A7595
α-Amylase from Bacillus amyloliquefaciens
liquid, ≥250 units/g
Synonym(s):
BAN™ 480L, 1,4-α-D-Glucan Glucano-hydrolase
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About This Item
CAS Number:
Enzyme Commission number:
3.2.1.1.
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
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form
liquid
Quality Level
specific activity
≥250 units/g
mol wt
55 kDa
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
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greener alternative category
, Enabling
storage temp.
2-8°C
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General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.
Application
α-Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. Product A7595 is from Bacillus amyloliquefaciens and is supplied as a liquid. α-Amylase has been used in various plant studies, such as metabolism studies in Arabidopsis. α-Amylase from Bacillus amyloliquefaciens has been used to hydrolyze sweetpotato amylopectin to identify cluster structure. The enzyme has been used to hydrolyze sago palm starch to reducing sugars, which are then used for ethanol fermentation by Saccharomyces cerevisiae FNCC 3012. The enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars.
Biochem/physiol Actions
α-Amylase is an endoamylase that randomly hydrolyzes the α-(1,4) glucan linkages in amylose and amylopectin. The breakdown products are oligosaccharides and dextrins of varying chain length. This enzyme works best at high temperatures, in the range of 70-90 ° Celcius.
The pH range for the α-amylase of B.amyloliquefaciens is 5.5 to 6.5, with a single maximum at 5.9. The activity is rapidly inactivated below pH 5.0.
An endoamylase that randomly hydrolyzes α-(1→4)-glycosidic linkages in amylose and amylopectin. The breakdown products are oligosaccharides and dextrins of varying chain length. This enzyme is active at high temperatures (70−90 °C).
Unit Definition
One unit is the amount of enzyme which dextrinizes 5.26 g of dry starch per hour under standard conditions.
Legal Information
A product of Novozyme Corp.
BAN is a trademark of Novozymes Corp.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
Certificates of Analysis (COA)
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Enzymatic and Acid Hydrolysis of Sago Starch for Preparation of Ethanol Production
Sunaryanto R, et al.
Microbiology Indonesia, 7(2), 68-74 (2013)
Annabel Bijttebier et al.
Carbohydrate research, 345(2), 235-242 (2009-12-08)
Amylopectin fine structures were studied following limited hydrolysis of gelatinised waxy maize starch by amylases with a different level of inner chain attack (LICA). This was done by size exclusion chromatography as well as by debranching the (partially hydrolysed) amylopectin
Fan Zhu et al.
Carbohydrate research, 346(9), 1112-1121 (2011-04-22)
Sweetpotato amylopectin was subjected to partial hydrolysis by α-amylase from Bacillus amyloliquefaciens to release the clusters. Clusters were then fractionated and precipitated by methanol and structurally characterized by gel-permeation chromatography and high-performance anion-exchange chromatography. An initial stage of α-amylolysis on
Lizhi Zhang et al.
The Plant cell, 22(11), 3603-3620 (2010-11-16)
Seed development and nitrogen (N) storage depend on delivery of amino acids to seed sinks. For efficient translocation to seeds, amino acids are loaded into the phloem in source leaves and along the long distance transport pathway through xylem-phloem transfer.
Phuong Lan Tran et al.
FEBS letters, 588(4), 620-624 (2014-01-21)
The action pattern of Bacillus licheniformis thermostable α-amylase (BLA) was analyzed using a series of (14)C-labeled and non-labeled maltooligosaccharides from maltose (G2) to maltododecaose (G12). Maltononaose (G9) was the preferred substrate, and yielded the smallest Km=0.36 mM, the highest kcat=12.86
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