Research Progress on Lignocellulosic Biomass Degradation Catalyzed by Enzymatic Nanomaterials

Luo, Hangyu; Liu, Xiaofang; Yu, Dayong; Yuan, Junfa; Tan, Jinyu; Li, Hu

doi:10.1002/asia.202200566

Cited by 11 publications

(7 citation statements)

References 184 publications

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“…Nanomaterials provide a larger immobilization surface, which increases the enzyme load per unit mass of particles and, thus, increases the efficiency of the immobilized enzymes [321,322]. The reuse of immobilized laccases improves the efficiency and durability of the process by reducing the costs associated with the loss of enzymes and materials [159,323]. To improve the decolorization performance of HR dyes, Wehaidy et al (2019) developed a method of laccase immobilization on a nanoporous Zeolite-X carrier [324] chemically belonging to hydrated aluminosilicates forming a three-dimensional network skeleton with the same size of interconnected pores and channels.…”

Section: Improvement Of Catalytic Activity Of Laccasesmentioning

confidence: 99%

Biochemical Characteristics of Laccases and their Practical Application in the Removal of Xenobiotics from Waters

Gałązka¹,

Jankiewicz²,

Szczepkowski³

2023

Preprint

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Industrialization, intensive farming, rapid population growth and urbanization are the source of a large number of pollutants entering the environment. The current concentration of xenobiotics released into the environment exceeds its natural ability to decompose them. Enzymatic degradation of pollutants seems to be an environmentally friendly process. Due to the wide spectrum of substrate specificity, from inorganic compounds to high molecular weight organic compounds such as PAH or dyes, as well as favorable biochemical properties, laccase has been used in the biological removal of xenobiotics from the environment. It is important to understand the degradation mechanisms of pollutants and to evaluate the final products in terms of their toxicity. The laccase oxidizes the substrates with the simultaneous reduction of molecular oxygen to water, which is the purest reaction co-substrate. That is why it is called a green biocatalyst. The trend is an increase in the production of enzymes related to the intensive development of industry, bioremediation or synthetic chemistry. This leads to the search for laccases with greater activity and stability under extreme conditions. The potential of laccases to degrade xenobiotics can be promoted by improving enzymatic catalytic characterization using protein engineering and other genetic engineering methods.

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Section: Improvement Of Catalytic Activity Of Laccasesmentioning

confidence: 99%

Biochemical Characteristics of Laccases and their Practical Application in the Removal of Xenobiotics from Waters

Gałązka¹,

Jankiewicz²,

Szczepkowski³

2023

Preprint

View full text Add to dashboard Cite

show abstract

“…In addition, there is a need for the enzymatic system to be stable; that is, the catalytic activity must be maintained for a few cycles. [89] The main stabilizing effects of an enzyme are caused by the simple fact that it is inside/bound to a solid particle. But there are also advantages related to the stability of the enzyme system when using polymers and the core-shell structure.…”

Section: Core-shell Polymeric Particles For Enzyme Immobilizationmentioning

confidence: 99%

“…In contrast, polymers (mainly synthetics) can offer a wide range of uses, proper specific surface area, and available functional groups, which can be selected according to each enzyme. [89] This great flexibility in choosing polymers for shell composition allows synthesizing of core-shell particles with diverse functionalities and properties. It implies that the shell materials can be selected according to the enzyme to be immobilized.…”

Section: Polymers For Core and Shellmentioning

confidence: 99%

A Comprehensive Review on Core‐Shell Polymeric Particles for Enzyme Immobilization

et al. 2022

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The search for ideal solid support that promotes enzyme stability, easy separation and reuse cycles in different processes has grown widely. In this sense, core‐shell polymer particles draw attention because they are already widely used in adsorption, catalysis, and drug delivery, due to their remarkable advantages in surface properties adjustment, excellent mechanical stability, and high chemical resistance, as a result of the combination of the characteristics of the polymers that form the core and shell of the structure. Thus, this review article provides an overview of the synthesis processes of these particles, highlighting the characteristics that can be obtained from each synthesis technique, as well as the most recently used techniques to obtain polymeric particles with core‐shell morphology. The advantages and main challenges for the application of these structures in the immobilization of enzymes are also discussed, providing a general summary of what has been explored in the literature. Despite the potential of application, the use of these materials in the immobilization of enzymes is still little explored, with studies focused mainly on lipases and around the same classes of polymers. Therefore, there is an opportunity window regarding the investigation of the immobilization of other enzymes of commercial interest on these polymeric supports.

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“…Therefore, due to its excellent geographic selectivity, benign reaction conditions, and environmental protection, lipase-based enzymatic esterification offers a wide variety of prospective applications in the field of catalysis. − Being a well-known natural protein, lipase is delicate and expensive, and because of this, it has long been considered a promising strategy to select a suitable carrier material to bind lipases using a variety of techniques to obtain lipase nanoreactors . The biocatalytic lipase nanoreactors have the advantages of easy recovery and separation, high efficiency, excellent operation stability, economically feasible, and environmental protection. , …”

Section: Introductionmentioning

confidence: 99%

The Mesoporous Polydopamine-Based Bowl-like Lipase Nanoreactor for the Biocatalytic Synthesis of Oleate Sterol Ester

Hou

Zhang

Zhao

et al. 2023

ACS Food Sci. Technol.

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Enzymatic esterification of phytosterols is essential for their stability and bioavailability in lipophilic foods. In this study, we created a new polydopamine-based bowl-like mesoporous carrier (BLM-PDA) for lipase loading and catalyzed the esterification of phytosterols and oleic acid to produce oleate sterol ester. Candida rugosa lipase (CRL) was selected to immobilize the polymer using physical adsorption. SEM, TEM, XRD, TGA, XPS, FT-IR, and BET were used to characterize it in order to confirm the successful preparation. These less-studied asymmetric bowl-like particles showed much enhanced performance in all aspects. According to the findings, BLM-PDA had a lipase loading of around 126.05 mg g −1 , and the thermal stability and reusability of BLM-PDA@CRL fared particularly well in activity tests. After 55 h, the catalyst successfully completed the oleate sterol ester yield of 81.07% of the transesterification cycle at 40 °C. Therefore, it offers more suggestions for using an immobilized lipase nanoreactor to the biosynthesis of sterol esters.

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Research Progress on Lignocellulosic Biomass Degradation Catalyzed by Enzymatic Nanomaterials

Cited by 11 publications

References 184 publications

Biochemical Characteristics of Laccases and their Practical Application in the Removal of Xenobiotics from Waters

Biochemical Characteristics of Laccases and their Practical Application in the Removal of Xenobiotics from Waters

A Comprehensive Review on Core‐Shell Polymeric Particles for Enzyme Immobilization

The Mesoporous Polydopamine-Based Bowl-like Lipase Nanoreactor for the Biocatalytic Synthesis of Oleate Sterol Ester

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