Study on improving the stability of adsorption-encapsulation immobilized Laccase@ZIF-67

Wang, Zhaobo; Ren, Dajun; Yu, Haiying; Jiang, Shan; Zhang, Shuqin; Zhang, Xiaoqing

doi:10.1016/j.btre.2020.e00553

Cited by 27 publications

(11 citation statements)

References 53 publications

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“…On the other hand, the immobilization of enzymes onto solid supports has become a key enabling technology to implement postsynthesis their exploitation in industrial processes, promoting enzyme reusability and recovery, 9 , 10 while enhancing their thermostability. 11 …”

Section: Introductionmentioning

confidence: 99%

Enhancing the Thermostability of Engineered Laccases in Aqueous Betaine-Based Natural Deep Eutectic Solvents

Varriale¹,

Delorme

Andanson

et al. 2021

ACS Sustainable Chem. Eng.

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In recent years, natural deep eutectic solvents (NADESs) have gained increasing attention as promising nontoxic solvents for biotechnological applications, due to their compatibility with enzymes and ability to enhance their activity. Betaine-based NADESs at a concentration of 25 wt % in a buffered aqueous solution were used as media to inhibit thermal inactivation of POXA1b laccase and its five variants when incubated at 70 and 90 °C. All the tested laccases showed higher residual activity when incubated in NADES solutions, with a further enhancement achieved also for the most thermostable variant. Furthermore, the residual activity of laccases in the presence of NADESs showed a clear advantage over the use of NADESs’ individual components. Molecular docking simulations were performed to understand the role of NADESs in the stabilization of laccases toward thermal inactivation, evaluating the interaction between each enzyme and NADESs’ individual components. A correlation within the binding energies between laccases and NADES components and the stabilization of the enzymes was demonstrated. These findings establish the possibility of preincubating enzymes in NADESs as a facile and cost-effective solution to inhibit thermal inactivation of enzymes when exposed to high temperatures. This computer-aided approach can assist the tailoring of NADES composition for every enzyme of interest.

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Section: Introductionmentioning

confidence: 99%

Enhancing the Thermostability of Engineered Laccases in Aqueous Betaine-Based Natural Deep Eutectic Solvents

Varriale¹,

Delorme

Andanson

et al. 2021

ACS Sustainable Chem. Eng.

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“…As shown in Figure 6D , the encapsulated DAE was successfully cycled for five times, and the residual activity was determined to be 56%. Wang et al immobilized laccase within ZIF67 by the one-pot synthesis strategy, which maintained 59% residual enzyme activity after five reaction cycles ( Wang et al, 2020 ). The gradual loss of activity during recycling may cause by mechanical damage to the enzyme.…”

Section: Resultsmentioning

confidence: 99%

Characterization of D-Allulose-3-Epimerase From Ruminiclostridium papyrosolvens and Immobilization Within Metal-Organic Frameworks

Yang

Fan

Zhao

et al. 2022

Front. Bioeng. Biotechnol.

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D-allulose is one sort of C-3 epimer of D-fructose with the low calorie (0.4 kcal/g) and high sweetness (70% of the relative sweetness of sucrose), which can be biosynthesized by D-allulose-3-epimerase (DAE). In this work, we report the characterization of a novel DAE from Ruminiclostridium papyrosolvens (RpDAE) by genome mining approach. The activity of RpDAE reached maximum at pH 7.5 and 60°C, supplemented with 1 mM Co2+. Using D-fructose (500 g/L) as the substrate for epimerization reaction, RpDAE produced D-allulose (149.5 g/L). In addition, RpDAE was immobilized within the microporous zeolite imidazolate framework, ZIF67, by in situ encapsulation at room temperature. The synthesized bio-composites were characterized by powder X-ray diffraction and Fourier transform infrared spectroscopy. RpDAE-ZIF67 maintained 56% of residual activity after five reaction cycles. This study provides helpful guidance for further engineering applications and industrial production of D-allulose.

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“…Several lignocellulosic supports have been applied in the immobilization of laccases. However, a large part of these ends up performing extensive pre-treatment protocols, making the final biocatalyst more expensive [ 51 , 59 , 60 , 61 , 62 , 63 ].…”

Section: Resultsmentioning

confidence: 99%

Corn Cob as a Green Support for Laccase Immobilization—Application on Decolorization of Remazol Brilliant Blue R

Santos

Baruque

Lira

et al. 2022

IJMS

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The high demand for food and energy imposed by the increased life expectancy of the population has driven agricultural activity, which is reflected in the larger quantities of agro-industrial waste generated, and requires new forms of use. Brazil has the greatest biodiversity in the world, where corn is one of the main agricultural genres, and where over 40% of the waste generated is from cobs without an efficient destination. With the aim of the valorization of these residues, we proposed to study the immobilization of laccase from Aspergillus spp. (LAsp) in residual corn cob and its application in the degradation of Remazol Brilliant Blue R (RBBR) dye. The highest yields in immobilized protein (75%) and residual activity (40%) were obtained at pH 7.0 and an enzyme concentration of 0.1 g.mL−1, whose expressed enzyme activity was 1854 U.kg−1. At a temperature of 60 °C, more than 90% of the initial activity present in the immobilized biocatalyst was maintained. The immobilized enzyme showed higher efficiency in the degradation (64%) of RBBR dye in 48 h, with improvement in the process in 72 h (75%). The new biocatalyst showed operational efficiency during three cycles, and a higher degradation rate than the free enzyme, making it a competitive biocatalyst and amenable to industrial applications.

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Study on improving the stability of adsorption-encapsulation immobilized Laccase@ZIF-67

Abstract: Graphical abstract

Cited by 27 publications

References 53 publications

Enhancing the Thermostability of Engineered Laccases in Aqueous Betaine-Based Natural Deep Eutectic Solvents

Enhancing the Thermostability of Engineered Laccases in Aqueous Betaine-Based Natural Deep Eutectic Solvents

Characterization of D-Allulose-3-Epimerase From Ruminiclostridium papyrosolvens and Immobilization Within Metal-Organic Frameworks

Corn Cob as a Green Support for Laccase Immobilization—Application on Decolorization of Remazol Brilliant Blue R

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