Highly efficient and regioselective acylation of arbutin catalyzed by lipase from Candida sp.

Jiang, Liyan; Xie, Xiaoguang; Yang, Hong; Wu, Zhuofu; Wang, Haoran; Yang, Fengjuan; Wang, Lei; Wang, Zhi

doi:10.1016/j.procbio.2015.02.014

Cited by 11 publications

(3 citation statements)

References 43 publications

(51 reference statements)

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“…The enzyme activity (μmol/mg/h) was defined as the amount (μmol) of the arbutin ester produced per hour per milligram of enzyme. The product was purified and characterized by NMR according to our previous research (32). Each experiment was performed in triplicates to obtain the average values.…”

Section: Regioselective Acylation Of Arbutinmentioning

confidence: 99%

Fabrication of a nano-biocatalyst for regioselective acylation of arbutin

Zheng

Xie

Wang

et al. 2018

Green Chemistry Letters and Reviews

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A nano-biocatalyst has been successfully prepared via coordination between zinc ion and the nitrogen atoms of the amide groups in the Candida sp. 99-125 lipase. The as-prepared nanoparticle has an excellent hierarchical structure with a large number of separate petals. In regioselective acylation of arbutin, the nano-biocatalyst showed enhanced enzyme activities to about 4.3-folds than the free enzyme. Meanwhile, the prepared nano-biocatalyst exhibited good operational reusability and only about 6% of enzyme activity has lost during 10 continuous reaction-recycles.

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Section: Regioselective Acylation Of Arbutinmentioning

confidence: 99%

Fabrication of a nano-biocatalyst for regioselective acylation of arbutin

Zheng

Xie

Wang

et al. 2018

Green Chemistry Letters and Reviews

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“…Many polyphenols commonly exist in the form of glycosides . The acylation of these molecules with different fatty and aromatic acids has been widely documented. − In contrast, the acylation of nonglycosylated polyphenols proves to be more difficult since they have fewer available reactive sites for acylation, as they lack the sugar moiety that can act as a nucleophile . This limits the options for direct acylation and makes the reactions more challenging.…”

Section: Introductionmentioning

confidence: 99%

Strategy for the Enzymatic Acylation of the Apple Flavonoid Phloretin Based on Prior α-Glucosylation

Gonzalez-Alfonso,

Alonso,

Poveda

et al. 2024

J. Agric. Food Chem.

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The acylation of flavonoids serves as a means to alter their physicochemical properties, enhance their stability, and improve their bioactivity. Compared with natural flavonoid glycosides, the acylation of nonglycosylated flavonoids presents greater challenges since they contain fewer reactive sites. In this work, we propose an efficient strategy to solve this problem based on a first α-glucosylation step catalyzed by a sucrose phosphorylase, followed by acylation using a lipase. The method was applied to phloretin, a bioactive dihydrochalcone mainly present in apples. Phloretin underwent initial glucosylation at the 4′-OH position, followed by subsequent (and quantitative) acylation with C8, C12, and C16 acyl chains employing an immobilized lipase from Thermomyces lanuginosus. Electrospray ionization-mass spectrometry (ESI-MS) and two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) confirmed that the acylation took place at 6-OH of glucose. The water solubility of C8 acyl glucoside closely resembled that of aglycone, but for C12 and C16 derivatives, it was approximately 3 times lower. Compared with phloretin, the radical scavenging capacity of the new derivatives slightly decreased with 2,2-diphenyl-1-picrylhydrazyl (DPPH) and was similar to 2,2azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS •+ ). Interestingly, C12 acyl-α-glucoside displayed an enhanced (3-fold) transdermal absorption (using pig skin biopsies) compared to phloretin and its α-glucoside.

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“…Lipases (triacylglycerol acyl-hydrolases, EC 3.1.1.3) are enzymes that can effectively hydrolyze the ester bonds of insoluble substrates in the water at the substrate-water interface [18]. They present broad-spectrum applications in foods (cheese and tea), pharmaceuticals, detergents, pulp and paper, tanneries, textiles, wastewater treatment, cosmetics, and biodiesel industries [19][20][21][22]. Since the optimal activities of lipases are affected by different physicochemical parameters, such as pH, temperature, autolysis (proteases), chemical agents, and ionic strength [23], the quest for new lipases with novel properties, high efficiency, low cost, and potential uses in various industries has gained prodigious interest among many researchers [24].…”

Section: Introductionmentioning

confidence: 99%

Penicillium fellutanum lipase as a green and ecofriendly biocatalyst for depolymerization of poly (ɛ‐caprolactone): Biochemical, kinetic, and thermodynamic investigations

Amin

Bhatti

Nawaz

et al. 2021

Biotech and App Biochem

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Microbial lipases hold a prominent position in biocatalysis by their capability to mediate reactions in aqueous and nonaqueous media. Herein, a lipase from Penicillium fellutanum was biochemically characterized and investigated its potential to degrade poly (ɛ‐caprolactone) (PCL). The lipase exhibited stability over a broad pH spectrum and performed best at pH 8.5 and 45 °C. The activation energy was determined to be 66.37 kJ/mol by Arrhenius plot, whereas Km and Vmax for pNPP hydrolysis were 0.75 mM and 83.33 μmol/mL/Min, respectively. A rise in temperature reduced the Gibbs free energy, whereas the enthalpy of thermal unfolding (∆H*) remains the same up to 54 °C following a modest decline at 61 °C. The entropy (∆S*) of the enzyme demonstrated an increasing trend up to 54 °C and dropped at 61 °C. Lipase retained stability by incubation with various industrially relevant organic solvents (benzene, hexanol, ether, and acetone). However, exposure to urea and guanidine hydrochloride influenced its catalytic activity to different extents. Under optimal operating conditions, lipase catalyzed the excellent degradation of PCL film degradation leading to 66% weight loss, increased surface erosion, and crystallinity. Fourier‐transform infrared spectrometry, differential scanning calorimetry, and scanning electron microscopy studies monitored the weight loss after enzymatic hydrolysis. The findings indicate that P. fellutanum lipase would be a prospective biocatalytic system for polyesters depolymerization and environmental remediation.

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Highly efficient and regioselective acylation of arbutin catalyzed by lipase from Candida sp.

Cited by 11 publications

References 43 publications

Fabrication of a nano-biocatalyst for regioselective acylation of arbutin

Fabrication of a nano-biocatalyst for regioselective acylation of arbutin

Strategy for the Enzymatic Acylation of the Apple Flavonoid Phloretin Based on Prior α-Glucosylation

Penicillium fellutanum lipase as a green and ecofriendly biocatalyst for depolymerization of poly (ɛ‐caprolactone): Biochemical, kinetic, and thermodynamic investigations

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