Effect of Metal Ions on the Hydrolytic and Transesterification Activities of Candida rugosa Lipase

Katiyar, Madhu; Ali, Amjad

doi:10.5650/jos.62.919

Cited by 14 publications

(8 citation statements)

References 17 publications

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“…On the other hand, Hg 2+ has been reported to act like a ROL activity inhibitor suggesting that thiol groups are required for the adequate function of the enzyme [74]. Similar results have been reported with other lipases from Pseudomonas aeruginosa AAU2 [109], Galactomyces geotrichum Y05 [110], Yarrowia lipolytica [111] and Candida rugosa [112]. In addition, no significant effects have been observed with the chelating agent EDTA, indicating that ROL activity is independent of any metal, hence, it is not a metalloprotein [74,104].…”

Section: Biochemical Propertiessupporting

confidence: 78%

Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications

2020

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Lipases are biocatalysts with a significant potential to enable a shift from current pollutant manufacturing processes to environmentally sustainable approaches. The main reason of this prospect is their catalytic versatility as they carry out several industrially relevant reactions as hydrolysis of fats in water/lipid interface and synthesis reactions in solvent-free or non-aqueous media such as transesterification, interesterification and esterification. Because of the outstanding traits of Rhizopus oryzae lipase (ROL), 1,3-specificity, high enantioselectivity and stability in organic media, its application in energy, food and pharmaceutical industrial sector has been widely studied. Significant advances have been made in the biochemical characterisation of ROL particularly in how its activity and stability are affected by the presence of its prosequence. In addition, native and heterologous production of ROL, the latter in cell factories like Escherichia coli, Saccharomyces cerevisiae and Komagataella phaffii (Pichia pastoris), have been thoroughly described. Therefore, in this review, we summarise the current knowledge about R. oryzae lipase (i) biochemical characteristics, (ii) production strategies and (iii) potential industrial applications.

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Section: Biochemical Propertiessupporting

confidence: 78%

Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications

2020

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“…23 Lipase activity can be improved by doping enzymes with metal ions. Katiyar et al 24 found that Ca 2+ could enhance the hydrolytic activity of Candida rugosa lipase (CRL); meanwhile, Cr 3+ and Co 3+ could enhance the transesterification activity of CRL. In another study, Nawani et al 25 reported that Mg 2+ , Na 1+ , and Li 1+ salts increased the hydrolytic activity of lipase of Bacillus J33 by 63, 63, and 23%, respectively.…”

Section: Introductionmentioning

confidence: 99%

Proline-Modified UIO-66 as Nanocarriers to Enhance Candida rugosa Lipase Catalytic Activity and Stability for Electrochemical Detection of Nitrofen

Cheng

Lai

Tan

et al. 2021

ACS Appl. Mater. Interfaces

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Immobilization can be used to improve the stability of lipases and enhances lipase recovery and reusability, which increases its commercial value and industrial applications. Nevertheless, immobilization frequently causes conformational changes of the lipases, which decrease lipase catalytic activity. in the present work, we synthesized UIO-66 and grafted UIO-66 crystals with proline for immobilization of Candida rugosa lipase (CRL). As indicated by steady-state fluorescence microscopy, grafting of proline onto UIO-66 crystals induced beneficial conformational change in CRL.

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“…PET-ases from Thermobifida species are also Ca 2+ -dependent, especially in terms of their thermal stability [ 34 ]. The positive effect of Ca 2+ on both activity and stability could be found in most of the reports [ 35 ]. The observed negative effect of the chelating agent EDTA confirmed that the enzyme activity depended on the Ca 2+ presence in the active site.…”

Section: Discussionmentioning

confidence: 91%

A Thermostable Lipase Isolated from Brevibacillus thermoruber Strain 7 Degrades Ɛ-Polycaprolactone

Atanasova

Paunova-Krasteva

Kambourova

et al. 2023

BioTech

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The tremendous problem with plastic waste accumulation has determined an interest in biodegradation by effective degraders and their enzymes, such as thermophilic enzymes, which are characterized by high catalytic rates, thermostability, and optimum temperatures close to the melting points of some plastics. In the present work, we report on the ability of a thermophilic lipase, by Brevibacillus thermoruber strain 7, to degrade Ɛ-polycaprolactone (PCL), as well as the enzyme purification, the characterization of its physicochemical properties, the product degradation, and its disruptive effect on the PCL surface. The pure enzyme showed the highest reported optimum temperature at 55 °C and a pH of 7.5, while its half-life at 60 °C was more than five hours. Its substrate specificity referred the enzyme to the subgroup of lipases in the esterase group. A strong inhibitory effect was observed by detergents, inhibitors, and Fe3+ while Ca2+ enhanced its activity. The monomer Ɛ-caprolactone was a main product of the enzyme degradation. Similar elution profiles of the products received after treatment with ultra-concentrate and pure enzyme were observed. The significant changes in PCL appearance comprising the formation of shallower or deeper in-folds were observed after a week of incubation. The valuable enzyme properties of the lipase from Brevibacillus thermoruber strain 7, which caused a comparatively quick degradation of PCL, suggests further possible exploration of the enzyme for effective and environment-friendly degradation of PCL wastes in the area of thermal basins, or in thermophilic remediation processes.

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Effect of Metal Ions on the Hydrolytic and Transesterification Activities of Candida rugosa Lipase

Cited by 14 publications

References 17 publications

Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications

Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications

Proline-Modified UIO-66 as Nanocarriers to Enhance Candida rugosa Lipase Catalytic Activity and Stability for Electrochemical Detection of Nitrofen

A Thermostable Lipase Isolated from Brevibacillus thermoruber Strain 7 Degrades Ɛ-Polycaprolactone

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