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Merck
CN

A2986

淀粉酶,麦芽原性 来源于芽孢杆菌

greener alternative

别名:

诺和锐1000BG, 生麦芽糖淀粉酶, 葡聚糖1,4-α-麦芽分解酶

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UNSPSC代码:
12352204
eCl@ss:
32160410
NACRES:
NA.54
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生物来源

Bacillus sp.

质量水平

表单

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

相关类别

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

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
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
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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