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Title: INFLUENCE OF ALTERNANSUCRASE-DERIVED OLIGOSACCHARIDES AND OTHER CARBOHYDRATES ON ENZYME ACTIVITY IN BIFIDOBACTERIUM ADOLESCENTIS

Author
item HOLT, S. - WESTERN IL UNIV
item TERESI, J - WESTERN IL UNIV
item Cote, Gregory

Submitted to: Letters in Applied Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 9/10/2007
Publication Date: 1/1/2008
Citation: Holt, S.M., Teresi, J., Cote, G.L. 2008. Influence of alternansucrase-derived oligosaccharides and other carbohydrates on alpha-gelactosidase and alpha-glucosidase activity in Bifidobacterium adolescentis. Letters in Applied Microbiology. 46(1):73-79.

Interpretive Summary: Fundamental information on the biological activity of novel sugar-based food ingredients is required in order to understand and predict their nutritional role and activity. In this paper, we studied the effect of novel sugar-derived food ingredients on enzyme levels in a bacterium important to good intestinal health. These novel carbohydrates significantly raised enzyme activity in the beneficial bacterium compared with most of the carbohydrates tested. This helps us to understand the effects of complex carbohydrates on intestinal bacteria, and may enable us to design new food ingredients and predict their activity. The results will be useful to researchers and designers of novel functional foods.

Technical Abstract: The objective of this study was to determine the influence of prebiotic oligosaccharides and other carbohydrates on enzyme activity in Bifidobacterium adolescentis. B. adolescentis was cultivated anaerobically for 48 hrs on each of seventeen test carbohydrates. Test carbohydrates included a battery of monosaccharides, disaccharides, and prebiotics such as a fructooligosaccharide and alternansucrase-derived oligosaccharides (AOS). Specific activities for alpha-galactosidase and alpha-glucosidase were determined from B. adolescentis cell extracts for each carbohydrate tested. Expression of each enzyme appeared to be controlled by different mechanisms. Each enzyme displayed a significantly different activity pattern toward the battery of test carbohydrates. Alpha-galactosidase was less tightly controlled than alpha-glucosidase since most carbohydrates displayed a significant increase in activity on the former enzyme. The highest activities for both enzymes were obtained on several of the AOS prebiotic carbohydrates. In addition, most of the AOS prebiotic carbohydrates showed significant increases in specific activity for both enzymes over that displayed by their corresponding acceptor carbohydrates.