glucoamylase


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glucoamylase

/glu·co·am·y·lase/ (gloo″ko-am´ĭ-lās) acid maltase.

glucoamylase

see amylase.
References in periodicals archive ?
Isolation and screening of a-amylase and glucoamylase producing fungi and their application in bioethanol production.
Production of thermostable glucoamylase by newly isolated Aspergillus flavus A.
Traits of higher capacity of glucoamylase production strains were shown in Table 1.
Guo C, Yunhui M, Pengfei S, Baishan F (2012) Direct binding glucoamylase onto carboxyl-functioned magnetic nanoparticles.
For example, the activation energies of immobilized glucoamylase and [beta]-galactosidase were almost the same as their free counterparts.
Optimization of a-amylase and glucoamylase production from three fungal strains isolated from Abakaliki, Ebonyi State.
Isolation and screening of a-amylase and Glucoamylase producing fungi and their Glucomaylase producing fungi and their application in Bioethanol production.
Physiochemical properties and kinetics of glucoamylase produced from deoxy-D-glucose resistant mutant of Aspergillus niger for soluble starch hydrolysis.
Dietary Supplements ENZYME DIGESTIVE SYSTEMIC CARBOHYDRASES [alpha]-Amylase X Glucoamylase X (aka amyloglucosidse) Diastase X Invertase X Lactase X [alpha]-Galactosidase X Cellulase X Hemicellulase X Pectinase X [beta]-Glucanase X Xylanase X PROTEASES Bromelain X X Papain X X Protease X X Peptidase X X Chymotrypsin X X Trypsin X X Pepsin X X LIPASES Lipase X Pancreatin X Pancrelipase X OTHER ENZYMES Catalase X X Lactoferrin X Lactoperoxidase X Lysozyme X Super Oxide X X Dismutase (SOD) COMMON ACTIVITY ENZYME COMMON SOURCE ORGANISMS UNITS CARBOHYDRASES [alpha]-Amylase Aspergillus oryzae, A.
Purification and properties of two forms of glucoamylase from Aspergillus niger.
4] MTCC174 Crude unprocessed enzyme ATCC 26602 cellulase SOL/M5 Crude extract from Pleurotus ostreatus L2524a Cellulase TJ14 Commercial cellulase Y5 Cellulase and [beta]-glucosidase ATCC 6508 [alpha]-Amylase and glucoamylase Baker yeast Hydrolysis by [H.