P2986
Pullulanase from Bacillus acidopullulyticus
aqueous solution, ≥400 units/mL
别名:
Promozyme™ 400L, Pullulan 6-glucano-hydrolase
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
EC Number:
232-983-9
MDL number:
form
aqueous solution
specific activity
≥400 units/mL
density
1.25 g/mL at 25 °C (lit.)
storage temp.
2-8°C
General description
Heat-stable debranching enzyme obtained from a selected strain of Bacillus acidopullulyticus, and belongs to the group of debranching enzymes known as pullulanases.
Other Notes
One unit is defined as the amount of enzyme which hydrolyzes pullulan, liberating reducing carbohydrate with a reducing power equivalent to 1.0 μmole glucose per minute at pH 5.0 and 40 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Legal Information
A product of Novozymes Corp.
Promozyme is a trademark of Novozymes Corp.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Yu-Liang Jiao et al.
Current microbiology, 62(1), 222-228 (2010-07-02)
The gene encoding a new extracellular amylopullulanase (type II pullulanase) was cloned from an extremely thermophilic anaerobic archaeon Thermococcus siculi strain HJ21 isolated previously from a deep-sea hydrothermal vent. The functional hydrolytic domain of the amylopullulanase (TsiApuN) and its MalE
Nan Jiang et al.
Wei sheng wu xue bao = Acta microbiologica Sinica, 51(6), 725-731 (2011-08-27)
Due to its ability of hydrolyzing alpha-1,6-linkages, pullulanase plays a significant role in the industries where starch is used as raw material, including food processing and bioenergy. Exploitation of this enzyme focuses not only on screening novel strains, but also
Fu-Pang Lin et al.
Applied biochemistry and biotechnology, 165(3-4), 1047-1056 (2011-07-14)
The enzymatically active region of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 (TsaNTOU1Apu) was identified by truncation mutagenesis. Two truncated TsaNTOU1Apu enzymes, TsaNTOU1ApuM957 and TsaNTOU1ApuK885, were selected and characterized. Both TsaNTOU1ApuM957 and TsaNTOU1ApuK885 showed similar specific activities toward various substrates. The overall