Protein–polymer bioconjugation, immobilization, and encapsulation: a comparative review towards applicability, functionality, activity, and stability

Çalbaş, Berke; Keobounnam, Ashley N.; Korban, Christopher; Doratan, Ainsley Jade; Jean, Tiffany; Sharma, Aryan Yashvardhan; Wright, Thaiesha A.

doi:10.1039/d3bm01861j

Biomater. Sci.

2024

DOI: 10.1039/d3bm01861j

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Protein–polymer bioconjugation, immobilization, and encapsulation: a comparative review towards applicability, functionality, activity, and stability

Berke Çalbaş,

Ashley N. Keobounnam,

Christopher Korban

et al.

Abstract: Protein–polymer bioconjugation, immobilization, and encapsulation exhibit a unique array of properties and can be tuned to produce desired effects for specific biomaterial applications.

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Glu@Zn‐Ni MOF Constructed Through Ligand Exchange for Bi‐Enzyme Immobilization With Improved Performance in Rare Ginsenoside Production

Yue,

Li,

Liu

et al. 2024

Applied Organom Chemis

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The biological conversion method using immobilized enzymes has become an important means to produce ginsenosides. Among them, the preprepared Zn‐Ni MOF could be used to immobilize glycosyltransferase by specific adsorption for ginsenoside Rh2 production. However, the low enzyme load of Zn‐Ni MOF limited its wide application. In this study, we successfully synthesized the Glu@Zn‐Ni MOF filled with nanospheres by modifying the previously prepared Zn‐Ni MOF with glutamic acid (Glu) through ligand exchange. This modification significantly increased the specific surface area of the Glu@Zn‐Ni MOF and enhanced the material's enzyme‐carrying capacity. After immobilizing glycosyltransferase (UGT) onto the Glu@Zn‐Ni MOF, the UGT@Glu@Zn‐Ni MOF demonstrated improved stability across different pH levels, temperatures, and repeated cycles. After seven cycles, the immobilized enzyme remained at 83.42% of its initial enzyme activity. To further enhance the process, we incorporated immobilized sucrose synthase into the system to form a coupled reaction. This approach not only reduced substrate costs but also increased the yield of ginsenoside Rh2. By optimizing the coupling reaction through adjustments to the reaction conditions and the addition of suitable surfactants and organic solvents, we achieved a yield of 5.41 μg/mL of Rh2. The development and optimization of this material hold significant potential and value for industrial applications in both material enhancement and ginsenoside synthesis.

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Glu@Zn‐Ni MOF Constructed Through Ligand Exchange for Bi‐Enzyme Immobilization With Improved Performance in Rare Ginsenoside Production

Yue,

Li,

Liu

et al. 2024

Applied Organom Chemis

View full text Add to dashboard Cite

show abstract

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Protein–polymer bioconjugation, immobilization, and encapsulation: a comparative review towards applicability, functionality, activity, and stability

Abstract: Protein–polymer bioconjugation, immobilization, and encapsulation exhibit a unique array of properties and can be tuned to produce desired effects for specific biomaterial applications.

Cited by 1 publication

References 232 publications

Glu@Zn‐Ni MOF Constructed Through Ligand Exchange for Bi‐Enzyme Immobilization With Improved Performance in Rare Ginsenoside Production

Glu@Zn‐Ni MOF Constructed Through Ligand Exchange for Bi‐Enzyme Immobilization With Improved Performance in Rare Ginsenoside Production

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