Abstract
β-Galactosidases of Mucoromycota are rarely studied, although this group of filamentous fungi is an excellent source of many industrial enzymes. In this study, 99 isolates from the genera Lichtheimia, Mortierella, Mucor, Rhizomucor, Rhizopus and Umbelopsis, were screened for their β-galactosidase activity using a chromogenic agar approach. Ten isolates from the best producers were selected, and the activity was further investigated in submerged (SmF) and solid-state (SSF) fermentation systems containing lactose and/or wheat bran substrates as enzyme production inducers. Wheat bran proved to be efficient for the enzyme production under both SmF and SSF conditions, giving maximum specific activity yields from 32 to 12,064 U/mg protein and from 783 to 22,720 U/mg protein, respectively. Oligosaccharide synthesis tests revealed the suitability of crude β-galactosidases from Lichtheimia ramosa Szeged Microbiological Collection (SZMC) 11360 and Rhizomucor pusillus SZMC 11025 to catalyze transgalactosylation reactions. In addition, the crude enzyme extracts had transfructosylation activity, resulting in the formation of fructo-oligosaccharide molecules in a sucrose-containing environment. The maximal oligosaccharide concentration varied between 0.0158 and 2.236 g/L depending on the crude enzyme and the initial material. Some oligosaccharide-enriched mixtures supported the growth of probiotics, indicating the potential of the studied enzyme extracts in future prebiotic synthesis processes.
Highlights
Introduction published maps and institutional affilβGalactosidases (β-D-galactoside galactohydrolase or lactase, EC 3.2.1.23) are important biocatalysts in many food and pharmaceutical applications, as they can catalyze both the hydrolysis and synthesis of glycosides affecting human health
The activity data and origin of ten isolates identified as the best producers, namely Lichtheimia ramosa Szeged Microbiological Collection (SZMC)
The results revealed the highest activities for strains belonging to the genera Rhizomucor, Lichtheimia and Umbelopsis
Summary
Introduction published maps and institutional affilβGalactosidases (β-D-galactoside galactohydrolase or lactase, EC 3.2.1.23) are important biocatalysts in many food and pharmaceutical applications, as they can catalyze both the hydrolysis and synthesis of glycosides affecting human health. Βgalactosidases are frequently used to produce lactose hydrolyzed foods through the degradation of lactose to galactose and glucose monomers in the dairy industry [1]. These special food products are beneficial for people with low intestine β-galactosidase levels that causes the condition of lactose intolerance. The hydrolyzing activity of β-galactosidases is utilized in various other applications, such as prevention against lactose-related crystallization in frozen foods and condensed milk, or ethanol and sweet syrup production from whey lactose [2]. Β-Galactosidases can synthesize galacto-oligosaccharide (GOS) and lactulose-derived. GOS (OsLu) molecules through the enzymatic transgalactosylation of lactose and lactulose, iations.
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