Application of transglutaminases in the modification of wool textiles

Cortez, João; Bonner, P.; Griffin, Martin

doi:10.1016/j.enzmictec.2003.08.004

Cited by 141 publications

(69 citation statements)

References 12 publications

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“…Recently, TGase has captured researchers' interest due to its attractive potential application in food industries [Zhu et al 1995], immobilization of enzymes [Josten et al 1999] and textile industries [Cortez et al 2004]. The relatively small quantity obtained, complex separation and purifi cation procedure required for TGase from animal tissues.…”

Section: Introductionmentioning

confidence: 99%

Isolation, purifi cation and characterisation of transglutaminase from rosemary (Rosmarinus officinalis L.) leaves

El-Hofi

Ismail

Nour

et al. 2014

Acta Sci Pol Technol Aliment

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Background. Rosemary (Rosmarinus offi cinalis L.) is a spice and medicinal herb widely used around the world of the natural antioxidants, and it has been widely accepted as one of the spices with the highest antioxidant activity. Transglutaminase (EC 2.3.2.13; TGase) is an enzyme capable of catalysing acyl transfer reactions by introducing covalent cross-links between proteins, as well as peptides and various primary amines. TGase activity in plants was fi rst observed in pea seedlings, and subsequently found in organs of both lower and higher plants. Recently, TGase has captured researchers' interest due to its attractive potential application in food industries. Therefore, the objectives of this study are isolation and purifi cation of TGase from new plant source rosemary (Rosmarinus offi cinalis L.) leaves at the laboratory scale. Moreover, investigation of the biochemical properties of the purifi ed TGase to provide a suitable TGase enzyme for food industry applications are in focus. Material and methods. Rosemary (Rosmarinus offi cinalis L.) leaves was used as a new plant source to TGase. The biochemical characteristics of the crude and purifi ed enzyme were determined. Results. Rosemary (Rosmarinus offi cinalis L.) TGase was purifi ed to homogeneity by successive three purifi cation steps including ammonium sulfate precipitatation, ion exchange chromatography on DEAE-Sephadex A-50 column and Size exclusion column chromatography on Sephadex G-100 column. Under experimental conditions, 20-30% of ammonium sulfate saturation in the enzyme solution had a high yield of enzyme activity could be obtained. The purifi ed enzyme from the Sephadex G-100 column had 21.35% yield with increased about 7.31 in purifi cation fold. Rosemary TGase exhibited optimum activity at pH 7.0 and 55°C for the catalytic reaction of hydroxylamine and Z-Gln-Gly. The purifi ed TGase almost maintained full activity after incubation for 15 min up to 60°C and it was completely inactivated at 85°C. The rosemary TGase was stimulated at 2-6 mM CaCl 2 concentrations while it lost about 5-20% from its activity by increasing CaCl 2 concentration. Sodium chloride (2-14%) shows no noticeable inhibition of the purifi ed TGase activity. Mg +2 , Ba +2 were acivited by the purifi ed TGase while it was strongly inhibited by Fe +2 , moderately by Cu +2 and Mn +2 . Conclusion. This paper reports on the purifi cation and characterisation of TGase from newly isolated plant, rosemary (Rosmarinus offi cinalis L.) leaves. Finding results of the TGase properties make this enzyme a good candidate for application in the food industry. However, additional work is required to increase activity yield during extraction and purifi cation for commercial scale of TGase from this plant.

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Section: Introductionmentioning

confidence: 99%

Isolation, purifi cation and characterisation of transglutaminase from rosemary (Rosmarinus officinalis L.) leaves

El-Hofi

Ismail

Nour

et al. 2014

Acta Sci Pol Technol Aliment

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“…The microbial enzyme has widespread and growing applications in the food processing industry. Recent research has shown that TGase can be employed in many others attractive applications such as, pharmaceuticals [3], textiles [6], tissue engineering [19], and in the formation of immunoconjugates to be applied in ELISA and biosensors [11]. To date, only one microbial TGase, that from the actinomycete Streptoverticilium mobarense, has met commercial applications [31].…”

Section: Introductionmentioning

confidence: 99%

Solid state bioreactor production of transglutaminase by Amazonian Bacillus circulans BL32 strain

Souza

Heck

Ayub

2008

J Ind Microbiol Biotechnol

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In this work, we investigated the production of transglutaminase (TGase) by an Amazonian isolated strain of Bacillus circulans by solid-state cultivation (SSC). Several agro-industrial residues, such as untreated corn grits, milled brewers rice, industrial fibrous soy residue, soy hull, and malt bagasse, were used as substrates for microbial growth and enzyme production. Growth on industrial fibrous soy residue, which is rich in protein and hemicellulose, produced the highest TGase activity (0.74 U g(-1) of dried substrate after 48 h of incubation). A 2(3) central composite design was applied to determine the optimal conditions of aeration, cultivation temperature and inoculum cell concentration to TGase production. The best culture conditions were determined as being 0.6 L air min(-1), 33 degrees C and 10 log (10) CFU g(-1) of dried substrate, respectively. Under the proposed optimized conditions, the model predicted an enzyme production of 1.16 U g(-1) of dried substrate, closely matching the experimental activity of 1.25 U g(-1). Results presented in this work point to the use of this newly isolated B. circulans strain as a potential alternative of microbial source for TGase production by SSC, using inexpensive culture media.

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“…TGase catalyses the formation of homologous and heterologous polymers within meat, soybean, milk, and wheat proteins, promoting the polymerization, texture improvement, restructuring, and gel formation in foods. 3 Research has shown that TGase can be used in many other non-food applications such as pharmaceuticals, 4 textiles, 5 immobilization of enzymes, 6 and tissue engineering. 7 Guinea-pig liver used to be the only source of commercial TGase, but the practical application of this enzyme was limited due to the scarce source, and the complicated separation and purification processes to obtain this TGase.…”

Section: Introductionmentioning

confidence: 99%

Kinetics of thermal inactivation of transglutaminase from a newly isolated Bacillus circulans BL32

Souza

Faccin

Mertins

et al. 2009

J of Chemical Tech & Biotech

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BACKGROUND: This paper describes the modeling of the kinetics of thermal inactivation of transglutaminase (TGase) from a newly isolated Bacillus circulans BL32, isolated from the Amazon environment. The purified enzyme was incubated at temperatures ranging from 30 to 70• C and values of the thermodynamic inactivation parameters, such as activation energy ( E), activation enthalpy ( H), activation entropy ( S), and free energy ( G) for thermal inactivation, were calculated.

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Application of transglutaminases in the modification of wool textiles

Cited by 141 publications

References 12 publications

Isolation, purifi cation and characterisation of transglutaminase from rosemary (Rosmarinus officinalis L.) leaves

Isolation, purifi cation and characterisation of transglutaminase from rosemary (Rosmarinus officinalis L.) leaves

Solid state bioreactor production of transglutaminase by Amazonian Bacillus circulans BL32 strain

Kinetics of thermal inactivation of transglutaminase from a newly isolated Bacillus circulans BL32

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