ARNOLD F H. Directed evolution:Creating biocatalysts for the future [J]. Chemical engineering science, 1996, (23):5091-5102.doi:10.1016/S0009-2509(96)00288-6.
LEUNG D W, CHEN E, GOEDDEL D V. A Method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction [J]. Technique, 1989.11-15.
[4]
SAMBROOK J, FRITSCH E F, MANIANTS T. Molecular cloning:A laboratory manual [M]. New York:Cold Spring Harbor Laboratory Press, 2001.
MONEAL J, REESE E T. The chiticase of Serratia marcescens [J]. Microbiology, 1969(7):689-696.
[7]
ZHAO H, MOORE J C, VOLKOV A A. Methods for optimizing industrial enzymes by directed evolution [M]. Washington D C:ASM Press, 1998.597-604.
[8]
FISCHER B, SUMNER I, GOODENOUGH P. Isolation and renaturetion of bioactive proteins expressed in Escherichia coli as inclusion bodies [J]. Arheimittelforschung, 1992.1512-1515.
[9]
ZHU Guo-ping, TENG Mai-kun, WU Chuan-jin. Mutation of G138P enhanced the thermostability of D glucose isomerase [J]. Acta Biochimica et Biophysica Sinica, 1998(6):77-80.
STEMMER W P C. Rapid evolution of a protein in vitro by DNA shuffling [J]. NATURE, 1994(4):389-391.
[13]
OUE S, OKAMOTO A, YANO T. Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues [J]. Journal of Biological Chemistry, 1999(4):2344-2349.
[14]
MIYAZAKI K, WINTRODE P L, GRAYLING R A. Directed evolution study of temperature adaption in a psychrophilic enzyme [J]. Molecular Biology, 2000(4):1015-1026.
[15]
BANEYX F. Recombinant protein expression in Escherichia coli [J]. Current Opinion in Biotechnology, 1999(5):441-421.doi:10.1016/S0958-1669(99)00003-8.
[16]
MISAWA S, KUMAGAI I. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies [J]. Biopolymers(Peptide Science), 1999(4):297-307.doi:10.1002/(SICI)1097-0282(1999)51:4< 297::AID-BIP5> 3.0.CO; 2-I.
