Biochemical characterization and evaluation of invertases produced from Saccharomyces cerevisiae CAT-1 and Rhodotorula mucilaginosa for the production of fructooligosaccharides

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.

Extraction and characterization of β-fructofuranosidases produced by Kluyveromyces marxianus CCMB 322

“…According to such methodology, the optimal pH is 3.9 and temperature of 46.5ºC in Inv-I, and pH 3.9 and 45.6ºC in Inv-E. Such values are close to those found for invertases obtained from Saccharomyces cerevisiae, with optimum pH and temperature of 4.5 and 50ºC, respectively, as reported in the study conducted by Barbosa et al (2018). K. marxianus invertase obtained using by-products of food processing as a substrate…”

The β-Fructofuranosidase from Rhodotorula dairenensis: Molecular Cloning, Heterologous Expression, and Evaluation of Its Transferase Activity

“…The ability to produce FOS of β-fructofuranosidases from some species of the genus Rhodotorula has also been analyzed with different results. Curiously, enzymes from Rhodotorula sp.-LEB-V10 and Rhodotorula mucilaginosa only generated sugars included in the 1 F-FOS series, whereas that from Rhodotoula glutinis, a yeast synthesizing numerous valuable compounds (carotenoids and lipids among others) with a wide industrial usage, did not produce any type of FOS [22][23][24][25]. However, the large protein RdINV from Rhodotorula dairenensis (~170 kDa, of which N-linked carbohydrates constituted~16% of the total mass) produced mainly 6-kestose, but also a varied mixture of FOS of the three referenced series [26], which makes it of biotechnological interest.…”

Response of selected microbial strains and their consortia to the presence of automobile paints: Biofilm growth, matrix protein content and hydrolytic enzyme activity

“…In contrast, Lincoln and More (2017) reported the inhibitory effects of Hg 2+ , Cu 2+ , pCMB, β-ME, and DTT on enzyme activity as well as the roles of Fe 2+ , Mg 2+ , and Mn 2+ as enzyme modulators on enzyme activity. Barbosa and co-workers (2018) found high structural stability of the enzyme produced by R. mucilaginosa . The data in the scientific papers clearly showed that the optimal conditions (pH and temperature) for invertase activity were 4.0 and 70 °C for R. mucilaginosa and 4.5 and 50 °C for S. cerevisiae .…”