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Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures

Paper ID Volume ID Publish Year Pages File Format Full-Text
18663 42732 2006 9 PDF Available
Title
Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures
Abstract

Extracellular lipases were obtained from solid (SSF) and submerged (SmF) thermotolerant Rhizopus homothallicus fungus cell cultures and purified to homogeneity. The two enzymes are monomers having a molecular mass of 29.5 kDa and an identical protein structure, since the N-terminal sequences and peptide maps were identical. However, some of their properties are different, namely the specific activity on trioctanoin (8600 U/mg with SmF and 10,700 U/mg with SSF), the temperature at which maximum activity occurs (30 °C with SmF and 40 °C with SSF) and the thermal stability (half-lives at 50 °C of 0.44 h with SmF and 0.72 h with SSF). These differences between the kinetic properties suggest that when they were tested, one or both fungal lipases might still have been associated with non-proteic compounds originating from the culture medium.

Keywords
Rhizopus homothallicus; Thermophilic and thermotolerant fungi; Solid state fermentation; Submerged fermentation; Lipase; Purification
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Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 5, 4 September 2006, Pages 1042–1050
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
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