Activation of crystalline cellulose to cellulose IIII results in efficient hydrolysis by cellobiohydrolase

被引:115
作者
Igarashi, Kiyohiko [1 ]
Wada, Masahisa [1 ]
Samejima, Masahiro [1 ]
机构
[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biomat Sci, Bunkyo Ku, Tokyo 1138657, Japan
关键词
ammonia cellulose; cellobiohydrolase; cellobiose dehydrogenase; crystalline polymorphs; solid-liquid interface;
D O I
10.1111/j.1742-4658.2007.05727.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystalline polymorphic form of cellulose (cellulose I-alpha-rich) of the green alga, Cladophora, was converted into cellulose IIII and I-beta by supercritical ammonium and hydrothermal treatments, respectively, and the hydrolytic rate and the adsorption of Trichoderma viride cellobiohydrolase I (Cel7A) on these products were evaluated by a novel analysis based on the surface density of the enzyme. Cellobiose production from cellulose IIII was more than 5 times higher than that from cellulose I. However, the amount of enzyme adsorbed on cellulose IIII was less than twice that on cellulose I, and the specific activity of the adsorbed enzyme for cellulose IIII was more than 3 times higher than that for cellulose I. When cellulose IIII was converted into cellulose I-beta by hydrothermal treatment, cellobiose production was dramatically decreased, although no significant change was observed in enzyme adsorption. This clearly indicates that the enhanced hydrolysis of cellulose IIII is related to the structure of the crystalline polymorph. Thus, supercritical ammonium treatment activates crystalline cellulose for hydrolysis by cellobiohydrolase.
引用
收藏
页码:1785 / 1792
页数:8
相关论文
共 36 条
[1]  
ABUJA PM, 1988, EUR BIOPHYS J BIOPHY, V15, P339, DOI 10.1007/BF00254721
[2]   Flow properties of microcrystalline cellulose suspension prepared by acid treatment of native cellulose [J].
Araki, J ;
Wada, M ;
Kuga, S ;
Okano, T .
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, 1998, 142 (01) :75-82
[3]  
ATALLA RH, 1984, SCIENCE, V223, P283, DOI 10.1126/science.223.4633.283
[4]   High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei [J].
Divne, C ;
Ståhlberg, J ;
Teeri, TT ;
Jones, TA .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 275 (02) :309-325
[5]   THE 3-DIMENSIONAL CRYSTAL-STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE-I FROM TRICHODERMA-REESEI [J].
DIVNE, C ;
STAHLBERG, J ;
REINIKAINEN, T ;
RUOHONEN, L ;
PETTERSSON, G ;
KNOWLES, JKC ;
TEERI, TT ;
JONES, TA .
SCIENCE, 1994, 265 (5171) :524-528
[6]   Selective degradation of the cellulose Iα component in Cladophora cellulose with Trichoderma viride cellulase [J].
Hayashi, N ;
Sugiyama, J ;
Okano, T ;
Ishihara, M .
CARBOHYDRATE RESEARCH, 1997, 305 (01) :109-116
[7]   The enzymatic susceptibility of cellulose microfibrils of the algal-bacterial type and the cotton-ramie type [J].
Hayashi, N ;
Sugiyama, J ;
Okano, T ;
Ishihara, M .
CARBOHYDRATE RESEARCH, 1997, 305 (02) :261-269
[8]   Surface density of cellobiohydrolase on crystalline celluloses - A critical parameter to evaluate enzymatic kinetics at a solid-liquid interface [J].
Igarashi, Kiyohiko ;
Wada, Masahisa ;
Hori, Ritsuko ;
Samejima, Masahiro .
FEBS JOURNAL, 2006, 273 (13) :2869-2878
[9]   Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose microcrystals [J].
Imai, T ;
Boisset, C ;
Samejima, M ;
Igarashi, K ;
Sugiyama, J .
FEBS LETTERS, 1998, 432 (03) :113-116
[10]   ISOLATED FUNGAL CELLULASE TERMINAL DOMAINS AND A SYNTHETIC MINIMUM ANALOG BIND TO CELLULOSE [J].
JOHANSSON, G ;
STAHLBERG, J ;
LINDEBERG, G ;
ENGSTROM, A ;
PETTERSSON, G .
FEBS LETTERS, 1989, 243 (02) :389-393