| Literature DB >> 28131958 |
Ibrahim Nasser Ahmed1, Ray Chang1, Wei-Bor Tsai2.
Abstract
Cellulase was adsorbed onto poly(acrylic acid), PAA, nanogel, that was fabricated via inverse-phase microemulsion polymerization. The PAA nanogel was around 150nm in diameter and enriched with carboxyl groups. The surface charge of PAA nanogel depended on the pHs of the environment and affected the adsorption of cellulase. The temperature stability of the immobilized cellulase was greatly enhanced in comparison to the free enzyme, especially at high temperature. At 80°C, the immobilized cellulase remained ∼75% of hydrolytic activity, in comparison to ∼55% for the free cellulase. Furthermore, the immobilized cellulase was more active than the free enzyme in acidic buffers. The immobilized cellulase could be recovered via centrifugation and can be used repeatedly, although the recovery ratio needs further improvement. In conclusion, PAA nanogel has the potential in the application of enzyme immobilization for biochemical processes.Entities:
Keywords: Cellulase; Cellulose; Enzyme stability; Nanogel; Poly(acrylic acid)
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Year: 2017 PMID: 28131958 DOI: 10.1016/j.colsurfb.2017.01.040
Source DB: PubMed Journal: Colloids Surf B Biointerfaces ISSN: 0927-7765 Impact factor: 5.268