Glucoamylase, Rhizopus sp. (g-Amylase, EC 3.2.1.3, Glucan 1,4-a-glucosidase, amyloglucosidase, Exo-1,4-a-glucosidase, lysosomal a-glucosidase, 1,4-a-D-glucan glucohydrolase)

Glucoamylase In addition to cleaving the last a(1-4)glycosidic linkages at the nonreducing end of amylose and amylopectin, yielding glucose, g-amylase will cleave a(1-6) glycosidic linkages. Unlike the other forms of amylase, g-amylase is most efficient in acidic environments and has an optimum pH of 3. Amylase enzymes are used extensively in bread making to break down complex sugars such as starch (found in flour) into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of alcohol and CO2. This imparts flavor and causes the bread to rise. While Amylase enzymes are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. This is the reason for long fermented doughs such as sour dough. Modern bread making techniques have included amylase enzymes (often in the form of malted barley) into bread improver thereby making the bread making process faster and more practical for commercial use.\n\nBacilliary amylase is also used in detergents to dissolve starches from fabrics. Workers in factories that work with amylase for any of the above uses are at increased risk of occupational asthma. 5-9% of bakers have a positive skin test, and a fourth to a third of bakers with breathing problems are hypersensitive to amylase. An inhibitor of alpha-amylase called phaseolamin has been tested as a potential diet aid. Blood serum amylase may be measured for purposes of medical diagnosis. A normal concentration is in the range 21-101 U/L. A higher than normal concentration may reflect one of several medical conditions, including acute inflammation of the pancreas, macroamylasemia, perforated peptic ulcer, and mumps. Amylase may be measured in other body fluids, including urine and peritoneal fluid.\n\nSource:\n1,4-a-D-Glucan glucohydrolase (EC 3.2.1.3.) from rhizopus sp.\n\nReaction Equation: Starch + nH2O = nGlucose\n\nContaminants: a-Amylase (same/less than) 0.001%\n\nPowder Activity: (same/more than)10u/mg powder (37 degrees C, pH 6.0)\n\nSpecific Activity: (same/more than) 20u/mg protein (37 degrees C, pH 6.0)\n\nAppearance: Lyophilized powder with white to light brown color\n\nSolubility: Colorless, transparent liquid\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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