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Biosynthesis of Starch
Published in Jean-Luc Wertz, Bénédicte Goffin, Starch in the Bioeconomy, 2020
Jean-Luc Wertz, Bénédicte Goffin
Starch-branching enzymes (E.C. 2.4.1.18) belong to the α-amylase superfamily of enzymes (also termed glycoside hydrolase family 13, GH13; CAZy).6, 30 They cleave an α-1,4-glucan chain and transfer the cleaved portion to the C6 position of a glucose unit from the same or another chain, creating an α-1,6 linked branch. In this way, BEs generate additional substrates for the SSs (i.e., non-reducing ends of chains). BEs share a common three-domain structure: an N-terminal domain containing the CBM of family 48, a central catalytic α-amylase domain characteristic for GH13 family members, and a C-terminal domain present in several α-amylases (Figure 3.13).
Modeling and evaluation of the sucrose-degrading activity of recombinantly produced oligo-1,6-glucosidase from A. gonensis
Published in Preparative Biochemistry & Biotechnology, 2023
Hakan Karaoglu, Zeynep Dengız Balta
According to the CAZy database (http://www.cazy.org/), oligo-1,6-glucosidase (O-1-6-glucosidase) (EC 3.2.1.10) is a member of the glycoside hydrolase family 13 subfamily 31 (GH13_31).[10] O-1-6-glucosidase hydrolyzes non-reducing ends of isomaltooligosaccharides, panose, palatinose, and an a-limit dextrin by breaking α-1,6-glucoside bonds, although it generally lacks activity on α-1,4-glucoside bonds of maltooligosaccharides.[11] The enzyme is also called isomaltase, sucrase-isomaltase, dextrin 6-α-D glucanohydrolase, palatinase, and α-limit dextrinase. O-1-6-glucosidase is commonly used in the saccharification step of HFS production because it hydrolyzes branched oligosaccharides of short lengths and increasing glucose yield.[12] O-1-6-glucosidase can also hydrolyze sucrose to its monomers, glucose and fructose (Figure 1), which are valuable for HFS.[13] While, sucrose hydrolyzing activity was not studied for HFS production before, isomaltooligosaccharides hydrolyzing activity of O-1-6-glucosidase has been well-studied.[14] The microorganisms surviving above the temperature of 40 °C are categorized as thermophilic. Thermophilic microorganisms generally inhabit hot springs and have unique metabolites, especially physically and chemically stable enzymes. Recently, thermophilic microorganisms and their enzymes have been extensively researched due to their advantages for industrial applications.[15]