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Evidence of structural changes of an enzymatic extract entrapped into alginate beads

Paper ID Volume ID Publish Year Pages File Format Full-Text
3438 171 2013 6 PDF Available
Title
Evidence of structural changes of an enzymatic extract entrapped into alginate beads
Abstract

In this work, we analyzed the structural changes of araujiain entrapped into alginate beads. Araujiain is an enzymatic preparation containing three known enzymatic fractions with each fraction individually presenting a similar catalytic performance. Fluorescence and infrared spectroscopy, thermal analysis and residual catalytic activity studies were carried out. A small red shift in the spectrum of araujiain was observed after the entrapment process. Changes in the polarity around the tryptophan (Trp) residues were associated with an enzyme conformational change. From the Fourier transform infrared spectroscopy (FTIR) analysis, it was demonstrated that interactions between the enzyme extract and Ca alginate caused different structural behavior in araujiain. According to the diffuse reflectance infrared Fourier transform spectroscopy (DRIFT) study, it was possible to conclude that a secondary structure with a high α-helical character was responsible for the highest activity of entrapped araujiain. Finally, from thermal analysis measurements, it was proved that entrapment of araujiain augments the thermal stability of both the enzyme extract and Ca alginate, indicating a possible interaction between enzyme extract and its support.

► We analyzed the structural changes of araujiain entrapped into alginate beads. ► A small red shift in the spectrum of the enzyme entrapped was observed indicating that Trp residues have more polarizable surroundings. ► A secondary structure with a high α-helical character was responsible for the highest activity of entrapped araujiain. ► Interactions between the enzyme extract and Ca alginate caused different structural behavior in araujiain. ► Entrapment of araujiain augments the thermal stability of both the enzyme extract and Ca alginate.

Keywords
Araujiain; Entrapment; Alginate beads; Conformational changes; Enzyme stabilization; Immobilization of enzymes
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Evidence of structural changes of an enzymatic extract entrapped into alginate beads
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 70, 15 January 2013, Pages 23–28
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