Solvent-dependent activity of Candida antarctica lipase B and its correlation with a regioselective mono aza-Michael addition - experimental and molecular dynamics simulation studies

Nazarian, Zohreh; Arab, Seyed Shahriar

doi:10.1016/j.heliyon.2022.e10336

Cited by 6 publications

(2 citation statements)

References 46 publications

(47 reference statements)

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“…While the predictive structures showed high accuracy that most regions exhibited a per-residue confidence metric (pLDDT) >90, the MD simulation was also conducted to evaluate structural stability at optimum temperature of CalB (50˚C) [50]. The RMSD of CalB and SeqB PLOS ONE remained stable at below 2.5 Å during the whole simulation period (Fig 3).…”

Section: (S1 Table and S3 Fig)mentioning

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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Section: (S1 Table and S3 Fig)mentioning

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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“…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 ]. Furthermore, it is difficult to store CalB for a long time.…”

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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Candida antarctica lipase B performance in organic solvent at varying water activities studied by molecular dynamics simulations

Tjørnelund,

Vind,

Brask

et al. 2023

Computational and Structural Biotechnology Journal

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Solvent-dependent activity of Candida antarctica lipase B and its correlation with a regioselective mono aza-Michael addition - experimental and molecular dynamics simulation studies

Cited by 6 publications

References 46 publications

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

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

Candida antarctica lipase B performance in organic solvent at varying water activities studied by molecular dynamics simulations

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