Interactive forces between lignin and cellulase as determined by atomic force microscopy

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• 作者：Chengrong Qin (4)
  Kimberley Clarke (5)
  Kecheng Li (5)
  
  4. College of Light Industry and Food Engineering ; Guangxi University ; 100 University Road ; Nanning ; Guangxi Province ; 530004 ; PR China
  5. Department of Chemical Engineering ; University of New Brunswick ; 2 Garland Court ; Incutech Complex ; Fredericton ; NB ; E3B 5A3 ; Canada
  
• 关键词：Non ; productive binding ; Lignin ; Enzymatic hydrolysis ; Atomic force microscopy ; Cellulase
• 刊名：Biotechnology for Biofuels
• 出版年：2014
• 出版时间：December 2014
• 年：2014
• 卷：7
• 期：1
• 全文大小：556 KB
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• 刊物类别：Chemistry and Materials Science
• 刊物主题：Biotechnology
  Plant Breeding/Biotechnology
  Renewable and Green Energy
  Environmental Engineering/Biotechnology
  
• 出版者：BioMed Central
• ISSN：1754-6834

文摘

Background Lignin is a complex polymer which inhibits the enzymatic conversion of cellulose to glucose in lignocellulose biomass for biofuel production. Cellulase enzymes irreversibly bind to lignin, deactivating the enzyme and lowering the overall activity of the hydrolyzing reaction solution. Within this study, atomic force microscopy (AFM) is used to compare the adhesion forces between cellulase and lignin with the forces between cellulase and cellulose, and to study the moiety groups involved in binding of cellulase to lignin. Results Trichoderma reesei, ATCC 26921, a commercial cellulase system, was immobilized onto silicon wafers and used as a substrate to measure forces involved in cellulase non-productive binding to lignin. Attraction forces between cellulase and lignin, and between cellulase and cellulose were compared using kraft lignin- and hydroxypropyl cellulose-coated tips with the immobilized cellulase substrate. The measured adhesion forces between kraft lignin and cellulase were on average 45% higher than forces between hydroxypropyl cellulose and cellulase. Specialized AFM tips with hydrophobic, -OH, and -COOH chemical characteristics were used with immobilized cellulase to represent hydrophobic, H-bonding, and charge-charge interactions, respectively. Forces between hydrophobic tips and cellulase were on average 43% and 13% higher than forces between cellulase with tips exhibiting OH and COOH groups, respectively. A strong attractive force during the AFM tip approach to the immobilized cellulase was observed with the hydrophobic tip. Conclusions This work shows that there is a greater overall attraction between kraft lignin and cellulase than between hydroxypropyl cellulose and cellulase, which may have implications during the enzymatic reaction process. Furthermore, hydrophobic interactions appear to be the dominating attraction force in cellulase binding to lignin, while a number of other interactions may establish the irreversible binding.