[1] Araujo R , Casal M, Cavaco-Paulo A. Application of enzymes for textile fibres processing. Biocatal Biotransfor,2008, 26(5):332-349.
[2] Sae-be P, Sangwatanaroj U, Punnapayak H. Analysis of the products from enzymatic scouring of cotton. Biotechnol J, 2007, 2(3):316-325.
[3] Tomme P, Boraston A, McLean B, et al. Characterization and affinity applications of cellulose-binding domains. J Chromatogr B Biomed Sci Appl, 1998, 715(1):283-296.
[4] Zhang Y, Chen S, Xu M, et al. Characterization of Thermobifida fusca Cutinase Carbohydrate-Binding-Module Fusion Proteins and Their Potential Application in Bioscouring. Appl. Environ. Microbiol, 2010,76(20):6870-6876.
[5] Linder M, Winiecka-Krusnell J, Linder E. Use of recombinant cellulose-binding domains of Trichoderma reesei cellulase as a selective immunocytochemical marker for cellulose in protozoa. Appl. Environ. Microbiol, 2002,68(5):2503-2508.
[6] Sakka K, Takada G, Karita S, et al. Identification and characterization of cellulose-binding domains in xylanase A of Clostridium stercorarium. Ann N Y Acad Sci, 1996, 782:241-251.
[7] Ciolacu D, Kovac J, Kokol V. The effect of the cellulose-binding domain from Clostridium cellulovorans on the supramolecular structure ofcellulose fibers. Carbohydr Res, 2010, 345(5):621-630.
[8] Black G W, Rixon J E, Clarke J H, et al. Cellulose-binding domains and linkersequences potentiate the activity of hemicellulases against complex substrates. J Biotechnol, 1997, 57(1-3):59-69.
[9] Gilkes N R, Henrissat B, Kilburn D G, et al. Domains in microbial β-1,4-glycanases: sequence conservation,function, and enzyme families. Microbiol Rev,1991, 55(2):303-315.
[10] Quentin M, Ebbelaar M, Derksen J, et al. Description of a cellulose-binding domain and a linker sequence from Aspergillus fungi. Appl. Microbiol. Biotechnol,2002, 58(2):658-662.
[11] Egmond M R, De V. Fusarium solani p isi cutinase. Biochimie,2000, 82(11): 1015-1021.
[12] Martinez C, De Geus P,Lauwereys M, et al. Fusarium solani cutinaseis a lipolytic enzyme with a catalytic serine accessible to solvent. Nature, 1992, 356: 615-618.
[13] Li Z F, Li B, Liu Z G, et al. Calcium Leads to Further Increase in Glycine-Enhanced Extracellular Secretion of Recombinant α-Cyclodextrin Glycosyltransferase in Escherichia coli. J Agric Food Chem, 2009, 57(14): 6231-6237.
[14] Thomas J G, Baneyx F. Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins. J Biol Chem, 1996, 271(19):11141-11147.
[15] Kusano K, Waterman M R, Sakaguchi M, et al. Protein synthesis inhibitors and ethanol selectively enhance heterologousexpression of P450s and related proteins in Escherichia coli. Arch Biochem Biophys, 1999, 367(1):129-136.
[16] Oganesyan N, Ankoudinova I, Kim S H , et al. EVect of osmotic stress and heat shock in recombinant protein overexpression and crystallization. Protein Expression and Purification, 2007,52(2):280-285.
[17] Samual D, Kumar T K, Ganesh G, et al. Proline inhibits aggregation during protein refolding. Protein Sci, 2000, 9(2):344-352.
[18] Yang D S, Yip C M, Huang T H J, et al. Manipulating the amyloid-beta aggregation pathway with chemical chaperones. J Biol Chem, 1999, 274:32970-32974.
[19] Voziyan PA, Fisher M T. Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: oV-pathway aggregation propensity does not determine the co-chaperonin requirement, Protein Sci, 2000, 9(12):2405-2412.
[20] Kempf B, Bremer E. Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments, Arch Microbiol, 1998, 170(5):319-330.
[21] Bukau B, Horwich A L. The Hsp70 and Hsp60 chaperone machines. Cell, 1998, 92:351-366.
[22] Blakwell J R, Horgan R. A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS, 1991, 295(1-3): 10-12.
[23] Schlicke M, Brakmann S. Expression and purification of histidinetagged bacteriophage T7 DNA polymerase. Protein Expr Purif, 2005, 39:247-253.
[24] de Marco A, Vigh L, Diamant S, et al. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes,plasmid- or benzyl alcohol-overexpressed molecular chaperones,Cell Stress Chaperones, 2005, 10(4):329-339.
[25] Diamant S, Eliahu N, Rosenthal D, et al. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J Biol Chem, 2001, 276(2001):39586-39591.
|