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Effect of deglycosylation on the properties of thermophilic invertase purified from the yeast Candida guilliermondii MpIIIa

Paper ID Volume ID Publish Year Pages File Format Full-Text
34657 45038 2014 8 PDF Available
Title
Effect of deglycosylation on the properties of thermophilic invertase purified from the yeast Candida guilliermondii MpIIIa
Abstract

•The invertase from Candida guilliermondii MpIIIa was purified and characterized.•So far, INV3a-N is the yeast invertase with the highest percentage of glycosylation.•INV3a-N is thermophilic and active in a wide range of pH and temperature values.•INV3a-N is active at high sucrose concentrations (up to 2 M sucrose).•Glycosylation plays a crucial role in inhibition of INV3a-N by sucrose.

Invertase from Candida guilliermondii MpIIIa was purified and biochemically characterized. The purified enzyme (INV3a-N) is a glycoprotein with a carbohydrate composition comprising nearly 74% of its total molecular weight (MW) and specific activity of 82,027 U/mg of protein. The enzyme displayed optimal activity at pH 5.0 and 65 ˚C. The Km and Vmax values for INV3a-N were 0.104 mM and 10.9 μmol/min/mg of protein, respectively, using sucrose as the substrate. The enzyme retained 50% and 20% of its maximal activity after 168 h and 30 days, respectively, at 50 ˚C. INV3a-N was fully active at sucrose concentrations of 400 mM and the activity of the enzyme dropped slowly at higher substrate concentration. Interestingly, the deglycosylated form of INV3a-N (INV3a-D) displayed 76–92% lower thermostability than that of INV3a-N at all temperatures assayed (50–70 ˚C), and was inhibited at sucrose concentrations of 200 mM. Findings here indicate glycosylation plays an important role, not only in the thermostability of INV3a-N, but also in the inhibition of the enzyme by sucrose. Since the enzyme is active at high sucrose concentrations, INV3a-N may be considered a suitable candidate for numerous industrial applications involving substrates with high sugar content or for improvement of ethanol production from cane molasses.

Keywords
Candida guilliermondii; Invertase; Glycosylation; Substrate inhibition; Thermostability
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Effect of deglycosylation on the properties of thermophilic invertase purified from the yeast Candida guilliermondii MpIIIa
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 9, September 2014, Pages 1480–1487
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
Full-text PDF Download
Online Support
Any Questions? feel free to contact us