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Biochemical Characterization and Evaluation of Invertases Produced From Saccharomyces Cerevisiae CAT-1 and Rhodotorula Mucilaginosa for the Production of Fructooligosaccharides

Biochemical Characterization and Evaluation of Invertases Produced From Saccharomyces Cerevisiae CAT-1 and Rhodotorula Mucilaginosa for the Production of Fructooligosaccharides

Paula Mirella Gomes Barbosa, Tobias Pereira de Morais, Cinthia Aparecida de Andrade Silva, Flávia Regina da Silva Santos, Nayara Fernanda Lisboa Garcia, Gustavo Graciano Fonseca, Rodrigo Simões Ribeiro Leite, etc.

Prep Biochem Biotechnol. 2018;48(6):506-513.

PMID: 29932819

Abstract:

Invertases are used for several purposes; one among these is the production of fructooligosaccharides. The aim of this study was to biochemically characterize invertase from industrial Saccharomyces cerevisiae CAT-1 and Rhodotorula mucilaginosa isolated from Cerrado soil. The optimum pH and temperature were 4.0 and 70 °C for Rhodotorula mucilaginosa invertase and 4.5 and 50 °C for Saccharomyces cerevisiae invertase. The pH and thermal stability from 3.0 to 10.5 and 75 °C for R. mucilaginosa invertase, respectively. The pH and thermal stability for S. cerevisiae CAT-1 invertase from 3.0 to 7.0, and 50 °C, respectively. Both enzymes showed good catalytic activity with 10% of ethanol in reaction mixture. The hydrolysis by invertases occurs predominantly when sucrose concentrations are ≤5%. On the other hand, the increase in the concentration of sucrose to levels above 10% results in the highest transferase activity, reaching about 13.3 g/L of nystose by S. cerevisiae invertase and 12.6 g/L by R. mucilaginosa invertase. The results demonstrate the high structural stability of the enzyme produced by R. mucilaginosa, which is an extremely interesting feature that would enable the application of this enzyme in industrial processes.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001574	Invertase from baker's yeast (S. cerevisiae)		9001-57-4	Price

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