Enzymatic properties of transglutaminase produced by a new strain of Bacillus circulans BL32 and its action over food proteins

Souza, Cláucia Fernanda Volken de; Venzke, Janaína Guimarães; Flôres, Simone Hickmann; Ayub, Marco Antônio Záchia

doi:10.1016/j.lwt.2010.08.015

Cited by 14 publications

(3 citation statements)

References 40 publications

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“…As a relatively new enzyme in baking, TGM catalyses the reaction between an εamino group on protein-bound glutamine residues leading to covalent crosslinking of protein (Motoki and Seguro 1998;Renzetti et al 2008;Renzetti et al 2012;Volken de Souza et al 2011;Zhu and Tramper 2008). During enzymatic catalyzed reaction of polymers, polymers undergo mainly two chemical reactions; being that polymers can be degraded to smaller fractions and amino acids (de-polymerization) or they can crosslink directly with protein residues (polymerization) to form high molecular weight polymers.…”

Section: Resultsmentioning

confidence: 99%

Rheological and functional properties of composite sweet potato – wheat dough as affected by transglutaminase and ascorbic acid

et al. 2015

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Effect of transglutaminase (TGM) and ascorbic acid (AA) on composite sweet potato - wheat dough functional and rheological properties was studied. Partial substitution of wheat flour with sweet potato flour at the level of 20 % significantly (P ≤ 0.05) reduced glutenin, gliadin, dough stability, protein weakening, storage modulus (G') and viscous modulus (G″). Mixolab revealed that both TGM and AA treated dough had stability and protein weakening closed to wheat dough (control), with TGM treated dough having the highest values. TGM Introduced new cross-link bonds as shown by the change of amino acid concentration, leading to an increase in storage modulus (G') and viscous modulus (G″), with G' being higher at all levels of TGM concentration. The opposite was observed for composite dough treated with AA as measured by controlled - stress rheometer. TGM treatment increased glutenin and gliadin content. Compared with the control, dough treated with AA exhibited high molecular weight of polymers than TGM treated dough. The results indicate that the TGM and AA modification of the mixolab and dynamic rheological characteristics (G' and G″) dependent on the changes of GMP, glutenin, gliadin and protein weakening in the composite dough. TGM and AA treatment could improve functional and rheological properties of sweet potato - wheat dough to levels that might be achieved with normal wheat bread. However, it's extremely important to optimize the concentrations of both additives to obtain the optimum response.

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Section: Resultsmentioning

confidence: 99%

Rheological and functional properties of composite sweet potato – wheat dough as affected by transglutaminase and ascorbic acid

et al. 2015

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“…The microbial transglutaminase (MTG) is widely used in the food industry to improve the texture and nutrition [4, 5]. Besides, TG has broad potential applications in biopharmaceuticals [6–9],tissue engineering [3, 7], site-directed protein cross-linking [1, 3, 10], and antibody-drug conjugates [11].…”

Section: Introductionmentioning

confidence: 99%

Improved the expression level of active transglutaminase by directional increasing copy of mtg gene in Pichia pastoris

Song

Shao²,

Guo

et al. 2019

BMC Biotechnol

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Background The microbial transglutaminase (MTG) is inactive when only the mature sequence is expressed in Pichia pastoris. Although co-expression of MTG and its N-terminal pro-peptide can obtain the active MTG, the enzyme activity was still low. One of the basic steps for strain improvement is to ensure a sufficient level of transcription of the heterologous gene, based on promoter strength and gene copy number. To date, high-copy-number recombinants of P. pastoris are achievable only by cloning of gene concatemers, so methods for rapid and reliable multicopy strains are therefore desirable. Results The coexpression strains harboring different copies mtg were obtained successfully by stepwise increasing Zeocin concentration based on the rDNA sequence of P. pastoris . The genome of coexpression strains with the highest enzyme activity was analyzed by real-time fluorescence quantitative PCR, and three copies of mtg gene ( mtg- 3c) was calculated according to the standard curve of gap and mtg genes ( gap is regarded as the single-copy reference gene). The maximum enzyme activity of mtg- 3c was up to 1.41 U/mL after being inducted for 72 h in 1 L flask under optimal culture conditions, and two protein bands were observed at the expected molecular weights (40 kDa and 5 kDa) by Western blot. Furthermore, among the strains detected, compared with mtg -2c, mtg -6c or mtg -8c, mtg -3c is the highest expression level and enzyme activity, implying that mtg -3c is the most suitable for co-expression pro-peptide and MTG. Conclusions This study provides an effective strategy for improving the expression level of active MTG by directional increasing of mtg copies in P. pastoris. Electronic supplementary material The online version of this article (10.1186/s12896-019-0542-6) contains supplementary material, which is available to authorized users.

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“…TGase from walleye pollack, fish for surimi, has been purified and characterized by Kumazawa et al [ 26 ]. Otherwise, many researchers have shown that TGase can be used in the processing of dairy, wheat and soybean products in order to improve texture, water-holding capacity, elasticity, nutritional value and appearance [ 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 ].…”

Section: Introductionmentioning

confidence: 99%

Changes in Morphology and Activity of Transglutaminase Following Cross-Linking and Immobilization on a Polypropylene Microporous Membrane

et al. 2011

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Transglutaminase (TGase) was cross-linked with glutaraldehyde, and cross-linked crystalline transglutaminase was immobilized on a polypropylene microporous membrane by UV-induced grafting. Immobilized enzyme activity were calculated to be 0.128 U/cm2 polypropylene microporous membrane. The microstructure and enzyme characteristics of free, cross-linked and immobilized transglutaminase were compared. The optimum temperature of free transglutaminase was determined to be approximately 40 °C, while cross-linking and immobilization resulted in an increase to approximately 45 °C and 50 °C. At 60 °C, immobilized, cross-linked and free transglutaminase retained 91.7 ± 1.20%, 63.2 ± 1.05% and 37.9 ± 0.98% maximum activity, respectively. The optimum pH was unaffected by the state of transglutaminase. However, the thermal and pH stabilities of cross-linked and immobilized transglutaminase were shown to increase.

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Enzymatic properties of transglutaminase produced by a new strain of Bacillus circulans BL32 and its action over food proteins

Cited by 14 publications

References 40 publications

Rheological and functional properties of composite sweet potato – wheat dough as affected by transglutaminase and ascorbic acid

Rheological and functional properties of composite sweet potato – wheat dough as affected by transglutaminase and ascorbic acid

Improved the expression level of active transglutaminase by directional increasing copy of mtg gene in Pichia pastoris

Changes in Morphology and Activity of Transglutaminase Following Cross-Linking and Immobilization on a Polypropylene Microporous Membrane

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