推荐产品
生物来源
Bacillus sp.
质量水平
形式
solid
环保替代产品特性
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
环保替代产品分类
储存温度
2-8°C
一般描述
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。
应用
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。
生化/生理作用
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。
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
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.
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
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
Dan Li et al.
New biotechnology, 27(4), 300-307 (2010-04-14)
A gene encoding a hyperthermostable maltogenic amylase of Staphylothermus marinus (SMMA) was cloned and overexpressed in Escherichia coli. SMMA consisted of 696 amino acids with a predicted molecular mass of 82.5 kDa. The enzyme was active in acidic conditions (pH
Shuang-Yan Tang et al.
The FEBS journal, 273(14), 3335-3345 (2006-07-22)
DNA shuffling was used to improve the thermostability of maltogenic amylase from Bacillus thermoalkalophilus ET2. Two highly thermostable mutants, III-1 and III-2, were generated after three rounds of shuffling and recombination of mutations. Their optimal reaction temperatures were all 80
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