Akademik Veri Yönetim Sistemi
International Food Innovation and Sustainability Congress, İstanbul, Türkiye, 16 - 18 Mayıs 2024, ss.171
The 4,6 glucanotransferase (Gtfb) enzyme, which belongs to the Glycosyl Hydrolase 70 family (GH70), exhibits differences in the II. and IV. gene regions compared to Glucansucrases (Gtfa) with the ability to produce α-glucans from the same family. Gtfb, unlike Gtfa, cleaves α-1→4 bonds and creates α-1→6 glucan chains attached to the non-reducing ends of starch and its derivatives via α-1→6 glycosidic linkages of single glucose molecules, thus producing resistant starch and isomaltooligosaccharides in the form of dietary fiber. The produced branched substrates can be used as effective coating agents in micro-particle production using spray dryer methods. It is thought to be successful in the encapsulation of postbiotics with antimicrobial properties. Recent studies have shown that oligosaccharides exhibit dietary fiber properties. Dietary fibers pass to the large intestine without being digested in the small intestine and are fermented by the large intestine. Probiotic microorganisms, which are very important for intestinal health, require nutrients called prebiotics for their survival. They produce short-chain fatty acids (acetate, propionate, and butyrate) that are beneficial for the body by using dietary fibers that have a prebiotic effect. As a result, in this study, it is thought that modified starch-based products can be produced using the Gtfb enzyme, which is beneficial for both health and can be used in foods for various purposes.