Temperature and Rheology Studies of Microbial Lipase Solution

Irfan Majeed, Bhat (2007) Temperature and Rheology Studies of Microbial Lipase Solution. [Student Project Report]

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Abstract

This Dissertation / Report is the outcome of investigation carried out by the creator(s) / author(s) at the department/division of Central Food Technological Research Institute (CFTRI), Mysore mentioned below in this page.

Item Type:	Student Project Report
Additional Information:	Lipases (Triacyl glycerol hydrolases) catalyze the hydrolysis of ester linkages in lipids with release of fatty acids and alcohol. Microbial lipases are commercially significant especially in leather, dairy & oleochemical industries. This project discusses the temperature and rheological studies of microbial lipase solutions. A number of shake flask experiments conducted, confirmed the Bingham plastic behaviour of lipase solution. It was observed that lipases show loss in thermal stability below 350C temperature and maximum activity levels at 350C. With increase in temperature activity loss was observed. Shear inactivation of lipases was investigated at shear rates of 58.05 s-1, 97.02 s-1 and 161.64 s-1 which shows that lipases suffer minimum activity loss at lower shear rates and higher activity loss with increasing rate of shear and exposure time. Shear was applied on lipase solution in a viscometer (Haake VT500) and temperature effect without shear on lipase activity was observed using water bath.
Uncontrolled Keywords:	Aspergillus niger Lipases Rheology microbial lipase solutions temperature
Subjects:	600 Technology > 05 Chemical engineering > 04 Fermentation Technology 500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions:	Fermentation Technology and Bioengineering
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	18 Jun 2007 04:34
Last Modified:	28 Dec 2011 09:27
URI:	http://ir.cftri.res.in/id/eprint/1200

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