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Title: Immobilization of cellulase on a silica gel substrate modified using a 3-APTES self-assembled monolayer

Cellulase was immobilized onto silica gel surfaces pretreated with (3-aminopropyl) triethoxy-silane (3-APTES), and glutaraldehyde (GA) was used as a cross-linker. A carboxymethyl cellulose sodium salt (CMC) solution was used for activity experiments. Protein assay was performed to determine the mass immobilized and compare with free enzyme. Cellulase was successfully demonstrated to be immobilized on the modified silica gel surface, and no detectable amount of enzyme was stripped off during the hydrolysis of the CMC solution. The specific activity of the immobilized cellulase is 7 ± 2 % compared to the similar amount of free cellulase. Significant activity over multiple reuses was observed. The seventh batch achieved 82 % activity of the initial batch, and the fifteenth batch retained 31 %. Lastly, it was observed that the immobilized cellulase retained 48 % of its initial activity after 4 days, and 22 % even after 14 days.
Authors:
 [1] ;  [1] ;  [1] ;  [1] ;  [1]
  1. Louisiana Tech Univ., Ruston, LA (United States)
Publication Date:
Grant/Contract Number:
EE0003120
Type:
Published Article
Journal Name:
SpringerPlus
Additional Journal Information:
Journal Volume: 5; Journal Issue: 1; Journal ID: ISSN 2193-1801
Publisher:
Springer
Research Org:
Louisiana Tech Univ., Ruston, LA (United States)
Sponsoring Org:
USDOE Office of Energy Efficiency and Renewable Energy (EERE)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; cellulase; (3-Aminopropyl) triethoxy-silane; glutaraldehyde; glucose; silica gel
OSTI Identifier:
1272638
Alternate Identifier(s):
OSTI ID: 1242890