A2986
Amylase, Maltogenic from Bacillus sp.
Synonym(s):
Novamyl 1000BG, Glucan 1,4-α-maltohydrolase, Maltogenic Amylase
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10 G
$112.00
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$319.00
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10 G
$112.00
50 G
$319.00
About This Item
$112.00
Check Cart for Availability
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biological source
Bacillus sp.
Quality Level
form
solid
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
storage temp.
2-8°C
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
Maltogenic amylases (MAse) are commonly used in the starch industry. They are used to hydrolyze starch, pullulan and cyclodextrin and to make novel carbohydrates [1].
Biochem/physiol Actions
Maltogenic amylase is in the amylolytic enzyme subfamily, which also consists of cyclomaltodextrinase, neopullulanase, and Thermoactinomyces vulgaris amylase II. These enzymes transfer the hydrolyzed sugar moiety to another sugar molecule. They have an (α/β)8 barrel and C domain as well as a 124-residue N domain, which is involved in homodimer formation [1].
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Hee-Seob Lee et al.
The Journal of biological chemistry, 277(24), 21891-21897 (2002-03-30)
Over 20 enzymes denoted as cyclomaltodextrinase, maltogenic amylase, or neopullulanase that share 40-86% sequence identity with each other are found in public data bases. These enzymes are distinguished from typical alpha-amylases by containing a novel N-terminal domain and exhibiting preferential
Lili Kandra et al.
Carbohydrate research, 340(7), 1311-1317 (2005-04-28)
Synthesis of acarviosinyl-isomaltosyl-spiro-thiohydantoin in yields up to 20%, has been achieved by Bacillus stearothermophilus maltogenic amylase (BSMA). BSMA is capable of transferring the acarviosine-glucose residue from an acarbose donor onto glucopyranosylidene-spiro-thiohydantoin. Reactions were followed using HPLC and MALDI-TOF MS. 1H
T J Kim et al.
Biochemistry, 40(47), 14182-14190 (2001-11-21)
The relation between the quaternary structure and the substrate specificity of Thermus maltogenic amylase (ThMA) has been investigated. Sedimentation diffusion equilibrium ultracentrifugation and gel filtration analyses, in combination with the crystal structure determined recently, have demonstrated that ThMA existed in
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
Hee-Kyung Bae et al.
Journal of agricultural and food chemistry, 50(11), 3309-3316 (2002-05-16)
Ascorbic acid (1), a natural antioxidant, was modified by employing transglycosylation activity of Bacillus stearothermophilus maltogenic amylase with maltotriose and acarbose as donor molecules to enhance its oxidative stability. The transglycosylation reaction with maltotriose as donor created mono- and di-glycosyl
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