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<i style="mso-bidi-font-style:normal"><span style="font-size:13.0pt;mso-bidi-font-size:10.0pt;font-family:"Times New Roman","serif"; mso-fareast-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB">Pongamia pinnata</span></i><span style="font-size:13.0pt;mso-bidi-font-size:10.0pt;font-family:"Times New Roman","serif"; mso-fareast-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB"> seed cake: A promising and inexpensive substrate for production of protease and lipase from <i style="mso-bidi-font-style: normal">Bacillus pumilus</i> SG2 on solid-state fermentation</span>

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Title Pongamia pinnata seed cake: A promising and inexpensive substrate for production of protease and lipase from Bacillus pumilus SG2 on solid-state fermentation
 
Creator Sangeetha, R
Geetha, A
Arulpandi, I
 
Subject Lipase
Protease
Solid state fermentation
Pongamia pinnata seed cake
 
Description 435-439
The
production of a protease and a lipase from Bacillus
pumilus SG2 on solid-state fermentation using Pongamia pinnata seed cake as substrate was studied. The seed cake
was proved to be a promising substrate for the bacterial growth and the enzyme
production. The initial pH, incubation time and moisture content were optimized
to achieve maximal enzyme production. Maximum protease production was observed
at 72 h and that
of the lipase at 96 h of incubation. The production of protease (9840 U/g DM)
and lipase (1974 U/g DM) were maximum at
pH 7.0 and at 60% moisture content. Triton X-100 (1%) was proved to be an
effective extractant for the enzymes and their optimal activity was observed at
alkaline pH and at 60ºC. The molecular mass of the protease and lipase was 24
and 40 kDa, respectively. Both the enzymes were found to be stable detergent
additives. The study demonstrated that inexpensive and easily available Pongamia seed cake could be used for
production of industrially important enzymes, such as protease and lipase.
 
Date 2011-12-23T10:34:54Z
2011-12-23T10:34:54Z
2011-12
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/13259
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(6) [December 2011]