Site-specific cross-linking of functional proteins by transglutamination

Kamiya, Noriho; Takazawa, Takeshi; Tanaka, Tsutomu; Ueda, Hiroshi; Nagamune, Teruyuki

doi:10.1016/s0141-0229(03)00154-6

Cited by 36 publications

(29 citation statements)

References 25 publications

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“…It had been reported that whey proteins had lower tendency to form cross-link reaction than caseins by MTGase (S˛anlı et al, 2011). In general, the native fold of the proteins (Tang et al, 2006) and the amino acid sequence specificity of MTGase (Kamiya et al, 2003) related to the differences in reactivities of the subunits.…”

Section: Resultsmentioning

confidence: 99%

In vitro gastrointestinal digestion study of a novel bio-tofu with special emphasis on the impact of microbial transglutaminase

Xing

Rui

Jiang

et al. 2016

PeerJ

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We have developed a novel bio-tofu, made from mixed soy and cow milk (MSCM), using Lactobacillus helveticus MB2-1 and Lactobacillus plantarum B1-6 incorporated with microbial transglutaminase (MTGase) as coagulant. MTGase was added to improve the textural properties and suit for cooking. However, the effect of MTGase on the digestion of mixed-protein fermented by lactic acid bacteria was unclear. This study aimed at evaluating the effect of MTGase on protein digestion of bio-tofu under simulated gastrointestinal digestion condition. The results showed that addition of MTGase could affect the particle size distribution, degree of hydrolysis, the content of soluble proteins and free amino acids. Based on the electrophoresis data, MTGase addition enhanced protein polymerization. During gastric and intestinal digestion process, proteins from bio-tofu were degraded into low molecular mass peptides. Our results suggested that incorporation of MTGase could lead to enzymatic modification of proteins of bio-tofu which may help in controlling energy intake and decrease the chance of food allergy.

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Section: Resultsmentioning

confidence: 99%

In vitro gastrointestinal digestion study of a novel bio-tofu with special emphasis on the impact of microbial transglutaminase

Xing

Rui

Jiang

et al. 2016

PeerJ

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“…For this reason, HMDA was chosen for the present study. Other routes include the functionalization with a lysine‐containing tag,23, 24 N ‐terminal glycine,25 or a glutamine‐containing tag 26, 27…”

Section: Resultsmentioning

confidence: 99%

Enzymatically catalyzed HES conjugation using microbial transglutaminase: Proof of feasibility

Besheer

Hertel

Kreßler

et al. 2009

Journal of Pharmaceutical Sciences

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“…For example, Kamiya et al . engineered a GGSPLAQSHGGS tag onto the N-terminus of an scFv of the anti-hen egg-white lysozyme antibody and were thus able to use mTGase to effectively conjugate various proteins to the engineered fragment [21]. Using a similar approach, Strop et al .…”

Section: Peptide Tagsmentioning

confidence: 99%

Site-Specifically Labeled Immunoconjugates for Molecular Imaging—Part 2: Peptide Tags and Unnatural Amino Acids

et al. 2016

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Molecular imaging using radioisotope- or fluorophore-labeled antibodies is increasingly becoming a critical component of modern precision medicine. Yet despite this promise, the vast majority of these immunoconjugates are synthesized via the random coupling of amine-reactive bifunctional probes to lysines within the antibody, a process that can result in heterogeneous and poorly defined constructs with suboptimal pharmacological properties. In an effort to circumvent these issues, the last 5 years have played witness to a great deal of research focused on the creation of effective strategies for the site-specific attachment of payloads to antibodies. These chemoselective modification methods yield immunoconjugates that are more homogenous and better defined than constructs created using traditional synthetic approaches. Moreover, site-specifically labeled immunoconjugates have also been shown to exhibit superior in vivo behavior compared to their randomly modified cousins. The over-arching goal of this two-part review is to provide a broad yet detailed account of the various site-specific bioconjugation approaches that have been used to create immunoconjugates for positron emission tomography (PET), single photon emission computed tomography (SPECT), and fluorescence imaging. In Part 1, we covered site-specific bioconjugation techniques based on the modification of cysteine residues and the chemoenzymatic manipulation of glycans. In Part 2, we will detail two families of bioconjugation approaches that leverage biochemical tools to achieve site-specificity. First, we will discuss modification methods that employ peptide tags either as sites for enzyme-catalyzed ligations or as radiometal coordination architectures. And second, we will examine bioconjugation strategies predicated on the incorporation of unnatural or non-canonical amino acids into antibodies via genetic engineering. Finally, we will compare the advantages and disadvantages of the modification strategies covered in both parts of the review and offer a brief discussion of the overall direction of the field.

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Site-specific cross-linking of functional proteins by transglutamination

Cited by 36 publications

References 25 publications

In vitro gastrointestinal digestion study of a novel bio-tofu with special emphasis on the impact of microbial transglutaminase

In vitro gastrointestinal digestion study of a novel bio-tofu with special emphasis on the impact of microbial transglutaminase

Enzymatically catalyzed HES conjugation using microbial transglutaminase: Proof of feasibility

Site-Specifically Labeled Immunoconjugates for Molecular Imaging—Part 2: Peptide Tags and Unnatural Amino Acids

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