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<span style="mso-bidi-language:HI">Purification and characterization of α-amylase from <i>Bacillus amyloliquefaciens</i> <span style="font-size:12.0pt;font-family:"Times New Roman";mso-fareast-font-family: "Times New Roman";mso-bidi-font-family:"Times New Roman";mso-ansi-language: EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:HI">NCIM 2829</span></span>

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Title Purification and characterization of α-amylase from Bacillus amyloliquefaciens NCIM 2829
 
Creator De, Mithu
Das, Kali P
Chakrabartty, P K
 
Subject α-Amylase
Bacillus amyloliquefaciens NCIM 2829
Circular dichroism
Fluorescence measurement
FT-IR spectroscopy
Secondary structure
Guanidine hydrochloride
Metal ions
Denaturation
 
Description 287-294
α-Amylase (EC 3.2.1.1) was purified to homogeneity
(specific activity 58,000 µmole min-1 mg protein-1) from
the culture filtrate of Bacillus amyloliquefaciens NCIM 2829. Its molecular
mass was found to be 67.5 kDa. The activity of the enzyme increased by almost
50% in the presence of Co+2 ion. Hg+2 and Cu+2
acted as strong inhibitors of the enzyme. The tryptophan moities of the enzyme
were fairly protected from the aqueous environment. However, the globular
interior of the protein was somewhat loosely packed. The protein had nearly an
equal amount of α-helical and β-sheet structure in dilute solution. In
concentrated solution, its secondary structure had a higher proportion of β-sheet
at the expense of some random coil structure. The protein showed a molten
globule state at a low concentration of chaotropic agent. The denaturation profile
of the protein showed no cooperativity. Co2+ enhanced the structural
stability of the enzyme.
 
Date 2015-01-16T11:41:42Z
2015-01-16T11:41:42Z
2005-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/30388
 
Language en_US
 
Relation C12N 9/28
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.42(5) [October 2005]