Processes
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2020
·Vol. 8
·期 5
·629
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IF 2.753
Yanhong Bi,Zhaoyu Wang,Rui Zhang,Yihan Diao,Yaoqi Tian,Zhengyu Jin
In this study, magnetic Fe3O4nanoparticles coated with polydopamine possessing abundant amino groups (Fe3O4@PDA) were conveniently prepared, detailed, and characterized, and then firstly used as a supporting matrix for immobilizingThermomyces lanuginosuslipase (Fe3O4@PDA@TLL). The effects of some crucial factors on the immobilization efficiency were investigated and the optimal protein loading and activity recovery were found to be 156.4 mg/g and 90.9%, respectively. Characterization studies revealed that Fe3O4@PDA@TLL displayed a broader pH and temperature adaptability as compared to the free TLL, which allows its use at wider ranges of reaction conditions. With regard to the stabilities, the immobilized TLL clearly displayed improved pH, thermal, and solvent tolerance stabilities compared to the free enzyme, suggesting that the biocompatible Fe3O4@PDA might be an outstanding material for immobilizing TLL and acting as alternative support for different enzymes.Keywords:magnetic nanoparticle;immobilization;Thermomyces lanuginosuslipase;stability
研究领域:
生物化学
·
材料科学
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产品关联
DOI
高影响因子
INDUSTRIAL CROPS AND PRODUCTS
·
2023
·
IF 5.9
Xiaoyan Ji,Rui Xu,Fei Wang,Xun Li
Biodiesel is recognized as green and renewable energy with low carbon intensity and less environmental impacts. The preparation of an economical immobilized lipase becomes much urgent challenge in the enzymatic production of biodiesel. In this study, recombinant Thermomyces lanuginosus lipase (TLL) was immobilized on the surface of silica-containing materials mediated by solid-binding peptides (SBPs). The obtained immobilized biocatalysts were effective in converting the oil from Jatropha curcas into biodiesel. The appropriate attachment mode of SBPs and TLL was investigated firstly, and the results showed that the activity of TLL was not negatively affected only when SBPs were fused at the C-terminus of TLL. Secondly, the immobilization efficiency of different SBPs (CecA, EctP1, VKT) on different silica-containing materials (SiO 2 , zeolite ZSM-5, SAR-100, MCM-41 and Na-Y) was systematically studied and it was concluded that the best immobilization efficiency was achieved for TLL-EctP1 immobilized on zeolite ZSM-5 (TLL- EctP1 @ZSM-5). TLL-EctP1 @ZSM-5 was found great performance in stability of pH, temperature, elution and storage. Eventually, biodiesel yield of 93 wt% was achieved using TLL-EctP1 @ZSM-5 as a biocatalyst to catalyze J. curcas oil for 48 h, and 81% of its initial yield was retained after 7 cycles of reuse. These results highlight the application of solid-binding peptides in enzyme immobilization for biocatalysts used in preparation of biodiesel or other chemicals.
研究领域:
生物化学
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可再生能源
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产品关联
DOI
高影响因子
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2015
·
IF 2.128
Wei-Wei Zhang,Xian-Ling Yang,Jun-Qi Jia,Na Wang,Cheng-Li Hu,Xiao-Qi Yu
Novel surfactant-activated magnetic cross-linked enzyme aggregates of Thermomyces lanuginosus lipase (TLL-magnetic-CLEAs) were developed and provided an efficient approach to improve the activity and stability of lipase for biodiesel production. In the methanolysis of Jatropha oil for biodiesel synthesis, the maximum yield in isopropyl ether was 88% after 48 h at 40 °C, representing 3.5-fold and 2.5-fold higher activity than that exhibited by free TLL and TLL CLEAs, respectively. Moreover, Tween 80-activated TLL-magnetic-CLEAs retained their activity during storage at 4 °C for 11 weeks and 10 cycles of repeated 48 h biodiesel reactions at 40 °C (over 30 days). Additionally, the surface morphology, particle size and loading of lipase aggregates were confirmed by Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM). The combination of interfacial activation, high specific enzyme activity, improved stability and easy recovery of magnetic CLEAs presents an attractive process for lipase immobilization and provides a promising catalyst for biodiesel production.
研究领域:
生物化学
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可再生能源
·
酶工程
✓ 已验证
产品关联
DOI
高影响因子
Frontiers in Bioengineering and Biotechnology
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2020
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IF 3.644
Bi Yanhong,Wang Zhaoyu,Tian Yaoqi,Fan Haoran,Huang Shuo,Lu Yihui,Jin Zhengyu
The immobilization of Thermomyces lanuginosus lipase on polydopamine-functionalized Fe3O4 magnetic nanoparticles (Fe3O4@PDA-TLL) as a nanobiocatalyst was successfully performed for the first time, and the Fe3O4@PDA-TLL was used for regioselective acylation of natural hyperoside with vinyl decanoate. The effects of several crucial factors, such as the reaction solvent, substrate molar ratio, temperature, and immobilized enzyme dosage, were investigated. Under optimum conditions, the reaction rate, 6″-regioselectivity, and maximum substrate conversion were as high as 12.6 mM/h, 100%, and 100%, respectively. An operational stability study demonstrated that the immobilized enzyme could maintain 90.1% of its initial maximum conversion even after reusing it five times. In addition, further investigations on the kinetic parameters, like Vmax, Km, Vmax/Km, and Ea, also revealed that the biocompatible Fe3O4@PDA could act as an alternative carrier for the immobilization of different enzymes.
研究领域:
生物化学
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纳米生物学
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酶工程
✓ 已验证
DOI
PubMed
高影响因子
Bioresources and Bioprocessing
·
2024
·Vol. 11
·期 1
·1-14
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IF 4.3
Chen Ming,She Weina,Zhao Xin,Chen Cheng,Zhu Benwei,Sun Yun,Yao Zhong
The Thermomyces lanuginosus lipase (TLLs) was successfully immobilized within a novel hydrogel matrix through a two-step crosslinking method. TLLs were initially crosslinked through the Schiff base reaction by oxidized carboxymethyl cellulose (OCMC). The water-soluble OCMC@TLLs complex was subsequently crosslinked by carboxymethyl chitosan (CMCSH) in a microfluidic apparatus to form the CMCHS/OCMC@TLLs microspheres. The CD (Circular Dichroism, CD) and FT-IR (Fourier Transform infrared spectroscopy, FT-IR) spectra demonstrated that the crosslinking of TLLs with OCMC resulted in a less significant impact on their structure compared to that with glutaraldehyde. CMCHS/OCMC@TLLs showed decreased catalytic performance due to the mass transfer resistance, while its thermal stability was greatly improved. The CMCHS/OCMC@TLLs were used to catalyze the lauroylation of arbutin in tetrahydrofuran. After 12 h of reaction under optimal conditions, the yield of 6′-O-lauryl arbutin reached an impressive 92.12%. The prepared 6′-O-lauryl arbutin has high lipophilicity and exhibits similar tyrosinase inhibitory activity and higher antioxidant activity compared to its parent compound.
研究领域:
生物化学
·
酶工程
·
食品科学
✓ 已验证
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）