Literature summary for 3.2.1.1 extracted from

Gashtasbi, F.; Ahmadian, G.; Noghabi, K.A.
New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization (2014), Enzyme Microb. Technol., 64-65, 17-23.

Search for more literature for 3.2.1.1

Application

Application	Comment	Organism
synthesis	use of probiotic Bacillus spores as a matrix for enzyme immobilization by covalent and adsorption methods. The maximum concentration of the alpha-amylase immobilized is 360 microg/1.2 10EE11spores. Maximum activity is achieved at an enzyme concentration of approximately 60 microg/0.4 10EE10 spores, corresponding to an estimated activity of 8000 IU per mg and 1.2 10EE11 spores for covalent immobilization and 85300 IU for the adsorption method. Enzyme immobilization yield is estimated to be 77% and 20.07% for the covalent and adsorption methods, respectively. The alpha-amylase immobilized by both methods, displays improved activity in the basic pH range. The optimum pH for the free enzyme is 5 while it shifts to 8 for the immobilized enzyme. The optimum temperatures for the free and immobilized enzymes are 0C and 0C, respectively. The covalently immobilized alpha-amylase retains 65% of its initial activity, even after 10 times of recycling	Bacillus licheniformis

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus licheniformis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
55000	-	x * 55000, SDS-PAGE	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Subunits

Subunits	Comment	Organism
?	x * 55000, SDS-PAGE	Bacillus licheniformis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)