Controlled adsorption of cellulase onto pretreated corncob by pH adjustment

被引:47
作者
Du, Ruoyu [1 ]
Su, Rongxin [1 ,2 ]
Li, Xuan [1 ]
Tantai, Xiaowei [1 ]
Liu, Zhaohui
Yang, Jifeng [1 ]
Qi, Wei [1 ]
He, Zhimin [1 ]
机构
[1] Tianjin Univ, State Key Lab Chem Engn, Tianjin Key Lab Membrane Sci & Desalinat Technol, Sch Chem Engn & Technol, Tianjin 300072, Peoples R China
[2] E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
关键词
Cellulase adsorption; Cellulase desorption; Enzyme recycling; pH adjustment; Langmuir adsorption isotherm; TRICHODERMA-REESEI CELLULASE; SODIUM-HYDROXIDE; ENZYME RECYCLE; LODGEPOLE PINE; HYDROLYSIS; DESORPTION; ACCESSIBILITY; RECOVERY; SOFTWOOD; BIOMASS;
D O I
10.1007/s10570-012-9653-0
中图分类号
TB3 [工程材料学]; TS [轻工业、手工业、生活服务业];
学科分类号
0805 ; 080502 ; 0822 ;
摘要
The effective recycling of cellulase requires an in-depth understanding of cellulase adsorption and desorption. In the present study, we examined the adsorption behaviors and stabilities of cellulase at different pH values. Acidic pH (< 4.8) was found to favor adsorption, whereas neutral and alkaline pH (especially pH 7 and 10) favored desorption. The influence of pH on cellulase activity was temperature dependent. Under mild conditions (e.g., pH 7 and 25 A degrees C), the effect of pH on cellulase activity was reversible, and the cellulase activity can return to almost 100% by adjusting the pH value to 4.8. However, under severe conditions (e.g. pH 10 and 50 A degrees C), irreversible inactivation may take place. We also explored the roles of pH and temperature in cellulase adsorption kinetics and isotherms. At pH 4.8, temperature had no remarkable effect on the adsorption capacity of the cellulases onto substrate. However, at pH 7 and 10, high temperatures lead to more cellulase desorption. Only at pH 4.8 does cellulase adsorption well fit (R (2) > 0.96) the pseudo-first-order kinetic and Langmuir adsorption isotherm (R (2) > 0.99) models.
引用
收藏
页码:371 / 380
页数:10
相关论文
共 47 条
[1]   Desorption of cellulases from cotton powder [J].
Azevedo, H ;
Ramos, LP ;
Cavaco-Paulo, A .
BIOTECHNOLOGY LETTERS, 2001, 23 (17) :1445-1448
[2]   Improving Enzymes for Biomass Conversion: A Basic Research Perspective [J].
Banerjee, Goutami ;
Scott-Craig, John S. ;
Walton, Jonathan D. .
BIOENERGY RESEARCH, 2010, 3 (01) :82-92
[3]   Modeling cellulase kinetics on lignocellulosic substrates [J].
Bansal, Prabuddha ;
Hall, Melanie ;
Realff, Matthew J. ;
Lee, Jay H. ;
Bommarius, Andreas S. .
BIOTECHNOLOGY ADVANCES, 2009, 27 (06) :833-848
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]  
Copeland RA, 2000, ENZYMES PRACTICAL IN
[6]  
Ding H, 2000, THESIS U CALIFORNIA
[7]   Effect of cellulase adsorption on the surface and interfacial properties of cellulose [J].
Dourado, F ;
Mota, M ;
Pala, H ;
Gama, FM .
CELLULOSE, 1999, 6 (04) :265-282
[8]   Do enzymatic hydrolyzability and Simons' stain reflect the changes in the accessibility of lignocellulosic substrates to cellulase enzymes? [J].
Esteghlalian, AR ;
Bilodeau, M ;
Mansfield, SD ;
Saddler, JN .
BIOTECHNOLOGY PROGRESS, 2001, 17 (06) :1049-1054
[9]   Adsorption of a Trichoderma reesei endoglucanase and cellobiohydrolase onto bleached Kraft fibres [J].
Gerber, PJ ;
Joyce, TW ;
Heitmann, JA ;
Siika-Aho, M ;
Buchert, J .
CELLULOSE, 1997, 4 (04) :255-268
[10]   MEASUREMENT OF CELLULASE ACTIVITIES [J].
GHOSE, TK .
PURE AND APPLIED CHEMISTRY, 1987, 59 (02) :257-268