Microbial Transglutaminase: Purification, Characterisation and Bioactive properties.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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Relation |
http://ir.cftri.com/11292/
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Title |
Microbial Transglutaminase: Purification,
Characterisation and Bioactive properties.
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Creator |
Mabel, M. J.
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Subject |
05 Enzymes
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Description |
Transglutaminase (TG; protein-glutamine γ-glutamyl transferase EC 2.3.2.13) is
an enzyme which can modify proteins by amine incorporation, cross-linking and deamidation.
The enzyme is of interest to food industries, because of its capability to
modify the functional properties of proteins. The cross-linking property of TG useful in
improving nutritional properties of foods by incorporating essential amino acids like
lysine to proteins and the possibility of improving the functional properties of foods by
TG treatment is promising. In view of the tremendous market potential for TG, there
exists enough scope for screening new sources of the enzyme which in turn is a
promising step towards the development of novel protein foods.
Screening and selection of bacterial, fungal and actinomycete species for
microbial transglutaminase production under submerged fermentation conditions was
carried out. Streptomyces griseocarneus MTCC 328 was found to produce the enzyme at
about 0.09 U/ml. The enzyme exhibited calcium independent activity and was
extracellular in nature. The optimization of media for the enzyme production using
statistically based experimental designs resulted in an enhanced enzyme activity of 0.32
U/ml. The enzyme was purified by ammonium sulphate precipitation, followed by
successive chromatographies on CM-cellulose and Sephadex G-75 columns with a 34
fold purification and specific activity of 1.5 U/mg proteins. The purified enzyme was
found to have optimum activity at 37 - 45 0C and in a range of pH 6.0-7.0. The activity of
the purified enzyme was inhibited by Cu2+, Zn2+, Hg2+, Co2+ and NEM (N-ethyl
maleimide), which suggests the presence of a thiol group in the MTG’s active site. The
bioactive property of the purified enzyme was confirmed by cross-linking 11S protein
fractions of soybean.
The effect of purified enzyme in improving the quality attributes of
transglutaminase mediated fructooligosaccharides, a low calorie prebiotic enriched
yoghurt was studied with respect to physicochemical properties such pH, syneresis or
whey separation, and sensory attributes like colour, texture etc during 15 days of storage.
Transglutaminase from the novel source isolated in this study was found to be potent in
improving the physicochemical properties of fructooligosaccharides enriched yoghurt.
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Contributor |
Prapulla, S. G.
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Date |
2012
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Type |
Thesis
NonPeerReviewed |
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Format |
application/pdf
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Language |
en
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Rights |
—
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Identifier |
http://ir.cftri.com/11292/1/mobelthes.pdf
Mabel, M. J. (2012) Microbial Transglutaminase: Purification, Characterisation and Bioactive properties. PhD thesis, University of Mysore. |
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