메뉴 건너뛰기




Volumn 49, Issue 1, 2011, Pages 121-129

Cloning, expression, and characterization of serine protease from thermophilic fungus Thermoascus aurantiacus var. levisporus

Author keywords

cloning; expression; Pichia pastoris; serine protease; Thermoascus aurantiacus var. levisporus

Indexed keywords

BENZYLSULFONYL FLUORIDE; ENZYME INHIBITOR; FUNGAL DNA; RECOMBINANT PROTEIN; SERINE PROTEINASE;

EID: 79952205649     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-011-9355-6     Document Type: Article
Times cited : (18)

References (56)
  • 1
    • 0037631417 scopus 로고    scopus 로고
    • Production of alkaline protease by immobilized cells of alkalophilic Bacillus sp
    • Adinarayana, K. and P. Ellaiah. 2003. Production of alkaline protease by immobilized cells of alkalophilic Bacillus sp. J. Sci. Indust. Res. (India) 62, 589-592.
    • (2003) J. Sci. Indust. Res. (India) , vol.62 , pp. 589-592
    • Adinarayana, K.1    Ellaiah, P.2
  • 2
    • 0034084579 scopus 로고    scopus 로고
    • High-level production of recombinant fungal endo-beta-1, 4-xylanase in the methylotrophic yeast Pichia pastoris
    • Berrin, J. G., G. Williamson, A. Puigserver, J. C. Chaix, W. R. McLauchlan, and N. Juge. 2000. High-level production of recombinant fungal endo-beta-1, 4-xylanase in the methylotrophic yeast Pichia pastoris. Protein Expr. Purif 19, 179-187.
    • (2000) Protein Expr. Purif , vol.19 , pp. 179-187
    • Berrin, J.G.1    Williamson, G.2    Puigserver, A.3    Chaix, J.C.4    McLauchlan, W.R.5    Juge, N.6
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 3042745637 scopus 로고    scopus 로고
    • A novel extracellular subtilisin-like protease from the hyperthermophile Aeropyrum pernix K1: biochemical properties, cloning, and expression
    • Catara, G., G. Ruggiero, F. L. a Cara, F. A. Digilio, A. Capasso, and A. M. Rossi. 2003. A novel extracellular subtilisin-like protease from the hyperthermophile Aeropyrum pernix K1: biochemical properties, cloning, and expression. Extremophiles 7, 391-399.
    • (2003) Extremophiles , vol.7 , pp. 391-399
    • Catara, G.1    Ruggiero, G.2    a Cara, F.L.3    Digilio, F.A.4    Capasso, A.5    Rossi, A.M.6
  • 5
    • 12544253371 scopus 로고    scopus 로고
    • Thermoactive extracellular proteases of Geobacillus caldoproteolyticus, sp. nov., from sewage sludge
    • Chen, X. G., O. Stabnikova, J. H. Tay, J. Y. Wang, and S. T. L. Tay. 2004. Thermoactive extracellular proteases of Geobacillus caldoproteolyticus, sp. nov., from sewage sludge. Extremophiles 8, 489-498.
    • (2004) Extremophiles , vol.8 , pp. 489-498
    • Chen, X.G.1    Stabnikova, O.2    Tay, J.H.3    Wang, J.Y.4    Tay, S.T.L.5
  • 6
    • 36549045126 scopus 로고    scopus 로고
    • Cloning of a gene encoding thermostable glucoamylase from Chaetomium thermophilum and its expression in Pichia pastoris
    • Chen, J., Y. Q. Zhang, C. Q. Zhao, A. N. Li, Q. X. Zhou, and D. C. Li. 2007. Cloning of a gene encoding thermostable glucoamylase from Chaetomium thermophilum and its expression in Pichia pastoris. J. Appl. Microbiol. 103, 2277-2284.
    • (2007) J. Appl. Microbiol. , vol.103 , pp. 2277-2284
    • Chen, J.1    Zhang, Y.Q.2    Zhao, C.Q.3    Li, A.N.4    Zhou, Q.X.5    Li, D.C.6
  • 7
    • 0033534477 scopus 로고    scopus 로고
    • Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization
    • Choi, I. G., W. G. Bang, S. H. Kim, and Y. G. Yu. 1999. Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization. J. Biol. Chem. 274, 881-888.
    • (1999) J. Biol. Chem. , vol.274 , pp. 881-888
    • Choi, I.G.1    Bang, W.G.2    Kim, S.H.3    Yu, Y.G.4
  • 8
    • 4143068641 scopus 로고    scopus 로고
    • The -lytic protease gene of Lysobacter enzyme genes
    • Epstein, D. M. and P. C. Wensink. 1998. The -lytic protease gene of Lysobacter enzyme genes. J. Biol. Chem. 263, 16568-16590.
    • (1998) J. Biol. Chem. , vol.263 , pp. 16568-16590
    • Epstein, D.M.1    Wensink, P.C.2
  • 9
    • 0024790307 scopus 로고
    • Thermostability of extracellular protease enzyme produced by Spicaria fusispora, a thermophilic fungus
    • Gaur, R., J. Yadav, and L. Pandey. 1989. Thermostability of extracellular protease enzyme produced by Spicaria fusispora, a thermophilic fungus. Hindustan Antibiot. Bull. 31, 36-37.
    • (1989) Hindustan Antibiot. Bull. , vol.31 , pp. 36-37
    • Gaur, R.1    Yadav, J.2    Pandey, L.3
  • 10
    • 33745213791 scopus 로고    scopus 로고
    • Alkaline protease production from alkalophilic Bacillus sp. isolated from natural habitats
    • Genckal, H. and C. Tari. 2006. Alkaline protease production from alkalophilic Bacillus sp. isolated from natural habitats. Enzyme Microb. Technol. 39, 703-710.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 703-710
    • Genckal, H.1    Tari, C.2
  • 12
    • 0037213311 scopus 로고    scopus 로고
    • An overview on fermentation, downstream processing and properties of microbial alkaline proteases
    • Gupta, R., Q. K. Beg, S. Khan, and B. Chauhan. 2002. An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl. Microbiol. Biotechnol 60, 381-395.
    • (2002) Appl. Microbiol. Biotechnol , vol.60 , pp. 381-395
    • Gupta, R.1    Beg, Q.K.2    Khan, S.3    Chauhan, B.4
  • 13
    • 0023644876 scopus 로고
    • In vitro processing of pro-subtilisin produced in Escherichia coli CJ7
    • Ikemura, H., H. Takagi, and M. J. Inouye. 1987. In vitro processing of pro-subtilisin produced in Escherichia coli CJ7. J. Biol. Chem. 262, 7859-7864.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inouye, M.J.3
  • 14
    • 23844527873 scopus 로고    scopus 로고
    • Expression and characterization of a thermostable serine protease (TfpA) from Thermomonospora fusca YX in Pichia pastoris
    • Kim, T. and X. G. Lei. 2005. Expression and characterization of a thermostable serine protease (TfpA) from Thermomonospora fusca YX in Pichia pastoris. Appl. Microbiol. Biotechnol. 68, 355-359.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 355-359
    • Kim, T.1    Lei, X.G.2
  • 15
    • 0027211941 scopus 로고
    • Purification, characterization and molecular cloning of an acidic amino acidspecific proteinase from Streptomyces fradiae ATCC 14544
    • Kitadokoro, K., E. Nakamura, M. Tamaki, T. Horii, H. Okamoto, M. Shin, T. Sato, and et al. 1993. Purification, characterization and molecular cloning of an acidic amino acidspecific proteinase from Streptomyces fradiae ATCC 14544. Biochim. Biophys. Acta. 1163, 149-157.
    • (1993) Biochim. Biophys. Acta. , vol.1163 , pp. 149-157
    • Kitadokoro, K.1    Nakamura, E.2    Tamaki, M.3    Horii, T.4    Okamoto, H.5    Shin, M.6    Sato, T.7
  • 17
    • 13844298133 scopus 로고    scopus 로고
    • Extracellular acid protease from Rhizopus oryzae: purification and characterization
    • Kumar, S., N. S. Sharma, M. R. Saharan, and R. Singh. 2005. Extracellular acid protease from Rhizopus oryzae: purification and characterization. Proc. Biochem. 40, 1701-1705.
    • (2005) Proc. Biochem. , vol.40 , pp. 1701-1705
    • Kumar, S.1    Sharma, N.S.2    Saharan, M.R.3    Singh, R.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0026572303 scopus 로고
    • Modified protocol for Yeast DNA mini-preparation
    • Lee, F. S. 1992. Modified protocol for Yeast DNA mini-preparation. Biotechnique 12, 679.
    • (1992) Biotechnique , vol.12 , pp. 679
    • Lee, F.S.1
  • 22
    • 34248372949 scopus 로고    scopus 로고
    • Purification and characterization of two thermostable proteases from the thermophilic fungus Chaetomium thermophilum
    • Li, A. N., A. Y. Ding, J. Chen, S. A. Liu, M. Zhang, and D. C. Li. 2007a. Purification and characterization of two thermostable proteases from the thermophilic fungus Chaetomium thermophilum. J. Microbiol. Biotechnol. 17, 624-631.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 624-631
    • Li, A.N.1    Ding, A.Y.2    Chen, J.3    Liu, S.A.4    Zhang, M.5    Li, D.C.6
  • 23
    • 58549119191 scopus 로고    scopus 로고
    • Cloning, expression and characterization of the serine protease gene from Chaetomium thermophilum
    • Li, A. N. and D. C. Li. 2009. Cloning, expression and characterization of the serine protease gene from Chaetomium thermophilum. J. Appl. Microbiol. 106, 369-380.
    • (2009) J. Appl. Microbiol. , vol.106 , pp. 369-380
    • Li, A.N.1    Li, D.C.2
  • 24
    • 34247383576 scopus 로고    scopus 로고
    • Functional expression of the keratinolytic serine protease gene sfp2 from Streptomyces fradiae var. k11 in Pichia pastoris
    • Li, J., P. J. Shi, X. Y. Han, K. Meng, P. L. Yang, Y. R. Wang, H. Y. Luo, N. F. Wu, B. Yao, and Y. L. Fan. 2007b. Functional expression of the keratinolytic serine protease gene sfp2 from Streptomyces fradiae var. k11 in Pichia pastoris. Protein Expr. Purif. 54, 79-86.
    • (2007) Protein Expr. Purif. , vol.54 , pp. 79-86
    • Li, J.1    Shi, P.J.2    Han, X.Y.3    Meng, K.4    Yang, P.L.5    Wang, Y.R.6    Luo, H.Y.7    Wu, N.F.8    Yao, B.9    Fan, Y.L.10
  • 25
    • 0032237875 scopus 로고    scopus 로고
    • Efficient amplification of inserted sequences from bacterial artificial chromo some clones thermal asymmetric interlaced PCR
    • Liu, Y. G. and N. Huang. 1998. Efficient amplification of inserted sequences from bacterial artificial chromo some clones thermal asymmetric interlaced PCR. Plant Mol. Biol. Reporter 16, 175-181.
    • (1998) Plant Mol. Biol. Reporter , vol.16 , pp. 175-181
    • Liu, Y.G.1    Huang, N.2
  • 26
    • 36348960082 scopus 로고    scopus 로고
    • Cloning and heterologous expression of aspartic protease SA76 related to biocontrol in Trichoderma harzianum
    • Liu, Y. and Q. Yang. 2007. Cloning and heterologous expression of aspartic protease SA76 related to biocontrol in Trichoderma harzianum. FEMS Microbiol. Lett. 277, 173-181.
    • (2007) FEMS Microbiol. Lett. , vol.277 , pp. 173-181
    • Liu, Y.1    Yang, Q.2
  • 28
    • 33947510415 scopus 로고    scopus 로고
    • Purification and partial characterization of serine protease from thermostable alkalophilic Bacillus laterosporus-AK1
    • Manavalan, A., A. Kalaichelvan, V. Kalyanasundaram, A. Perumal, and A. Manavalan. 2007. Purification and partial characterization of serine protease from thermostable alkalophilic Bacillus laterosporus-AK1. World J. Microbiol. Biotechnol. 23, 475-481.
    • (2007) World J. Microbiol. Biotechnol. , vol.23 , pp. 475-481
    • Manavalan, A.1    Kalaichelvan, A.2    Kalyanasundaram, V.3    Perumal, A.4    Manavalan, A.5
  • 29
    • 29344442436 scopus 로고
    • Isolation, partial purification, and some properties of protease I from a thermophilic mold Thermoascus aurantiacus var levisporus
    • Marcy, R. M., T. C. Engelhardt, and J. M. Upadhyay. 1984. Isolation, partial purification, and some properties of protease I from a thermophilic mold Thermoascus aurantiacus var levisporus. Mycopathologia 87, 57-65.
    • (1984) Mycopathologia , vol.87 , pp. 57-65
    • Marcy, R.M.1    Engelhardt, T.C.2    Upadhyay, J.M.3
  • 30
    • 0024117004 scopus 로고
    • Intracellular precursors and secretion of alkaline extracellular protease of Yarrowia lipolytica
    • Matoba, S., J. Fukuyama, R. A. Wing, and D. M. Ogrydziak. 1988. Intracellular precursors and secretion of alkaline extracellular protease of Yarrowia lipolytica. Mol. Cell. Biol. 8, 4904-4916.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4904-4916
    • Matoba, S.1    Fukuyama, J.2    Wing, R.A.3    Ogrydziak, D.M.4
  • 31
    • 34147107575 scopus 로고    scopus 로고
    • Partial characterization of protease from a thermophilic fungus, Thermoascus aurantiacus, and its hydrolytic activity on bovine casein
    • Merheb, C. W., H. Cabrala, E. Gomesa, and R. Da-Silva. 2007. Partial characterization of protease from a thermophilic fungus, Thermoascus aurantiacus, and its hydrolytic activity on bovine casein. Food Chemistry 104, 127-131.
    • (2007) Food Chemistry , vol.104 , pp. 127-131
    • Merheb, C.W.1    Cabrala, H.2    Gomesa, E.3    Da-Silva, R.4
  • 32
    • 24144445153 scopus 로고    scopus 로고
    • Purification and characterization of extracellular alkaline serine protease from Stenotrophomonas maltophilia strain S-1
    • Miyaji, T., Y. Otta, T. Shibata, K. Mitsui, T. Nakagawa, T. Watanabe, Y. Niimura, and N. Tomizuka. 2005. Purification and characterization of extracellular alkaline serine protease from Stenotrophomonas maltophilia strain S-1. Lett. Appl. Microbiol. 41, 253-257.
    • (2005) Lett. Appl. Microbiol. , vol.41 , pp. 253-257
    • Miyaji, T.1    Otta, Y.2    Shibata, T.3    Mitsui, K.4    Nakagawa, T.5    Watanabe, T.6    Niimura, Y.7    Tomizuka, N.8
  • 33
    • 0037269814 scopus 로고    scopus 로고
    • Cloning of and genetic variation in protease VCP1 from the nematophagous fungus Pochonia chlamydosporia
    • Morton, C. O., P. R. Hirsch, J. P. Peberdy, and B. R. Kerry. 2003. Cloning of and genetic variation in protease VCP1 from the nematophagous fungus Pochonia chlamydosporia. Mycol. Res. 107, 38-46.
    • (2003) Mycol. Res. , vol.107 , pp. 38-46
    • Morton, C.O.1    Hirsch, P.R.2    Peberdy, J.P.3    Kerry, B.R.4
  • 34
    • 42149194232 scopus 로고    scopus 로고
    • Cloning, characterization, and expression of the gene encoding alkaline protease in the marine yeast Aureobasidium pullulans 10
    • Ni, X., Z. Chi, C. Ma, and C. Madzak. 2008. Cloning, characterization, and expression of the gene encoding alkaline protease in the marine yeast Aureobasidium pullulans 10. Mar. Biotechnol. 10, 319-327.
    • (2008) Mar. Biotechnol. , vol.10 , pp. 319-327
    • Ni, X.1    Chi, Z.2    Ma, C.3    Madzak, C.4
  • 36
    • 0015541861 scopus 로고
    • Protease production by thermophilic fungi
    • Ong, P. S. and G. M. Gaucher. 1973. Protease production by thermophilic fungi. Can. J. Microbiol. 19, 129-133.
    • (1973) Can. J. Microbiol. , vol.19 , pp. 129-133
    • Ong, P.S.1    Gaucher, G.M.2
  • 37
    • 4344635429 scopus 로고    scopus 로고
    • Gene cloning and expression of an alkaline serine protease with dehairing function from Bacillus pumilus
    • Pan, J., Q. Huang, and Y. Z. Zhang. 2004. Gene cloning and expression of an alkaline serine protease with dehairing function from Bacillus pumilus. Curr. Microbiol. 49, 165-169.
    • (2004) Curr. Microbiol. , vol.49 , pp. 165-169
    • Pan, J.1    Huang, Q.2    Zhang, Y.Z.3
  • 38
  • 39
    • 40549101853 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans
    • Peña-Montes, C., A. González, D. Castro-Ochoa, and A. Farrés. 2008. Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans. Appl. Microbiol. Biotechnol. 78, 603-612.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 603-612
    • Peña-Montes, C.1    González, A.2    Castro-Ochoa, D.3    Farrés, A.4
  • 41
    • 0000186374 scopus 로고
    • Chymotrypsin
    • H. U. Bergmeyer (Ed.), Berlin, New York, and London: Academic Press
    • Rick, W. 1974. Chymotrypsin. In H. U. Bergmeyer (ed.) Methods of Enzymatic Analysis. Academic Press, Berlin, New York, and London.
    • (1974) Methods of Enzymatic Analysis
    • Rick, W.1
  • 44
    • 0030608049 scopus 로고    scopus 로고
    • Sequence of the gene encoding a highly thermostable neutral proteinase from Bacillus sp. Strain EA1: expression in Escherichia coli and characterization
    • Saul, D. J., L. C. Williams, J. S. David, H. S. Toogood, R. M. Daniel, and P. L. Bergquist. 1996. Sequence of the gene encoding a highly thermostable neutral proteinase from Bacillus sp. Strain EA1: expression in Escherichia coli and characterization. Biochimica et Biophysica Acta 1308, 74-80.
    • (1996) Biochimica Et Biophysica Acta , vol.1308 , pp. 74-80
    • Saul, D.J.1    Williams, L.C.2    David, J.S.3    Toogood, H.S.4    Daniel, R.M.5    Bergquist, P.L.6
  • 45
    • 0035146624 scopus 로고    scopus 로고
    • cDNA cloning and immunologic characterization of Peno18, the vacuolar serine protease major allergen of Penicillium oxalicum
    • Shen, H. D., C. W. Wang, W. L. Lin, H. Y. Lai, M. F. Tam, H. Chou, S. R. Wang, and S. H. Han. 2001. cDNA cloning and immunologic characterization of Peno18, the vacuolar serine protease major allergen of Penicillium oxalicum. J. Lab. Clin. Med. 137, 115-124.
    • (2001) J. Lab. Clin. Med. , vol.137 , pp. 115-124
    • Shen, H.D.1    Wang, C.W.2    Lin, W.L.3    Lai, H.Y.4    Tam, M.F.5    Chou, H.6    Wang, S.R.7    Han, S.H.8
  • 46
    • 0019953786 scopus 로고
    • Purification and partial characterization of a thiol proteinase from the thermophilic fungus Humicola lanuginosa
    • Shenolikar, S. and K. J. Stevenson. 1982. Purification and partial characterization of a thiol proteinase from the thermophilic fungus Humicola lanuginosa. Biochem. J. 205, 147-152.
    • (1982) Biochem. J. , vol.205 , pp. 147-152
    • Shenolikar, S.1    Stevenson, K.J.2
  • 47
    • 54849440103 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis
    • Shi, X. Z., X. F. Zhao, and J. X. Wang. 2008. Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol. 25, 589-597.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 589-597
    • Shi, X.Z.1    Zhao, X.F.2    Wang, J.X.3
  • 48
    • 33748560143 scopus 로고    scopus 로고
    • Improved production of alkaline protease from a mutant of alkalophilic Bacillus pantotheneticus using molasses as a substrate
    • Shikha, A. Sharan, and N. S. Darmwal. 2007. Improved production of alkaline protease from a mutant of alkalophilic Bacillus pantotheneticus using molasses as a substrate. Bioresour. Technol. 98, 881-885.
    • (2007) Bioresour. Technol. , vol.98 , pp. 881-885
    • Shikha, A.S.1    Darmwal, N.S.2
  • 49
    • 0024425004 scopus 로고
    • The a-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
    • Silen, J. L. and D. A. Agard. 1989. The a-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature 341, 462-464.
    • (1989) Nature , vol.341 , pp. 462-464
    • Silen, J.L.1    Agard, D.A.2
  • 50
    • 1542653185 scopus 로고    scopus 로고
    • High-throughput TAIL PCR as a tool to identify DNA flanking insertions
    • Singer, T. and E. Burke. 2003. High-throughput TAIL PCR as a tool to identify DNA flanking insertions. Methods Mol. Biol. 8, 241-272.
    • (2003) Methods Mol. Biol. , vol.8 , pp. 241-272
    • Singer, T.1    Burke, E.2
  • 51
    • 0033804304 scopus 로고    scopus 로고
    • Rapid isolation of promoter sequences by TAIL PCR: the 5′ flanking regions of Pal and Pgigenes from yams (Dioscorea)
    • Terauchi, R. and G. Kahl. 2000. Rapid isolation of promoter sequences by TAIL PCR: the 5′ flanking regions of Pal and Pgigenes from yams (Dioscorea). Mol. Gen. Genet. 4, 554-560.
    • (2000) Mol. Gen. Genet. , vol.4 , pp. 554-560
    • Terauchi, R.1    Kahl, G.2
  • 52
    • 33847112385 scopus 로고    scopus 로고
    • Isolation, activity and immunological characterisation of a secreted aspartic protease, CtsD, from Aspergillus fumigatus
    • Vickers, I., E. P. Reeves, K. A. Kavanagh, and S. Doyle. 2007. Isolation, activity and immunological characterisation of a secreted aspartic protease, CtsD, from Aspergillus fumigatus. Protein Expr. Purif. 53, 216-224.
    • (2007) Protein Expr. Purif. , vol.53 , pp. 216-224
    • Vickers, I.1    Reeves, E.P.2    Kavanagh, K.A.3    Doyle, S.4
  • 53
    • 33744493948 scopus 로고    scopus 로고
    • Characterization of an extracellular protease and its cDNA from the nematode-trapping fungus Monacrosporium microscaphoides
    • Wang, M., J. Yang, and K. Q. Zhang. 2006. Characterization of an extracellular protease and its cDNA from the nematode-trapping fungus Monacrosporium microscaphoides. Can. J. Microbiol. 52, 130-139.
    • (2006) Can. J. Microbiol. , vol.52 , pp. 130-139
    • Wang, M.1    Yang, J.2    Zhang, K.Q.3
  • 54
    • 0021760521 scopus 로고
    • Compilation of published signal sequences
    • Watson, M. E. 1984. Compilation of published signal sequences. Nucleic Acids Res. 12, 5145-5164.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5145-5164
    • Watson, M.E.1
  • 55
    • 52449110181 scopus 로고    scopus 로고
    • Cloning of the subtilisin Pr1A gene from a strain of locust specific fungus, Metarhizium anisopliae, and functional expression of the protein in Pichia pastoris
    • Wei, Z., Y. Cao, and Y. X. Xia. 2008. Cloning of the subtilisin Pr1A gene from a strain of locust specific fungus, Metarhizium anisopliae, and functional expression of the protein in Pichia pastoris. World J. Microbiol. Biotechnol. 24, 2481-2488.
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , pp. 2481-2488
    • Wei, Z.1    Cao, Y.2    Xia, Y.X.3
  • 56
    • 34248671964 scopus 로고    scopus 로고
    • Purification and cloning of a novel serine protease from the nematode-trapping fungus Dactylellina varietas and its potential roles in infection against nematodes
    • Yang, J., L. Liang, Y. Zhang, J. Li, L. Zhang, F. Ye, Z. Gan, and K. Q. Zhang. 2007. Purification and cloning of a novel serine protease from the nematode-trapping fungus Dactylellina varietas and its potential roles in infection against nematodes. Appl. Microbiol. Biotechnol. 75, 557-565.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 557-565
    • Yang, J.1    Liang, L.2    Zhang, Y.3    Li, J.4    Zhang, L.5    Ye, F.6    Gan, Z.7    Zhang, K.Q.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.