Overexpression and purification of microbial pro-transglutaminase from Streptomyces cinnamoneum and in vitro processing by Streptomyces albogriseolus proteases

Taguchi, Seiichi; Arakawa, Kumiko; Yokoyama, Keiichi; Takehana, Shino; Takagi, Hiroshi; Momose, Haruo

doi:10.1016/s1389-1723(02)80228-6

Cited by 21 publications

(3 citation statements)

References 17 publications

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“…Viable technological methods contribute to more efficient use of raw materials, thereby improving the cost-benet ratio of food production. 364,365 TGMs also have potential applications in other industries, including the leather and textile sectors. 366 In a recent study, transglutaminase enzymes (TGMs) were subjected to enzymatic immobilization using magnetic nanoparticles (MNPs).…”

Section: Transferasesmentioning

confidence: 99%

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Advancements in enzyme immobilization on magnetic nanomaterials: toward sustainable industrial applications

Gama Cavalcante,

Dari,

Izaias da Silva Aires

et al. 2024

RSC Adv.

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Section: Transferasesmentioning

confidence: 99%

“…Viable technological methods contribute to more efficient use of raw materials, thereby improving the cost–benefit ratio of food production. 364,365 TGMs also have potential applications in other industries, including the leather and textile sectors. 366 …”

Section: Enzymatic Magnetic Nanoparticle Applicationsmentioning

confidence: 99%

Advancements in enzyme immobilization on magnetic nanomaterials: toward sustainable industrial applications

Gama Cavalcante,

Dari,

Izaias da Silva Aires

et al. 2024

RSC Adv.

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“…According to (Kikuchi et al 2003), subtilisin-like protease SAM-P45 was able to hydrolyze MTG at Ser41. Subtilisin shared high homology with SAM-P45 particularly in regions around the active sites meaning residues outside of this area might play critical role in digesting MTG (Suzuki et al 1997;Taguchi et al 2002).…”

Section: Crosslinking Of Spimentioning

confidence: 99%

Heterologous signal peptides-directing secretion of Streptomyces mobaraensis transglutaminase by Bacillus subtilis

Qiao

et al. 2018

Appl Microbiol Biotechnol

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Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase

Dube

Schäfer

Neidhart

et al. 2006

Eur Food Res Technol

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Microbial transglutaminase (MTG) isolated from Streptomyces mobaraensis has been available on a commercial scale for several years. MTG generates inter- and intramolecular cross-links between gamma-carboxylamide groups of glutamine residues and epsilon-amino groups of lysine residues in proteins. Due to its great potential to improve various functional properties of proteins, MTG is mainly used to enhance texture, stability, and water binding. Application of MTG for the production of plant protein-based foodstuffs such as tofu, noodles, bread and bakery products, is still limited to raw materials from soybean and wheat. However, with the increasing demand for vegetarian foods, the utilisation of novel proteins as functional ingredients, e.g. from peas, lupins, sesame, and sunflower, seems promising. To open new horizons for MTG application, this review aims at demonstrating the actual potential of MTG in processing foodstuffs based on vegetable proteins. Particular focus was laid on novel plant protein sources suitable for cross-linking with MTG. Furthermore, strategies for improving texture and nutritive value of the proteins are discussed

show abstract

Overexpression and purification of microbial pro-transglutaminase from Streptomyces cinnamoneum and in vitro processing by Streptomyces albogriseolus proteases

Cited by 21 publications

References 17 publications

Advancements in enzyme immobilization on magnetic nanomaterials: toward sustainable industrial applications

Advancements in enzyme immobilization on magnetic nanomaterials: toward sustainable industrial applications

Heterologous signal peptides-directing secretion of Streptomyces mobaraensis transglutaminase by Bacillus subtilis

Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase

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