Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica

Siódmiak, Tomasz; Haraldsson, Guđmundur G.; Dulęba, Jacek; Ziegler-Borowska, Marta; Siódmiak, Joanna; Marszałł, Michał Piotr

doi:10.3390/catal10080876

Cited by 15 publications

(29 citation statements)

References 71 publications

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“…Furthermore, in the case of immobilized enzymes, besides the support nature and structure, the reaction media strongly influenced the enzyme interaction with the inert support, modifying their catalytic properties, as recently presented by Siodmiak. 71 Four polar aprotic and nonpolar solvents were used in the study considering the biocatalyst stability. Based on our recent study, when n -hexane was found as the optimal solvent for the EKR of some racemic heteroaryl-ethanols mediated by CaL-B immobilized on chitosan–magnetic nanoparticles, 16 the stability of this new bioconjugate containing chitosan and the same enzyme in various solvents (dichloromethane – DCM, tetrahydrofuran – THF, chloroform and n -hexane) was further studied (see section 2.3.1).…”

Section: Resultsmentioning

confidence: 99%

A robust and efficient lipase based nanobiocatalyst for phenothiazinyl-ethanol resolution

et al. 2023

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Section: Resultsmentioning

confidence: 99%

A robust and efficient lipase based nanobiocatalyst for phenothiazinyl-ethanol resolution

et al. 2023

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“…Hence, optimum temperature reported here were slightly different than previous studies. For example, at pH 7.4, an optimum temperature of 55˚C of for CalB was reported [58] while at pH 8.0, purified CalB demonstrated an optimum temperature of 52˚C [42].…”

Section: Plos Onementioning

confidence: 99%

Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B

Jaito,

Kaewsawat,

Phetlum

et al. 2023

PLoS ONE

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Here we employed sequence-based and structure-based screening for prospecting lipases that have structural homolog to Candida antarctica lipase B (CalB). CalB, a widely used biocatalyst, was used as structural template reference because of its enzymatic properties. Structural homolog could aid in the discovery of novel wild-type enzymes with desirable features and serve as a scaffold for further biocatalyst design. The available metagenomic data isolated from various environments was leveraged as a source for bioprospecting. We identified two bacteria lipases that showed high structural similarity to CalB with <40% sequence identity. Partial purification was conducted. In comparison to CalB, the enzymatic characteristics of two potential lipases were examined. A candidate exhibited optimal pH of 8 and temperature of 50°C similar to CalB. The second lipase candidate demonstrated an optimal pH of 8 and a higher optimal temperature of 55°C. Notably, this candidate sustained considerable activity at extreme conditions, maintaining high activity at 70°C or pH 9, contrasting with the diminished activity of CalB under similar conditions. Further comprehensive experimentation is warranted to uncover and exploit these novel enzymatic properties for practical biotechnological purposes.

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“…CalB is expected to be a non-toxic and renewable energy source. It has the highest catalytic activity at neutral pH and 45 °C [ 12 , 13 , 14 ]. However, CalB is water soluble, which makes it highly sensitive to organic solvents, leading to reduced reaction efficiency [ 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

Thermally Stable and Reusable Silica and Nano-Fructosome Encapsulated CalB Enzyme Particles for Rapid Enzymatic Hydrolysis and Acylation

Jang

Sohn

Chang

2023

IJMS

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This study reports the preparation of silica-coated and nano-fructosome encapsulated Candida antarctica lipase B particles (CalB@NF@SiO2) and a demonstration of their enzymatic hydrolysis and acylation. CalB@NF@SiO2 particles were prepared as a function of TEOS concentration (3–100 mM). Their mean particle size was 185 nm by TEM. Enzymatic hydrolysis was performed to compare catalytic efficiencies of CalB@NF and CalB@NF@SiO2. The catalytic constants (Km, Vmax, and Kcat) of CalB@NF and CalB@NF@SiO2 were calculated using the Michaelis–Menten equation and Lineweaver–Burk plot. Optimal stability of CalB@NF@SiO2 was found at pH 8 and a temperature of 35 °C. Moreover, CalB@NF@SiO2 particles were reused for seven cycles to evaluate their reusability. In addition, enzymatic synthesis of benzyl benzoate was demonstrated via an acylation reaction with benzoic anhydride. The efficiency of CalB@NF@SiO2 for converting benzoic anhydride to benzyl benzoate by the acylation reaction was 97%, indicating that benzoic anhydride was almost completely converted to benzyl benzoate. Consequently, CalB@NF@SiO2 particles are better than CalB@NF particles for enzymatic synthesis. In addition, they are reusable with high stability at optimal pH and temperature.

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Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica

Cited by 15 publications

References 71 publications

A robust and efficient lipase based nanobiocatalyst for phenothiazinyl-ethanol resolution

A robust and efficient lipase based nanobiocatalyst for phenothiazinyl-ethanol resolution

Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B

Thermally Stable and Reusable Silica and Nano-Fructosome Encapsulated CalB Enzyme Particles for Rapid Enzymatic Hydrolysis and Acylation

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