Evaluation of solid and submerged fermentations for the production of cyclodextrin glycosyltransferase by Paenibacillus campinasensis H69-3 and characterization of crude enzyme


Autoria(s): Alves-Prado, Heloiza Ferreira; Gomes, Eleni; Da Silva, Roberto
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/03/2006

Resumo

Cyclodextrin glycosyltransferase (CGTase) is an enzyme that produces cyclodextrins from starch by an intramolecular transglycosylation reaction. Cyclodextrins have been shown to have a number of applications in the food, cosmetic, pharmaceutical, and chemical industries. In the current study, the production of CGTase by Paenibacillus campinasensis strain H69-3 was examined in submerged and solid-state fermentations. P. campinasensis strain H69-3 was isolated from the soil, which grows at 45 C, and is a Gram-variable bacterium. Different substrate sources such as wheat bran, soybean bran, soybean extract, cassava solid residue, cassava starch, corn starch, and other combinations were used in the enzyme production. CGTase activity was highest in submerged fermentations with the greatest production observed at 48-72 h. The physical and chemical properties of CGTase were determined from the crude enzyme produced from submerged fermentations. The optimum temperature was found to be 70-75 degrees C, and the activity was stable at 55 degrees C for 1 h. The enzyme displayed two optimum pH values, 5.5 and 9.0 and was found to be stable between a pH of 4.5 and 11.0.

Formato

234-246

Identificador

http://link.springer.com/article/10.1385%2FABAB%3A129%3A1%3A234

Applied Biochemistry and Biotechnology. Totowa: Humana Press Inc., v. 129, n. 1-3, p. 234-246, 2006.

0273-2289

http://hdl.handle.net/11449/19938

WOS:000203004800019

Idioma(s)

eng

Publicador

Humana Press Inc

Relação

Applied Biochemistry and Biotechnology

Direitos

closedAccess

Palavras-Chave #cyclodextrin glycosyltransferase #Paenibacillus campinasensis #submerged fermentation #solid-state fermentation
Tipo

info:eu-repo/semantics/article