Activity enhancement of Fe3O4/SiO2 nanoparticle immobilized cellulase with glutaraldehyde and co-culture with Clostridium sp. TCW1 for biohydrogen production from cellulase

• Main Authors: CHANG, HAO-MING, 張浩銘
• Other Authors: HUANG, CHI-YU
• Format: Others
• Language: zh-TW
• Published: 2016
• Online Access: http://ndltd.ncl.edu.tw/handle/33444401285538058847

碩士 === 東海大學 === 環境科學與工程學系 === 104 === Cellulose is the most abundant organic material in the world. Many municipal solid wastes or agricultural wastes contain a great amount of cellulose. Use of these cellulosic wastes to produce bio-hydrogen not only remove these wastes but also reduce the cost of raw materials from bio-hydrogen production. Cellulases catalyse the hydrolysis of cellulose and convert cellulose into cellobiose, glucose or other sugar. Due to the high price and solubility, cellulase is hard to recover from the substrate mixture after reaction for reuse. Therefore it is critical to find more techno-economic methods to improve the economics of cellulase utilization. Magnetic nanoparticles provide advantages as the supporting material for enzyme immobilization over traditional materials such as low cytotoxicity, large specific surface area and easy separation from reaction mixture by magnetic field. This study immobilized commercial cellulase from Trichoderma reesi on the Fe3O4/SiO2 magnetic nanoparticles by covalent binding via glutaraldehyde. The optimal cellulase immobilization condition and reaction activity of immobilized enzyme have been investigated. Finally immobilized cellulase was co-cultured with a hydrogen-producing pure culture Clostridium sp. TCW1 to investigate hydrogen production yield. From these results, it can be concluded that the immobilization of cellulase on magnetic Fe3O4/SiO2 nanoparticle with covalent binding via glutaraldehyde is a suitable method to significantly improve stability and reusability of cellulase. When co-cultured with Clostridium sp. TCW1, immobilized cellulase can improve hydrogen production yield from cellulase.