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

  • Session 1B: Enzyme Catalysis and Engineering
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Abstract

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 Gramvariable 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°C, and the activity was stable at 55°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.

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Authors and Affiliations

  1. Biochemistry and Applied Microbiology Laboratory, UNESP-State University of São Paulo, Rua Cristóvão Colombo no. 2265, 15054-000, São José do Rio Preto, SP, Brazil

    Heloiza Ferreira Alves-Prado, Eleni Gomes & Roberto Da Silva

  2. Biology Institute, UNESP-State University of São Paulo, Rio Claro, SP, Brazil

    Heloiza Ferreira Alves-Prado

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  1. Heloiza Ferreira Alves-Prado
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  2. Eleni Gomes
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  3. Roberto Da Silva
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Correspondence to Roberto Da Silva.

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Alves-Prado, H.F., Gomes, E. & Da Silva, R. Evaluation of solid and submerged fermentations for the production of cyclodextrin glycosyltransferase by Paenibacillus campinasensis H69-3 and characterization of crude enzyme. Appl Biochem Biotechnol 129, 234–246 (2006). https://doi.org/10.1385/ABAB:129:1:234

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