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Results for "

starch hydrolysis

" in MedChemExpress (MCE) Product Catalog:

14

Inhibitors & Agonists

2

Biochemical Assay Reagents

5

Natural
Products

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-B2193
    α-Amylase
    2 Publications Verification

    Environmental Pollutants Amylases Others
    α-Amylase is a hydrolase enzyme that catalyses the hydrolysis of internal α-1, 4-glycosidic linkages in starch to yield products like glucose and maltose.
    α-Amylase
  • HY-W145519

    Environmental Pollutants Biochemical Assay Reagents Cardiovascular Disease
    Hydroxyethyl starch (MW170-230 kDa) is a type of hydroxyethyl starch with a molecular weight of 170-230 kDa. A medium-molecular-weight hydroxyethyl starch (HES 200/0.62) exhibits minimal intravascular hydrolysis. The rapidly degradable medium-molecular-weight Hydroxyethyl starch 200/0.5 causes almost no coagulation disorders and improves hemorheological parameters .
    Hydroxyethyl starch (MW170-230 kDa)
  • HY-W115731

    Environmental Pollutants Endogenous Metabolite Biochemical Assay Reagents Others
    Dextrins are a group of low molecular weight carbohydrates produced by the hydrolysis of starch. Dextrin is commonly used as a thickener, stabilizer or binder in a variety of foods including baked goods, beverages and confectionary. In addition, it is used in the production of adhesives, paper and textiles. Its unique chemical properties make it an important ingredient in a variety of industrial processes, especially in construction and packaging.
    Dextrin
  • HY-B2192

    Amylases Metabolic Disease Cancer
    Amylase is an enzyme produced by pancreas and salivary glands, catalyzing the hydrolysis of starch into sugars. Amylase are broadly classified into α, β, and γ subtypes .
    Amylase
  • HY-P2968

    Amylases Others
    Bacterial α-Amylase catalyses the hydrolysis of internal α-1,4-glycosidic linkages in starch in low molecular weight products, such glucose, maltose and maltotriose units. Bacterial α-Amylase is often used in biochemical studies .
    Bacterial α-Amylase
  • HY-N6675

    Amylases Glycosidase Inflammation/Immunology
    Gardenia yellow is a competitive inhibitor of α-Amylase (HY-B2193) and α-glucosidase. Gardenia yellow can bind to the catalytic sites of α-Amylase and α-glucosidase, inhibit starch digestion, and significantly increase the contents of resistant starch and slowly digestible starch in starch-based systems. Gardenia yellow reduces the glycemic index and hydrolysis index. Gardenia yellow can be used in diabetes-related research .
    Gardenia yellow
  • HY-B2193A

    1,4-alpha-D-Glucan-glucanohydrolase, ptyalin

    Biochemical Assay Reagents Metabolic Disease Inflammation/Immunology
    α-Amylase, Human Saliva (1,4-alpha-D-Glucan-glucanohydrolase) is a hydrolase enzyme that can be isolated from human saliva. α-Amylase, Human Saliva catalyses the hydrolysis of internal α-1, 4-glycosidic linkages in starch to yield products like glucose and maltose. α-Amylase, Human Saliva can be used in life science research .
    α-Amylase, Human Saliva
  • HY-B2193C

    1,4-alpha-D-Glucan-glucanohydrolase, amy2, PPA, PA

    Biochemical Assay Reagents Others
    α-Amylase, Porcine Pancreatic (1,4-alpha-D-Glucan-glucanohydrolase) is a hydrolase enzyme that can be isolated from porcine pancreatic. α-Amylase, Porcine Pancreatic catalyses the hydrolysis of internal α-1, 4-glycosidic linkages in starch to yield products like glucose and maltose. α-Amylase, Porcine Pancreatic can be used in life science research .
    α-Amylase, Porcine Pancreatic
  • HY-B2193B

    Amylase, a-Amylase, 1,4-a-D-glucan glucanohydrolase, glycogenase

    Biochemical Assay Reagents Others
    α-Amylase, Human Pancreas (Amylase) is a hydrolase enzyme that can be isolated from human pancreas. α-Amylase, Human Pancreas catalyses the hydrolysis of internal α-1, 4-glycosidic linkages in starch to yield products like glucose and maltose. α-Amylase, Human Pancreas can be used in life science research .
    α-Amylase, Human Pancreas
  • HY-B2192A

    Maltin

    Biochemical Assay Reagents Others
    Diastase, Aspergillus oryzae (Maltin) is a starch hydrolase derived from Aspergillus oryzae. Diastase, Aspergillus oryzae catalyzes starch hydrolysis through sequential stages, first producing dextrins, then glucose and maltose .
    Diastase, Aspergillus oryzae
  • HY-N8326

    Others Others
    Maltononaose is a linear oligosaccharide consisting of 9 glucose units linked by alpha-1, 4-glucoside bonds. Maltononaose is used as a substrate to study the subsites affinity of glucoamylase. Maltononaose can be used to determine the activity of amylase and to optimize the process of starch hydrolysis .
    Maltononaose
  • HY-E70118

    Glycosidase Others
    oligo-α-1,6-Glucosidase, Bacillus cereus ATCC7064 is a hydrolase that mainly hydrolyzes oligosaccharides with α-1,6-glycosidic bonds. oligo-α-1,6-Glucosidase, Bacillus cereus ATCC7064 can catalyzes the exo hydrolysis of α-1,6-glucoside bonds from the nonreducing ends of panose, palatinose, α-limit dextrins, and isomaltooligosaccharides. oligo-α-1,6-Glucosidase, Bacillus cereus ATCC7064 participates in the degradation pathway of starch and glycogen, assisting enzymes such as α-amylase to completely hydrolyzes amylopectin .
    oligo-α-1,6-Glucosidase, Bacillus cereus ATCC7064
  • HY-B2193F

    Amylases Metabolic Disease
    Amylase, Human (HEK293) is an enzyme, catalyzing the hydrolysis of starch into sugars. Amylase are broadly classified into α, β, and γ subtypes .
    Amylase, Human (HEK293)
  • HY-N18049

    Amylases Metabolic Disease
    Decussatin is an α-Amylases inhibitor isolated from the Tibetan medicinal plant Swertia mussotii. By inhibiting the catalytic activity of α-Amylases, Decussatin reduces the hydrolysis of complex carbohydrates such as starch and the intestinal absorption of glucose, thereby lowering blood glucose levels in the body. Decussatin shows no significant in vitro antibacterial or antifungal activity. Decussatin can be used for the research of type 2 diabetes .
    Decussatin

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