biological source
Bacillus sp.
form
solid
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
greener alternative category
storage temp.
2-8°C
Quality Level
General description
我们致力于为您带来更加绿色的替代产品，这些产品遵守一项或多项绿色化学12项原则。当用于淀粉乙醇研究时，该产品经优化可提高能效和防止浪费。有关详细信息，请参阅 《Biofiles》的文章。
Application
麦芽糖淀粉酶（MAse）通常用于淀粉工业。 它们用于水解淀粉、支链淀粉和环糊精，并制备新的碳水化合物。
Biochem/physiol Actions
麦芽淀粉酶属于淀粉分解酶亚科，它也由环麦芽糊精酶、新普鲁兰酶和 普通热放线菌 淀粉酶II组成。这些酶将水解的糖部分转移到另一个糖分子。其具有（α/β）8桶和C结构域以及参与近似二聚体形成的124个残基N结构域。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
J L Uma Maheswar Rao et al.
Applied biochemistry and biotechnology, 142(2), 179-193 (2007-11-21)
The purified alpha-amylase of Geobacillus thermoleovorans had a molecular mass of 26 kDa with a pI of 5.4, and it was optimally active at 100 degrees C and pH 8.0. The T 1/2 of alpha-amylase at 100 degrees C increased
Jae-Hoon Shim et al.
Journal of bacteriology, 191(15), 4835-4844 (2009-05-26)
The physiological functions of two amylolytic enzymes, a maltogenic amylase (MAase) encoded by yvdF and a debranching enzyme (pullulanase) encoded by amyX, in the carbohydrate metabolism of Bacillus subtilis 168 were investigated using yvdF, amyX, and yvdF amyX mutant strains.
Tae-Yang Jung et al.
The Journal of biological chemistry, 287(11), 7979-7989 (2012-01-10)
Staphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 °C, which hydrolyzes α-(1-4)-glycosyl linkages in cyclodextrins and in linear malto-oligosaccharides. This enzyme has a long N-terminal extension that is conserved among
Hee-Kyung Bae et al.
Journal of agricultural and food chemistry, 50(11), 3309-3316 (2002-05-16)
Ascorbic acid (1), a natural antioxidant, was modified by employing transglycosylation activity of Bacillus stearothermophilus maltogenic amylase with maltotriose and acarbose as donor molecules to enhance its oxidative stability. The transglycosylation reaction with maltotriose as donor created mono- and di-glycosyl
Sung-Hoon Park et al.
Biochimica et biophysica acta, 1751(2), 170-177 (2005-06-25)
The goal of this study was to develop a maltose-producing enzyme using protein engineering and to clarify the relation between the substrate specificity and the structure of the substrate-binding site of dimeric maltogenic amylase isolated from Thermus (ThMA). Ala290 at
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