Protein engineering to improve the stability of Thermomyces lanuginosus lipase in methanol

Okamura, Taiki; Nogami, Yohei; Matsumoto, Takuya; Yamada, R.; Ogino, Hiroyasu

doi:10.1016/j.bej.2022.108659

Cited by 6 publications

(1 citation statement)

References 26 publications

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“…Many previous studies have suggested that the formation of new h-bonds is beneficial to the organic solvent tolerance of lipases. For instance, Oghino suggested that the half-life of A28S variants of Thermomyces lanuginosus lipase was increased to 6.7-folds longer than the wild type, due to the newly formed h-bonds between A28S and D274 [135]. Zhu indicated that the substitutions of charged residues will improve the solvent resistance of lipases [136].…”

Section: Computer-aided Methods For Solvent Tolerance Engineeringmentioning

confidence: 99%

Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art

Cheng

Nian

2023

Molecules

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As some of the most widely used biocatalysts, lipases have exhibited extreme advantages in many processes, such as esterification, amidation, and transesterification reactions, which causes them to be widely used in food industrial production. However, natural lipases have drawbacks in terms of organic solvent resistance, thermostability, selectivity, etc., which limits some of their applications in the field of foods. In this systematic review, the application of lipases in various food processes was summarized. Moreover, the general structure of lipases is discussed in-depth, and the engineering strategies that can be used in lipase engineering are also summarized. The protocols of some classical methods are compared and discussed, which can provide some information about how to choose methods of lipase engineering. Thermostability engineering and solvent tolerance engineering are highlighted in this review, and the basic principles for improving thermostability and solvent tolerance are summarized. In the future, comput er-aided technology should be more emphasized in the investigation of the mechanisms of reactions catalyzed by lipases and guide the engineering of lipases. The engineering of lipase tunnels to improve the diffusion of substrates is also a promising prospect for further enhanced lipase activity and selectivity.

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Section: Computer-aided Methods For Solvent Tolerance Engineeringmentioning

confidence: 99%

Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art

Cheng

Nian

2023

Molecules

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Continuous Flow Synthesis of Hexyl Laurate Using Immobilized Thermomyces Lanuginosus Lipase from Residual Babassu Mesocarp

de S. Lira,

do Nascimento,

Lima

et al. 2024

ChemPlusChem

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This work applied BM as support for immobilization of lipase TLL in packed‐bed reactor and its application for the synthesis of hexyl laurate. Initially, the percolation of a solution containing 5 mg of TLL at 25 oC generated an immobilized derivative with hydrolytic activity of 504.7 U/g and 31.7% of recovered activity. Subsequent treatment with n‐hexane, as well as the effect of temperature on the immobilization process were able to improve the activities of the final BM‐TLLF, achieving a hydrolysis activity of 7023 U/g and esterification activity of 430 U/g against 142 U/g and 113.5 U/g respectively presented by commercial TLIM. Desorption studies showed that the TL IM has 18 mg of protein per gram of support, compared to 4.92 mg presented by BM‐TLL. Both biocatalysts were applied to synthesize hexyl laurate, achieving 98% conversion at 40°C within a residence time of 2 hours. Notably, BM‐TLLF displayed exceptional recyclability, maintaining catalytic efficiency over 12 cycles. This reflects a productivity of 180 mg of product/h/U of the enzyme, surpassing 46 mg/h/U obtained for TLIM. These results demonstrate the efficacy of continuous flow technology in creating a competitive and integrated process offering an exciting alternative for the valorization of residual lignocellulosic biomass.

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Transition of stability of putidaredoxin reductase by introducing proline

Okamura,

Aritomi,

Matsumoto

et al. 2024

Biochemical Engineering Journal

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Protein engineering to improve the stability of Thermomyces lanuginosus lipase in methanol

Cited by 6 publications

References 26 publications

Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art

Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art

Continuous Flow Synthesis of Hexyl Laurate Using Immobilized Thermomyces Lanuginosus Lipase from Residual Babassu Mesocarp

Transition of stability of putidaredoxin reductase by introducing proline

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