Biotechnological relevance of the lipase A from Candida antarctica

Monteiro, Rodolpho R. C.; Virgen-Ortíz, José J.; Berenguer-Murcia, Ángel; Rocha, Thays N. da; Santos, José Cleiton Sousa dos; Alcántara, Andrés R.; Fernández-Lafuente, Roberto

doi:10.1016/j.cattod.2020.03.026

Cited by 82 publications

(45 citation statements)

References 287 publications

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“…The results showed that Candida tropicalis could produce lipase. It is also found that another type of Candida, Candida Antarctica, and Candida parapsilosis, also has lipase (Ribas et al, 2019;Monteiro et al, 2020).…”

Section: Discussionmentioning

confidence: 96%

The Ability of Soil Candida albicans Secreted Potential Protease and Lipase

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et al. 2020

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Soil microorganisms have one function as a source of producing extracellular enzymes, especially the lipase and protease enzymes used to catalysis a chemical process. Protease is one of the enzymes with the best prospects for development because it is quite widely applied in various industries, both food and non-food. Most of the lipases used in the food and pharmaceutical industries come from microorganisms. This study aimed to look at the extracellular enzyme activity of Candida tropicalis isolated from the soil of the medicinal plantations of the Faculty of Pharmacy Unjani. The study was conducted through a fermentation process to obtain bioactive metabolites of isolates. The result was analyzed using ANOVA within a 5% interval of confidence, continuing with PostHoc. Based on these results, the Candida tropicalis metabolite giving the best proteolytic index value (0,6556 ± 0,0090) U/mL. The results showed that the metabolite isolate of Candida tropicalis had the highest activity, amounting to 5,776 ± 0,495 U/mL. The best results of lipolytic index value (0,394 ± 0,053) U/mL. The Candida tropicalis metabolites produced the highest lipase enzyme after nine days of fermentation in 5.2917±0,0167 U/mL.

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Section: Discussionmentioning

confidence: 96%

The Ability of Soil Candida albicans Secreted Potential Protease and Lipase

Puspadewi

Adirestuti

Dewi

et al. 2020

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“…[9,32,[58][59][60][61][62][63][64][65][66][67][68][69][70]. As lipases are one of the most (if not the most) frequently used biocatalysts [71][72][73][74][75][76], it is not surprising to find a plethora of immobilization protocols described for these enzymes [77][78][79][80][81][82]. Interestingly, in many instances some strategies to improve enzyme features are combined.…”

Section: Enzymatic Biocatalysismentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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“…In the case of lipases, lipases immobilized on octyl agarose or glutaraldehyde-amino agarose have been employed, as this seems to alter the lipase features response to changes in the medium as stated above [ 56 , 57 , 58 , 64 , 65 , 67 , 68 , 69 , 70 , 72 , 73 , 74 , 76 ]. As lipases, this study includes the lipases A and B from Candida antarctica (CALA and CALB) [ 82 , 83 , 84 , 85 , 86 , 87 , 88 ], and the lipases from Candida rugosa (CRL) [ 89 ] and from Rhizomucor miehei (RML) [ 90 , 91 ]. Moreover, Eversa ® Transform 2.0 (EVT), a recombinant commercial enzyme that has been improved from the initial lipase from Thermomyces lanuginosus to improve their performance in biodiesel production [ 92 , 93 ] has been also studied.…”

Section: Introductionmentioning

confidence: 99%

Effect of Concentrated Salts Solutions on the Stability of Immobilized Enzymes: Influence of Inactivation Conditions and Immobilization Protocol

et al. 2021

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This paper aims to investigate the effects of some salts (NaCl, (NH4)2SO4 and Na2SO4) at pH 5.0, 7.0 and 9.0 on the stability of 13 different immobilized enzymes: five lipases, three proteases, two glycosidases, and one laccase, penicillin G acylase and catalase. The enzymes were immobilized to prevent their aggregation. Lipases were immobilized via interfacial activation on octyl agarose or on glutaraldehyde-amino agarose beads, proteases on glyoxyl agarose or glutaraldehyde-amino agarose beads. The use of high concentrations of salts usually has some effects on enzyme stability, but the intensity and nature of these effects depends on the inactivation pH, nature and concentration of the salt, enzyme and immobilization protocol. The same salt can be a stabilizing or a destabilizing agent for a specific enzyme depending on its concentration, inactivation pH and immobilization protocol. Using lipases, (NH4)2SO4 generally permits the highest stabilities (although this is not a universal rule), but using the other enzymes this salt is in many instances a destabilizing agent. At pH 9.0, it is more likely to find a salt destabilizing effect than at pH 7.0. Results confirm the difficulty of foreseeing the effect of high concentrations of salts in a specific immobilized enzyme.

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Biotechnological relevance of the lipase A from Candida antarctica

Cited by 82 publications

References 287 publications

The Ability of Soil Candida albicans Secreted Potential Protease and Lipase

The Ability of Soil Candida albicans Secreted Potential Protease and Lipase

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

Effect of Concentrated Salts Solutions on the Stability of Immobilized Enzymes: Influence of Inactivation Conditions and Immobilization Protocol

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