starch

Hydroxypropyl starch (2-Hydroxypropyl starch) is a modified starch used for food addition. It is not absorbed intact by the intestinal tract, but can be significantly hydrolyzed by intestinal enzymes and subsequently fermented by intestinal flora.

Hydroxyethyl starch (Mw 110-150 kDa) is a biochemical reagent used in research, including drug delivery studies.

Starch soluble is a biochemical reagent utilized as a biomaterial or organic compound in life science research.

Hydroxyethyl starch is a biochemical reagent that can be used as a biomaterial for life science related research and as a sulfonylation reagent for organic synthesis and drug discovery.

Maltose (maltobiose) is a reducing sugar, a disaccharide formed by two glucose units linked via a (1-4) bond. It functions as a carbon source, regulates osmotic pressure, and provides antioxidant properties. Maltose serves as an efficient carbon source for yeast, bacteria, and fungi.

Amylose is a polysaccharide composed of α-D-glucose units linked by α(1→4) glycosidic bonds, accounting for about 20% of the total amount of starch. Amylose spatial conformation curls into a helix and forms a blue complex with iodine, which is widely used in the food industry, and can be used in a variety of researches as a natural product and a biochemical reagent.

Amylopectin is a highly branched polysaccharide based on glucose. It forms starch together with amylose. The glycosidic bond of amylopectin is α- Glucan chain α- 1, 4 and branching points α- 1,6.

ADP-Glucose (ADPG) is an immediate precursor used in the biosynthesis, by glucose addition, of storage polysaccharides in plants, green algae, and cyanobacteria, as well as structural polysaccharides in certain bacteria.[1],[2] It is used by amylose synthases or starch synthases in plastids in the production of amylose, amylopectins, starch, and other polysaccharides. ADPG is normally generated within plastids, although it can be biosynthesized in the cytoplasm of certain grasses and imported into plastids by a membrane-bound transporter.[3]

Octenyl succinic anhydride (OSA) is utilized to esterify starch, producing octenyl succinylated starch (OS-starch), a hydrocolloid with amphiphilic properties. This modification by OSA influences the interaction between molecules on the outer surface of starch granules through alterations in molecular structures.

Pullulanase (R-enzyme), a starch debranching enzyme utilized in biochemical research, cleaves α-1,6 glucosidic linkages in starch, amylopectin, pullulan, and related oligosaccharides. This conversion of polysaccharides into smaller fermentative sugars facilitates saccharification processes [1].

Maltononaose is a linear oligosaccharide consisting of 9 glucose units linked by α-1,4-glycosidic bonds. It is commonly used as a substrate for starch-hydrolyzing enzymes such as glucoamylase, for studying enzyme subsite binding characteristics and activity determination.

β-Phosphoglucomutase, from Lactococcus sp. (EC 5.4.2.6), is part of the isomerase family and catalyzes the conversion of β-D-glucose-1-phosphate to β-D-glucose-6-phosphate. This enzyme plays a role in the metabolism of starch and sucrose.

β-Phosphoglucomutase, E. coli (EC 5.4.2.6), is an enzyme from the isomerase family that catalyzes the conversion of β-D-glucose-1-phosphate to β-D-glucose-6-phosphate. This enzyme plays a role in the metabolism of starch and sucrose.

Trehalose-6-phosphate hydrolase, Escherichia coli (EC 3.2.1.93), is a member of the hydrolase family, functioning as a glycosidase that hydrolyzes O- and S-glycosyl compounds. This enzyme plays a role in the metabolism of starch and sucrose, with substrates α,α-trehalose-6-phosphate and water, producing D-glucose and D-glucose-6-phosphate.

α-Amylase, Porcine (EC 3.2.1.1), is a protein enzyme that hydrolyzes the α-glycosidic bonds in large α-linked polysaccharides such as starch and glycogen, resulting in the formation of glucose and maltose.

Trehalose-6-phosphate hydrolase, also known as Bacillus subtilis (EC 3.2.1.93), is part of the hydrolase enzyme family specializing in the hydrolysis of O- and S-glycosidic compounds. It plays a role in the metabolism of starch and sucrose. The substrates for this enzyme are α,α'-trehalose-6-phosphate and water, producing D-glucose and D-glucose-6-phosphate as products.

α-Amylase, Bacteroides fragilis (EC 3.2.1.1), is a protein enzyme that hydrolyzes the α-glycosidic bonds in large α-linked polysaccharides such as starch and glycogen, resulting in the production of glucose and maltose.

α-Glucosidase, Saccharomyces cerevisiae (EC 3.2.1.20), is an enzyme classified as a glucosidase found in the brush border of the small intestine. It acts on 1,4-α-glycosidic bonds to break down starch and disaccharides into glucose.

α-Amylase, Escherichia coli (EC 3.2.1.1) is a protein enzyme that hydrolyzes the α-glycosidic bonds of large α-linked polysaccharides, such as starch and glycogen, producing glucose and maltose.