Purification, characterisation, and gene cloning of transglutaminase from Streptoverticillium cinnamoneum CBS 683.68

Duran, Robert; Junqua, Magali; Schmitter, Jean Marie; Gancet, C.; Goulas, Philippe

doi:10.1016/s0300-9084(98)80073-4

Cited by 60 publications

(37 citation statements)

References 17 publications

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“…Therefore, TTA 02 SDS 14 isolate was selected for identification and further studies. The analysis of partial MTGase gene sequence showed that it shares 93% similarity (at the nucleotide sequence) with that from Streptomyces cinnamoneous as reported by Duran et al (1998).…”

Section: Screening Of Mtgase Producing Streptomycessupporting

confidence: 65%

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MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

Fawzya¹,

Zilda²,

Chaniago

et al. 2016

Squalen Bull. Marine Fisheries Postharvest Biotech.

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Transglutaminase (TGase), an enzyme that catalyzes the formation of inter-and intra-molecular -(l-glutamyl) lysine (GL) crosslinks, plays an important role in surimi-based products production. The development and the diversification of surimi-based products have recently been getting popular in Indonesia. These surimi-based products can be made from various types of fish. These products generally exhibit good gel strength properties, depending on the fish type and the processing method used. Transglutaminase plays an important role in generating such properties. Fish's endogenous TGase reduces quickly after it is caught and is almost completely destroyed by freezing it, applying exogenous TGase may improve fish's gel forming ability. Microbial transglutaminase (MTGase) can potentially be used to increase gel properties. In this research, a total of 228 Streptomyces strains from marine and terrestrial environments were screened and selected based on their ability to produce MTGase. Strain TTA 02 SDS 14 exhibited the highest activity; and therefore, it was selected for further study. The 16S-rRNA gene analysis showed that it shared 99% similarity to S. thioluteus. In order to optimize MTGase activity, enzyme production was carried out using six different formulas media, designated as media A, B, C, D, E, and F. The result shows that the highest MTGase activity was observed in medium B that contains pepton (1.5%), MgSO 4 .7H 2 0 (0.1%), KH 2 PO 4 (0.5%), Na 2 HPO 4 (0.5%), soybean powder (2%), potato starch (2%), and glucose (1.5%). The MTGase activity reached the highest level (1.45 U/ml) after 4 days of incubation

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Section: Screening Of Mtgase Producing Streptomycessupporting

confidence: 65%

“…cinnamoneum (Duran et al, 1998), Streptoverticillium mobaraense (Kikuchi et al, 2003), Streptoverticillium ladakanum (Tellez-Luis et al, 2004), Streptomyces netropsis (Yu et al, 2008), and Streptoverticillium hygroscopicus (Aidaroos et al, 2011). It has also been reported to be found in Bacillus subtilis spores (Liu et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

Fawzya¹,

Zilda²,

Chaniago

et al. 2016

Squalen Bull. Marine Fisheries Postharvest Biotech.

View full text Add to dashboard Cite

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“…Thus, the enzyme can be recovered by the separation of the broth from the solid material (ZHu et al, 1995). Duran et al (1998) reported the capacity of transglutaminase expression by Streptoverticillium cinnamoneum and found high amino acid homology with the transglutaminase produced by Streptoverticillium S-8112. Surprisingly, the physiological function of microbial TGases is not fully understood even though many studies were published reporting their structural characteristics (KANAJI et al, 1993;DURAN et al, 1998;KAsHiwAGi et al, 2002).…”

Section: Microbial Transglutaminasementioning

confidence: 99%

Use of transglutaminases in foods and potential utilization of plants as a transglutaminase source – Review

Luciano

Arntfield

2012

Biotemas

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ResumoUso de transglutaminases em alimentos e a potencial utilização de plantas como uma fonte de transglutaminase -Revisão. Transglutaminases (TGases) são enzimas capazes de catalisar reações de transferência de grupos alquila, o que introduz ligações covalentes entre proteínas, peptídeos e aminas primárias. TGases de origem animal foram as primeiras a serem estudadas e são divididas em nove grupos de isoenzimas. Estas enzimas exercem diversas funções no metabolismo da maior parte dos animais, e são Ca 2+ -dependentes. TGases microbianas e de plantas também foram identificadas, e existe uma vasta heterogeneidade entre suas sequências de aminoácidos. No entanto, parece que todas as transglutaminases possuem uma tríade de aminoácidos específicos em seu sítio catalítico composto por Cys-His-Asp. Esta sequência pode ser encontrada em todas as estruturas terciárias das enzimas estudadas até hoje. As TGases de origem microbiana são extensamente utilizadas para a modificação de alimentos, principalmente devido ao seu baixo custo e facilidade de extração e purificação quando comparadas com as enzimas de origem animal. TGases também são encontradas em grande parte das plantas, e sua utilização para transformação de alimentos já foi proposta. Contudo, a literatura demonstra um único estudo que utiliza TGase vegetal em um alimento, onde a polpa de maçã foi utilizada para melhorar a qualidade da carne de porco. A transferência dos genes de TGase de mamíferos para plantas também tem sido experimentado, sendo que já se conseguiu sua expressão em arroz e folhas de tabaco. Estes resultados podem levar a uma nova técnica de produção de transglutaminases, onde elas poderão ser literalmente plantadas para serem utilizadas em alimentos. Palavras-chave: Ligação entre proteínas; Plantio molecular; Textura de alimentos; Transglutaminase AbstractTransglutaminases (TGases) are enzymes able to catalyze acyl-transfer reactions introducing covalent cross-links between proteins, peptides and primary amines. Animal TGases were the first studied and are divided in nine different groups of isoenzymes. They have a wide range of functions in the metabolism of most animal cells, and share the characteristic of being Ca 2+ -dependent. Microbial and plant TGases were also identified, and there is a vast heterogeneity among their amino acid sequences. Interestingly, it seems that all transglutaminases share a specific amino acid triad of Cys-His-Asp in their catalytic site, which can be found in all tertiary structures Revista Biotemas, 25 (4), dezembro de 2012 2 F. B. Luciano e S. D. Arntfield of the enzymes yet studied so far. Microbial TGases are the most widely used for food modification due to lower costs and high yields involved with their extraction and purification when compared to mammal sources. TGases are ubiquitously found in a variety of plants, and their utilization for food transformation has been proposed. However, there is only a single attempt using vegetal TGase in food systems, where apple pomace was used to improve the quality ...

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“…They are also widely present in most animal tissues and body fluids (Folk 1983;Lorand & Conrad 1984). TGases have been discovered in microorganisms including Candida albicans (Ruiz-Herrera et al 1995), Bacillus subtilis (Kobayashi et al 1996), Escherichia coli (Schmidt et al 1998), Physarum polycephalum (Klein et al 1992), and actinomycetes (Kanaji et al 1993;Gerber et al 1994;Duran et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Optimization of transconjugation and characterization of attB integration site for Streptomyces cinnamoneus producing transglutaminase

Park

Choi

2014

Biologia

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An effective transformation method for molecular genetic studies of Streptomyces cinnamoneus producing transglutaminase was established using intergeneric conjugal transfer based on the bacteriophage ΦC31 att/int system. The high efficiency of S. cinnamoneus transconjugation was obtained on mannitol soya flour medium containing 50 mM MgCl2, using 2.5 × 10 8 Escherichia coli as donor and spores treated with heat treatment at 35• C for 10 min as host. By cloning and sequencing the attB integration site, a single attB site within an open reading frame coding for a pirin homologue was located in S. cinnamoneus genome. Its sequence exhibited the highest degree of sequence similarity with that of Streptomyces clavuligerus. These results provide sufficient efficiency to enable conjugal transfer of genetic elements for S. cinnamoneus, and also should facilitate molecular genetic studies for improvement in production ability of transglutaminase used in food industry.

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Purification, characterisation, and gene cloning of transglutaminase from Streptoverticillium cinnamoneum CBS 683.68

Cited by 60 publications

References 17 publications

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

MICROBIAL TRANSGLUTAMINASE OF INDONESIAN Streptomyces sp. : Screening and Production in several media

Use of transglutaminases in foods and potential utilization of plants as a transglutaminase source – Review

Optimization of transconjugation and characterization of attB integration site for Streptomyces cinnamoneus producing transglutaminase

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