Interaction of a digestive protease, Candida rugosa lipase, with three surfactants investigated by spectroscopy, molecular docking and enzyme activity assay

Zhang, Rui; Liu, Yang; Huang, Xinran; Xu, Mengchen; Liu, Rutao; Zong, Wansong

doi:10.1016/j.scitotenv.2017.11.305

Cited by 49 publications

(13 citation statements)

References 36 publications

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“…Upon the gradual addition of maltol to CAT solution, the absorption intensity of the peak at 210 nm decreased significantly, which could reflect the transition of π → π* of the polypeptide backbone structure and the change of CAT skeleton structure . No significant changes of the peak at 280 nm were observed with changes in the concentration of maltol, indicating maltol have no influence on the transformation of CAT chromophores …”

Section: Resultsmentioning

confidence: 97%

Binding mechanism of maltol with catalase investigated by spectroscopy, molecular docking, and enzyme activity assay

Huo¹,

Zhao²,

Wang

et al. 2019

J of Molecular Recognition

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Maltol is a flavor additive that is widely used in the daily diet of humans, and its biosafety attention is concomitantly increasing. Catalase (CAT) is an antioxidant enzyme to maintain homeostasis in the tissue's environment of human body and protect cells from oxidative damages. The adverse effects of maltol to CAT activity within mouse hepatocytes as well as the structural and functional changes of CAT on molecular level were investigated by multiple spectroscopy techniques, enzyme activity experiments, and molecular docking. Results suggested that when the maltol concentrations reached to 8 × 10 −5 mol L −1 , the viability of hepatocytes decreased to 93%, and CAT activity was stimulated by maltol to 111% than the control group after exposure for 24 hours. Changes in CAT activity on molecular level were consistent with those on cellular level. The fluorescence quenching of CAT by maltol was static with the forming of maltol-CAT complex. Moreover, ultraviolet-visible (UV-visible) absorption, synchronous fluorescence, and circular dichroism (CD) spectra reflected that the presence of maltol caused conformational change of CAT and made the CAT molecule skeleton loose and increased α-helix of CAT. Maltol mainly bound with CAT through hydrogen bond, and binding site that is near the heme ring in the enzyme activity center did not interact with its main amino acid residues. This study explores the combination between maltol and CAT, providing references for evaluating health damages caused by maltol.

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Section: Resultsmentioning

confidence: 97%

Binding mechanism of maltol with catalase investigated by spectroscopy, molecular docking, and enzyme activity assay

Huo¹,

Zhao²,

Wang

et al. 2019

J of Molecular Recognition

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“…After being added with Tween 20, Triton X-100, or SDS, the residual enzyme activities of An605 and An3131 were all lower than 20% compared with the respective control ( Figures 3J,K ). Studies indicated that SDS could break the intramolecular and intermolecular hydrogen bonds of the enzyme, resulting in molecular unfolding, conformational change, and destruction of the enzyme ( Zhang et al, 2018 ). Tween 20 and Triton X-100 are non-ionic surfactants, with a critical micelle concentration (CMC), that is, the concentration of aggregation to form micelles ( Goswami, 2020 ).…”

Section: Resultsmentioning

confidence: 99%

Characterization of an Aspergillus niger for Efficient Fatty Acid Ethyl Ester Synthesis in Aqueous Phase and the Molecular Mechanism

Huang

et al. 2022

Front. Microbiol.

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Fatty acid ethyl esters are important flavor chemicals in strong-flavor baijiu. Microorganisms are the main contributors to ester synthesis during baijiu manufacture. However, the ester synthesis was unstable between batches. This was owing to a limited knowledge of the mechanisms for ester synthesis by microorganisms. In this work, a fatty acid ethyl ester synthesizing Aspergillus niger strain CGMCC (China General Microbiological Culture Collection) 3.4309 was identified. The conversion ratios of ethyl valerate, ethyl caproate, ethyl caprylate, and ethyl caprate were 7.87, 29.20, 94.80, and 85.20%, respectively, under the optimized conditions. A comparison of transcriptomes under the initial and optimized ester synthetic conditions indicated that 23 genes were upregulated in transcription level and encoded enzymes with potential abilities for ester synthesis. Eleven of the enzymes were expressed, and three of them, numbered An605, An1097, and An3131, showed the ability to catalyze fatty acid ethyl ester synthesis under aqueous phase, with capric acid as the preferred substrate. The possible enzymatic catalytic mechanism was proposed based on homology modeling and molecular docking. This study reported for the first time that A. niger showed the ability to efficiently catalyze the synthesis of short- and medium-chain fatty acid ethyl esters in aqueous phase, identified the key enzymes, and analyzed the basic enzymatic properties. This is helpful to promote the application of related microorganisms and enzyme resources in the baijiu industry.

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“…Compared with nonionic surfactants, anionic surfactants have a stronger hydrophobic effect ( Holmberg et al, 2018 ; Ozyilmaz et al, 2020 ). Zhang et al (2018 ) employed molecular docking to provide an insight into the interactions of CRL and SDS. They found that the principal binding region of SDS and CRL is close to the hydrophobic force–dominated cavity, which can keep the active conformation of CRL.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Interfacial Activated Candida rugosa Lipase Onto Magnetic Chitosan Using Dialdehyde Cellulose as Cross-Linking Agent

Wang

Liu

et al. 2022

Front. Bioeng. Biotechnol.

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Candidarugosa lipase (CRL) was activated with surfactants (sodium dodecyl sulfate [SDS]) and covalently immobilized onto a nanocomposite (Fe3O4-CS-DAC) fabricated by combining magnetic nanoparticles Fe3O4 with chitosan (CS) using polysaccharide macromolecule dialdehyde cellulose (DAC) as the cross-linking agent. Fourier transform infrared spectroscopy, transmission electron microscope, thermogravimetric analysis, and X-ray diffraction characterizations confirmed that the organic–inorganic nanocomposite support modified by DAC was successfully prepared. Enzymology experiments confirmed that high enzyme loading (60.9 mg/g) and 1.7 times specific enzyme activity could be obtained under the optimal immobilization conditions. The stability and reusability of immobilized CRL (Fe3O4-CS-DAC-SDS-CRL) were significantly improved simultaneously. Circular dichroism analysis revealed that the active conformation of immobilized CRL was maintained well. Results demonstrated that the inorganic–organic nanocomposite modified by carbohydrate polymer derivatives could be used as an ideal support for enzyme immobilization.

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Interaction of a digestive protease, Candida rugosa lipase, with three surfactants investigated by spectroscopy, molecular docking and enzyme activity assay

Cited by 49 publications

References 36 publications

Binding mechanism of maltol with catalase investigated by spectroscopy, molecular docking, and enzyme activity assay

Binding mechanism of maltol with catalase investigated by spectroscopy, molecular docking, and enzyme activity assay

Characterization of an Aspergillus niger for Efficient Fatty Acid Ethyl Ester Synthesis in Aqueous Phase and the Molecular Mechanism

Immobilization of Interfacial Activated Candida rugosa Lipase Onto Magnetic Chitosan Using Dialdehyde Cellulose as Cross-Linking Agent

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