Immobilization of indigenous holocellulase on iron oxide (Fe2O3) nanoparticles enhanced hydrolysis of alkali pretreated paddy straw

Ajay Kumar, Surender Singh*, Rameshwar Tiwari, Renu Goel, Lata Nain

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

The holocellulase from Aspergillus niger SH3 was characterized and found to contain 125 proteins including cellulases (26), hemicellulases (21), chitinases (10), esterases (6), amylases (4) and hypothetical protein (32). The crude enzyme was immobilized on five different nanoparticles (NPs) via physical adsorption and covalent coupling methods. The enzyme-nanoparticle complexes (ENC) were screened for protein binding, enzymatic activities and immobilization efficiency. Magnetic enzyme-nanoparticle complexes (MENC) showed higher immobilization efficiency (60–80%) for most of the enzymes. MENC also showed better catalytic efficiencies in term of higher Vmax and lower Km than free enzyme. Saccharification yields from alkali treated paddy straw were higher (375.39 mg/gds) for covalently immobilized MENC than free enzyme (339.99 mg/gds). The immobilized enzyme was used for two cycles of saccharification with 55% enzyme recovery. Hence, this study for the first time demonstrated the immobilization of indigenous enzyme and its utilization for saccharification of paddy straw.

Original languageEnglish (US)
Pages (from-to)538-549
Number of pages12
JournalInternational Journal of Biological Macromolecules
Volume96
DOIs
StatePublished - Mar 1 2017
Externally publishedYes

Keywords

  • Aspergillus niger
  • Extracellular proteome
  • Glycoside hydrolase
  • LC MS/MS
  • Proteomics
  • Solid-state fermentation

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

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