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A7595

Sigma-Aldrich

α-Amylase from Bacillus amyloliquefaciens

greener alternative

liquid, ≥250 units/g

Synonyme(s) :

BAN 480L, 1,4-α-D-Glucan Glucano-hydrolase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
3.2.1.1.
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Forme

liquid

Niveau de qualité

Activité spécifique

≥250 units/g

Poids mol.

55 kDa

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

Autre catégorie plus écologique

Température de stockage

2-8°C

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Description générale

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.

Actions biochimiques/physiologiques

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).

Définition de l'unité

One unit is the amount of enzyme which dextrinizes 5.26 g of dry starch per hour under standard conditions.

Informations légales

A product of Novozyme Corp.
BAN is a trademark of Novozymes Corp.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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

Protocoles

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

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