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<span style="mso-bidi-font-weight:bold" lang="EN-IN">Characterization of a thermostable α-amylase from a thermophilic <i>Streptomyces</i> <i><span style="font-size:12.0pt;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";mso-ansi-language:EN-IN;mso-fareast-language: EN-IN;mso-bidi-language:AR-SA" lang="EN-IN">megasporus </span></i><span style="font-size:12.0pt;font-family:"Times New Roman";mso-fareast-font-family: "Times New Roman";mso-ansi-language:EN-IN;mso-fareast-language:EN-IN; mso-bidi-language:AR-SA;mso-bidi-font-weight:bold" lang="EN-IN">strain SD12</span></span>

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Title Characterization of a thermostable α-amylase from a thermophilic Streptomyces megasporus strain SD12
 
Creator Dey, Sabita
Agarwal, Shubha O
 
Description 150-157
An extracellular
α-amylase (1,4-α D-glucan glucan hydrolase; EC 3.2.1.1 ) was isolated from the
cell free broth of Streptomyces megasporus SD12 grown in glucose,
soluble starch and raw starch. The enzyme was purified 55-fold with a specific
activity of 847.33 U mg-1 of protein and with a yield of 36%
activity. The apparent molecular mass of the enzyme was 97 kDa, as estimated by
SDS-PAGE. The pI of the
enzyme was 5.4 and it was stable at a pH range of 5.5 to 8.5 with an optimum pH 6. The enzyme was stable
upto 85°C with a half life of 60 min. With soluble starch as
substrate the enzyme exhibited a Km and kcat value
of 4.4 mg ml-1 and 2335 U min-1 mg" of protein
respectively. The major end products of starch hydrolysis were maltotriose and
maltose depending on the incubation period. The production of the enzyme with agricultural
wastes as substrates was 643 to 804 U min-1 mg-1 of protein
in submerged fermentation whereas solid state fermentation could produce only
206 U min-1 mg-1 of protein.
 
Date 2012-12-31T19:18:46Z
2012-12-31T19:18:46Z
1999-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15436
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.36(3) [June 1999]