play an important role in lipid metabolism ( 4,5 ).Because lipases are water-soluble enzymes that hydrolyze insoluble long-chain TAG substrates, the cleavage reaction has to occur at the lipid-water interface ( 6-8 ). The mechanisms involved in the enzymatic lipolysis depend strongly on the mode of organization of the lipid substrate in interfacial structures such as monolayers, micelles, liposomal dispersions, and oil-in-water emulsions. Lipases interact with these lipid complexes, or "super-substrates," via hydrophobic domains that are exposed upon contact as the result of a substrate-induced conformational change, which sometimes has been called "interfacial activation" ( 3, 9 ). The two-dimensional (2-D) nature of this lipase reaction does not obey Michaelis-Menten kinetics and depends critically on the quality of the interface ( 3,8,9 ). Obtaining accurate, i.e., substrate-specifi c, measurements of lipase activity, as well as developing reliable lipase assay

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Understanding Candida rugosa lipases: An overview

Cited by 207 publications

References 138 publications

Alteration of Chain Length Selectivity of Candida antarctica Lipase A by Semi‐Rational Design for the Enrichment of Erucic and Gondoic Fatty Acids

Alteration of Chain Length Selectivity of Candida antarctica Lipase A by Semi‐Rational Design for the Enrichment of Erucic and Gondoic Fatty Acids

Candida parapsilosis Secreted Lipase as an Important Virulence Factor

An ultraviolet spectrophotometric assay for the screening of sn-2-specific lipases using 1,3-O-dioleoyl-2-O-α-eleostearoyl-sn-glycerol as substrate

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