A Comparative Biochemical Characterization of Microbial Transglutaminases: Commercial vs. a Newly Isolated Enzyme from Streptomyces Sp.

dc.creatorMacedo, JA
dc.creatorSette, LD
dc.creatorSato, HH
dc.date2010
dc.dateAPR
dc.date2014-11-18T19:34:52Z
dc.date2015-11-26T16:58:09Z
dc.date2014-11-18T19:34:52Z
dc.date2015-11-26T16:58:09Z
dc.date.accessioned2018-03-28T23:45:45Z
dc.date.available2018-03-28T23:45:45Z
dc.identifierFood And Bioprocess Technology. Springer, v. 3, n. 2, n. 308, n. 314, 2010.
dc.identifier1935-5130
dc.identifierWOS:000274583400016
dc.identifier10.1007/s11947-009-0209-8
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/52932
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/52932
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/52932
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1277855
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionA new microbial transglutaminase (MTGase or MTG, EC 2.3.2.13) from a Streptomyces sp. strain isolated from Brazilian soil samples was characterized in crude and purified forms. The aim of this work is to provide relevant information about a new transglutaminase and to compare its characteristics with the well-known commercial transglutaminase from Ajinomoto Co. Inc. (Activa (R) TG-BP). The enzyme from Streptomyces sp., in both crude and pure forms, exhibited optimal activity in the 6.0-6.5 pH range and at 35-40 degrees C. The results for the commercial enzyme were the same. A second maximum of activity was observed at pH 10.0 with both the crude Streptomyces sp. enzyme and the commercial enzyme. This interesting fact has not been reported in the literature previously. The fact that this second maximum of activity does not appear on the purified form of the enzyme may suggest the presence of an isoenzyme on the crude extract. All of the enzymes tested were stable over the pH range from 4.5 to 8.0 and up to 45 degrees C. The decline in activity of the commercial transglutaminase above 45 C and pH 8.0 was more gradual. The activities of all the MTG samples were independent of Ca(+2) concentration, but they were elevated in the presence of K(+), Ba(2+), and Co(2+) and inhibited by Cu(2+) and Hg(2+), which suggests the presence of a thiol group in the MTG's active site. The purified enzyme presented a Km of 6.37 mM and a V(max) of 1.7 U/mL, while the crude enzyme demonstrated a K(m) of 6.52 mM and a V(max) of 1.35 U/mL.
dc.description3
dc.description2
dc.description308
dc.description314
dc.descriptionFood Biochemistry Laboratory of UNICAMP
dc.descriptionMicrobial Resource Division (CPQBA/UNICAMP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationFood And Bioprocess Technology
dc.relationFood Bioprocess Technol.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectTransglutaminase
dc.subjectStreptomyces sp.
dc.subjectCBMAI 837
dc.subjectBiochemical characterization
dc.subjectCommercial transglutaminase
dc.subjectStreptoverticillium-mobaraense
dc.subjectPurification
dc.titleA Comparative Biochemical Characterization of Microbial Transglutaminases: Commercial vs. a Newly Isolated Enzyme from Streptomyces Sp.
dc.typeArtículos de revistas


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