Nickel-Functionalized Chitosan for the Oriented Immobilization of Histidine-Tagged Enzymes: A Promising Support for Food Bioprocess Applications

Andrade, Bruna Coelho de; Gennari, Adriano; Renard, Gaby; Benvenutti, Edilson Valmir; Chies, Jocelei Maria; Volpato, Giandra; Souza, Cláucia Fernanda Volken de

doi:10.1007/s10562-021-03912-1

Cited by 6 publications

(2 citation statements)

References 74 publications

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“…Laccase used in the clarification of fruit juices oxidizes most of the phenols in the juice, minimizing turbidity and increasing its stability [109][110][111][112]. As the use of laccase as a food additive is still not allowed, this enzyme is used in the food industry in an immobilized form [32,113,114].…”

Section: Applications 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: Applications 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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“…Compared with random immobilization, directional immobilization through affinity tags results in higher enzyme activity and improved thermal and operational stabilities. De Andrade et al 21 developed a chitosan (CS)-based carrier functionalized with glutaraldehyde, Nα, Nα-BIS(carboxymethyl)-L-lysine hydrate, and nickel for directed immobilization of His-labeled recombinant β-galactosidase. After 16 h of immobilization, the efficiency of the complexes reached approximately 70%, with an active recovery rate of over 50%.…”

Section: Introductionmentioning

confidence: 99%

One-Step Purification and Immobilization of Glycosyltransferase with Zn–Ni MOF for the Synthesis of Rare Ginsenoside Rh2

Li,

Liu,

et al. 2024

ACS Appl. Mater. Interfaces

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Uridine diphosphate (UDP)-glucosyltransferases (UGTs) have received increasing attention in the field of ginsenoside Rh2 conversion. By harnessing the metal chelation between transition metal ions and imidazole groups present on Histagged enzymes, a specific immobilization of the enzyme within metal−organic frameworks (MOFs) is achieved. This innovative approach not only enhances the stability and reusability of the enzyme but also enables one-step purification and immobilization. Consequently, the need for purifying crude enzyme solutions is effectively circumvented, resulting in significant cost savings during experimentation. The use of immobilized enzymes in catalytic reactions has shown great potential for achieving higher conversion rates of ginsenoside Rh2. In this study, highly stable mesoporous Zn−Ni MOF materials were synthesized at 150 °C by a solvothermal method. The UGT immobilized on the Zn−Ni MOF (referred to as UGT@Zn−Ni MOF) exhibited superior pH adaptability and thermal stability, retaining approximately 76% of its initial activity even after undergoing 7 cycles. Furthermore, the relative activity of the immobilized enzyme remained at an impressive 80.22% even after 45 days of storage. The strong specific adsorption property of Zn−Ni MOF on His-tagged UGT was confirmed through analysis using polyacrylamide gel electrophoresis. UGT@Zn−Ni MOF was used to catalyze the conversion reaction, and the concentration of rare ginsenoside Rh2 was generated at 3.15 μg/mL. The results showed that Zn−Ni MOF is a material that can efficiently purify and immobilize His-tagged enzyme in one step and has great potential for industrial applications in enzyme purification and ginsenoside synthesis.

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The Brønsted-Lewis Acid Sites in Metal–Organic Framework Biomimetic Nanozyme for Cooperatively Enhancing the Hydrolysis of Lactose

Yi,

Xing,

et al. 2024

Catal Lett

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Nickel-Functionalized Chitosan for the Oriented Immobilization of Histidine-Tagged Enzymes: A Promising Support for Food Bioprocess Applications

Cited by 6 publications

References 74 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

One-Step Purification and Immobilization of Glycosyltransferase with Zn–Ni MOF for the Synthesis of Rare Ginsenoside Rh2

The Brønsted-Lewis Acid Sites in Metal–Organic Framework Biomimetic Nanozyme for Cooperatively Enhancing the Hydrolysis of Lactose

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