Site-specific, covalent immobilization of an engineered enterokinase onto magnetic nanoparticles through transglutaminase-catalyzed bioconjugation

Wang, Jinghong; Tang, Ming-Ze; Yu, Xinyan; Xu, Chong-Mei; Yang, Hong-Ming; Tang, Jin‐Bao

doi:10.1016/j.colsurfb.2019.02.018

Cited by 21 publications

(14 citation statements)

References 49 publications

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“…Several techniques have been devised to preserve the activity of biomolecules upon immobilization, among them the immobilization using mTGase as site-specific binding (Tominaga et al 2004). The immobilization mediated by transglutaminase-catalyzed bioconjugations offers the advantage of improved selectivity and compatibility with sensitive biological systems relative to traditional chemical methodologies (Wang et al 2019).…”

Section: Enzymes Immobilization Mediated By Mtgase-catalyzed Bioconju...mentioning

confidence: 99%

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Duarte

Matte

Bizarro

et al. 2019

World J Microbiol Biotechnol

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Because of their protein cross-linking properties, transglutaminases are widely used in several industrial processes, including the food and pharmaceutical industries. Transglutaminases obtained from animal tissues and organs, the first sources of this enzyme, are being replaced by microbial sources, which are cheaper and easier to produce and purify. Since the discovery of microbial transglutaminase (mTGase), the enzyme has been produced for industrial applications by traditional fermentation process using the bacterium Streptomyces mobaraensis. Several studies have been carried out in this field to increase the enzyme industrial productivity. Researches on gene expression encoding transglutaminase biosynthesis were performed in Streptomyces lividans, Escherichia coli, Corynebacterium glutamicum, Yarrowia lipolytica, and Pichia pastoris. In the first part of this review, we presented an overview of the literature on the origins, types, mediated reactions, and general characterizations of these important enzymes, as well as the studies on recombinant microbial transglutaminases. In this second part, we focus on the application versatility of mTGase in three broad areas: food, pharmacological, and biotechnological industries. The use of mTGase is presented for several food groups, showing possibilities of applications and challenges to further improve the quality of the end-products. Some applications in the textile and leather industries are also reviewed, as well as special applications in the PEGylation reaction, in the production of antibody drug conjugates, and in regenerative medicine.

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Section: Enzymes Immobilization Mediated By Mtgase-catalyzed Bioconju...mentioning

confidence: 99%

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Duarte

Matte

Bizarro

et al. 2019

World J Microbiol Biotechnol

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“…However, the nonspecific covalent methods utilizing amine, carboxylic acid, and hydroxyl groups in the native proteins suffer from the loss of protein bioactivity. , Besides, all of the above methods need highly purified proteins prior to their immobilization. To this end, many site-specific covalent methods have been developed. − They often rely on the fusion of the protein with a tag that mediates the immobilization on a derivatized surface. The tailored fusion tag selectively and covalently reacts with an immobilized substrate.…”

mentioning

confidence: 99%

Covalent Inhibitor-Based One-Step Method for Endothelin Receptor A Immobilization: from Ligand Recognition to Lead Identification

et al. 2020

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Protein immobilization is particularly significant in proteomics, interactomics, and in vitro drug screening. It is an essential primary step for numerous biological techniques that rely on immobilized proteins with controlled orientation, high conformational stability, and high activity (CHH). These have challenged the current immobilization strategy and demanded increasing efforts for an efficient method to meet the CHH immobilization in a single step. Herein, we proposed a covalent inhibitorbased, one-step method for G protein-coupled receptor (GPCR) immobilization inspired by the covalent reaction between an epidermal growth factor receptor (EGFR)-tag and its inhibitor ibrutinib. We immobilized endothelin receptor A (ETA) containing a fusion EGFR tag onto an ibrutinib-coated macroporous silica gel. The immobilized ETA proved to have demonstrable ligand-binding activity and specificity, thus resulting in a chromatographic technology allowing receptor−ligand interaction analysis and lead identification. Such immobilization method is attractable, owing to the properties of mild reacting conditions, fast rate, high yield, and good stability of the conjugated protein. It will be applicable to biochips, biosensors, and biocatalysts.

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“…Several strategies were established to maintain biomolecular activity during immobilization including immobilization using MTGase for site-specific usage (Tominaga et al, 2004). Increased selectivity and consistency with responsive biological systems with regard to conventional chemical methodologies can be achieved by immobilization by transglutaminase-catalyzed bioconjugation (Wang et al, 2019). (Synowiecki & Wołosowska, 2006) reported that a silica gel adjusted utilizing 3-aminopropyl-triethoxysilane using MTGase as a cross-linking factor has been impounded from βglucosidase from Sulfolobusshibatae and the immobilization mechanism has not affected the optimum temp and pH of the substrate hydrolysis.…”

Section: Enzymes Immobilization Mediated By Mtgase-catalyzed Bioconjugationmentioning

confidence: 99%

Current industrial applications of microbial transglutaminase: A review

Muhammad¹,

Al‐Adeeb²,

Al‐Ansi³

et al. 2021

IJAEMS

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Transglutaminases are commonly used in a number of manufacturing operations, including the food and pharmaceutical industry, owing to their protein cross-linking properties. Transglutaminases derived from animal tissues and lungs, which were the first origins of this enzyme, are being substituted out in preference of microbial sources, which are less expensive and simpler to generate and purify. Following the identification of microbial transglutaminase (MTGase), the enzyme was formulated for industrial purposes using a conventional fermentation process based on the bacterium S. mobaraensis. Many trials have been conducted in this area in order to improve enzyme efficiency for commercial purposes. Several hosts microorganisms such as E. coli, Y. lipolytica, S. lividans, P. pastoris and C. glutamicum gene expression studies were conducted for transglutaminase production. This study reflects on the MTGase application in two broad industries: food and biotechnology. The usage of mTGase is presented for many food classes, highlighting implementation possibilities and obstacles to further enhance end-product efficiency. Few applications in the textile and leather industry, as well as applications in the PEGylation reaction, the development of antibody drug conjugates, and regenerative medicine, are also addressed.

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Site-specific, covalent immobilization of an engineered enterokinase onto magnetic nanoparticles through transglutaminase-catalyzed bioconjugation

Cited by 21 publications

References 49 publications

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

Covalent Inhibitor-Based One-Step Method for Endothelin Receptor A Immobilization: from Ligand Recognition to Lead Identification

Current industrial applications of microbial transglutaminase: A review

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