Activation mechanism of Yarrowia lipolytica lipase immobilized on carbon nanotubes

Feng, Wei; Sun, Xiuchan; Ji, Peijun

doi:10.1039/c2sm25231g

Cited by 35 publications

(36 citation statements)

References 44 publications

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“…In this case, immobilization of enzymes on hydrophobic supports with large surface area results in cleaving these dimers and stabilizing molecules in their open form. As a result, the apparent activity is enhanced due to pushing the equilibrium toward the monomeric open form .…”

Section: Conformational Control Over Lipase Activitymentioning

confidence: 99%

A review on the important aspects of lipase immobilization on nanomaterials

Shuai

Das

Naghdi

et al. 2017

Biotech and App Biochem

132

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Lipase is one of the most widely used enzymes and plays an important role in biotechnological and industrial processes including food, paper, and oleochemical industries, as well as in pharmaceutical applications. However, its aqueous solubility and instability make its application relatively difficult and expensive. The immobilization technique is often used to improve lipase performance, and the strategy has turned out to be a promising method. Immobilized lipase on nanomaterials (NMs) has shown superiority to the free lipase, such as improved thermal and pH stability, longer stable time, and the capacity of being reused. However, immobilization of lipase on NMs also sometimes causes activity loss and protein loading is relatively lowered under some conditions. The overall performance of immobilized lipase on NMs is influenced by mechanisms of immobilization, type of NMs being used, and physicochemical features of the used NMs (such as particle size, aggregation behavior, NM dimension, and type of coupling/modifying agents being used). Based on the specific features of lipase and NMs, this review discusses the recent developments, some mechanisms, and influence of NMs on lipase immobilization and their activity. Multiple application potential of the immobilized lipases has also been considered.

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Section: Conformational Control Over Lipase Activitymentioning

confidence: 99%

A review on the important aspects of lipase immobilization on nanomaterials

Shuai

Das

Naghdi

et al. 2017

Biotech and App Biochem

132

View full text Add to dashboard Cite

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“…The lid could adopt an open conformation to permit substrates approaching catalytic site (active state of lipase) or adopt a close conformation to prevent substrates from accessing to the inner pocket (inactive state of lipase) [18][19][20][21]. The lid of YLLIP2 lipase is composed by Thr88-Leu105 residues, and Ala277-Leu290 ones exhibited flexible motions [16,22].…”

Section: Introductionmentioning

confidence: 99%

The role of temperature and solvent microenvironment on the activity of Yarrowia lipolytica Lipase 2: Insights from molecular dynamics simulation

Cao

Deng

Lei

et al. 2014

Journal of Molecular Catalysis B: Enzymatic

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“…7(b). Peijun Ji et al27 used MD simulation to study lipase immobilized onto CNT in heptane media and also found that the adsorption could induces an open of lid (Thr88–Leu105) and the segment (Asn277–Leu290), favoring exposure of active site. It is also observed from Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Some observations from the work provide molecular evidences for experimental findings. More importantly, some novel observations are obtained with respect to previous studies on adsorbed enzymes1516272829, which could provide valuable information for understanding the catalytic property, the specificity, the functional modification, solvent selection and some key experimental operations for the immobilized serine protease in organic media.…”

mentioning

confidence: 95%

Molecular mechanism of carbon nanotube to activate Subtilisin Carlsberg in polar and non-polar organic media

Zhang

Yuan

et al. 2016

Sci Rep

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In the work, we mainly used molecular dynamics (MD) simulation and protein structure network (PSN) to study subtilisin Carlsberg (SC) immobilized onto carbon nanotube (CNT) in water, acetonitrile and heptane solvents, in order to explore activation mechanism of enzymes in non-aqueous media. The result indicates that the affinity of SC with CNT follows the decreasing order of water > acetonitrile > heptane. The overall structure of SC and the catalytic triad display strong robustness to the change of environments, responsible for the activity retaining. However, the distances between two β-strands of substrate-binding pocket are significantly expanded by the immobilization in the increasing order of water < acetonitrile < heptane, contributing to the highest substrate-binding energy in heptane media. PSN analysis further reveals that the immobilization enhances structural communication paths to the substrate-binding pocket, leading to its larger change than the free-enzymes. Interestingly, the increase in the number of the pathways upon immobilization is not dependent on the absorbed extent but the desorbed one, indicating significant role of shifting process of experimental operations in influencing the functional region. In addition, some conserved and important hot-residues in the paths are identified, providing molecular information for functional modification.

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Activation mechanism of Yarrowia lipolytica lipase immobilized on carbon nanotubes

Cited by 35 publications

References 44 publications

A review on the important aspects of lipase immobilization on nanomaterials

A review on the important aspects of lipase immobilization on nanomaterials

The role of temperature and solvent microenvironment on the activity of Yarrowia lipolytica Lipase 2: Insights from molecular dynamics simulation

Molecular mechanism of carbon nanotube to activate Subtilisin Carlsberg in polar and non-polar organic media

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