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Cross-linked enzyme aggregates (CLEAs) and magnetic nanocomposite grafted CLEAs of GH26 endo-Beta-1,4-mannanase: Improved activity, stability and reusability.

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Relation http://ir.cftri.com/13406/
http://dx.doi.org/doi:10.1016/j.ijbiomac.2017.07.154
 
Title Cross-linked enzyme aggregates (CLEAs) and magnetic
nanocomposite grafted CLEAs of GH26
endo-Beta-1,4-mannanase: Improved activity, stability and
reusability.
 
Creator Deepesh, Panwar
Gaurav Singh, Kaira
Mukesh, Kapoor
 
Subject 05 Enzymes
 
Description A comparative study on immobilization of recombinant endo-β-1,4-mannanase (ManB-1601),
using cross-linked aggregated form (MB-C) and novel chitosan magnetic nanocomposites of
MB-C (MB-Mag-C) was carried out. FT-IR and Raman spectroscopy were used to confirm the
surface modifications while, scanning electron and atomic force microscopy were performed to
demonstrate the surface topology and magnetic nature of MB-C and MB-Mag-C. Among MB-C
and MB-Mag-C, the former showed better activity and stability in broad range of pH, thermostability
and kinetic parameters while, the latter showed higher temperature optima and solvent
stability. MB-C and MB-Mag-C when compared with free enzyme showed up to 73.2% higher
activity (pH 4-9), up to 95.6% higher stability (pH 3-10, 9 h incubation at room temperature), up
to 15 oC higher optimal temperature, higher stability (up to 83%) in the presence of solvents and
up to 1.62-fold higher deactivation energy (Ed). Immobilized enzymes were able to repeatedly
hydrolyze locust bean gum till 12 cycles and generated predominantly di-, tri- and tetra- species
of β-manno-oligosaccharides.
 
Date 2017
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/13406/1/International%20Journal%20of%20Biological%20Macromolecules%202017%20%282%29.pdf
Deepesh, Panwar and Gaurav Singh, Kaira and Mukesh, Kapoor (2017) Cross-linked enzyme aggregates (CLEAs) and magnetic nanocomposite grafted CLEAs of GH26 endo-Beta-1,4-mannanase: Improved activity, stability and reusability. International Journal of Biological Macromolecules, 105. pp. 1289-1299. ISSN 0141-8130