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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.

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

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: Endo-β-1,4-mannanase; Cross-linked enzyme aggregates; Chitosan magnetic nanocomposites; Thermal inactivation kinetics; β-manno-oligosaccharides
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Feb 2018 04:19
Last Modified: 03 Jun 2019 11:17
URI: http://ir.cftri.com/id/eprint/13406

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