Isoamylase (EC 3.2.1.68), belonging to the glycoside hydrolase subfamily GH13-11. It catalyzes the hydrolysis of the α-1,6-D-glucosidic linkages in amylopectin, glycogen, and derived oligosaccharides. ISO has high hydrolytic activity against macromolecular substrates such as pullulan and glycogen, while low hydrolytic activity for small molecule branched dextrin. Isoamylase is mainly composed of three domains: terminal domain, domain, and C-terminal domain. Domain A consists of helixes and an (α/β)8-fold barrel structure. The C-terminal domain of isoamylase is composed of a small helix and a reverse fold, which is folded by 6 folded pieces to form a sandwich-type spatial structure. The two catalytic sites of glutamicacid/asparticacid (Glu/Asp) exist in the active center, which is an acid-base catalytic mechanism. ISO is used in food, feed, detergents, and other industries due to its high debranching efficiency and transglycosylation activity.
Fig.1 Overall structure of Isoamylase. (Woo E-J, et al., 2008)
In the starch granule state, the enzyme modification maintaining the semi-crystalline structure is a challenge. At CD BioGlyco, we offer high-stability isoamylase-treated starch manufacture and detection services. We have always been well received by customers with quality service and reliable products. The services we offer are as follows:
Fig.2 Flow chart of isoamylase modification. (CD BioGlyco)
CD BioGlyco has a Carbohydrate Manufacturing platform to provide you with a high-performance and cost-effective process. We provide high-quality Modified Starch Manufacturing services to customers all over the world. We will continue to improve the quality of our services to better meet customer needs. If you are interested in our services, please feel free to for more details.
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