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Volumn 112, Issue 5, 2011, Pages 441-446

Purification and characterization of a novel aspartic protease from basidiomycetous yeast Cryptococcus sp. S-2

Author keywords

Basidiomycetous; Cloning; Cryptococcus; Extracellular; Protease; Purification

Indexed keywords

AMINO ACID RESIDUES; AMINO ACID SEQUENCE; ASPARTIC PROTEASE; AZOCASEIN; BASIDIOMYCETOUS; CLEAVAGE PRODUCTS; CRYPTOCOCCUS; CRYPTOCOCCUS SP; EXTRACELLULAR; HOMOLOGY SEARCH; HUMAN PEPSIN; MILK-CLOTTING ACTIVITY; OPEN READING FRAME; PEPSIN A; PEPTIDE BONDS; PH RANGE; PROTEASE; PROTEIN SUBSTRATE; PROTEOLYTIC ACTIVITIES; SDS-PAGE; SEQUENCING ANALYSIS; SYNTHETIC SUBSTRATES;

EID: 81255160845     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2011.07.013     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 85010237426 scopus 로고
    • Isolation and characterization of a yeast Cryptococcus sp. S-2 that produces raw starch-digesting alpha-amylase, xylanase and polygalacturonase
    • Iefuji H., Limura Y., Obata T. Isolation and characterization of a yeast Cryptococcus sp. S-2 that produces raw starch-digesting alpha-amylase, xylanase and polygalacturonase. Biosci. Biotechnol. Biochem. 1994, 58:2261-2262.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 2261-2262
    • Iefuji, H.1    Limura, Y.2    Obata, T.3
  • 2
    • 45449118076 scopus 로고    scopus 로고
    • An acidic and thermostable carboxymethyl cellulase from the yeast Cryptococcus sp. S-2: purification, characterization and improvement of its recombinant enzyme production by high cell-density fermentation of Pichia pastoris
    • Thongekkaew J., Ikeda H., Masaki K., Iefuji H. An acidic and thermostable carboxymethyl cellulase from the yeast Cryptococcus sp. S-2: purification, characterization and improvement of its recombinant enzyme production by high cell-density fermentation of Pichia pastoris. Protein Expr. Purif. 2008, 60:140-146.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 140-146
    • Thongekkaew, J.1    Ikeda, H.2    Masaki, K.3    Iefuji, H.4
  • 3
    • 0033752932 scopus 로고    scopus 로고
    • Production, purification and characterization of an extracellular lipase from the yeast, Cryptococcus sp. S-2
    • Kamini N.R., Fuji T., Kurosu T., Iefuji H. Production, purification and characterization of an extracellular lipase from the yeast, Cryptococcus sp. S-2. Process Biochem. 2000, 36:317-324.
    • (2000) Process Biochem. , vol.36 , pp. 317-324
    • Kamini, N.R.1    Fuji, T.2    Kurosu, T.3    Iefuji, H.4
  • 4
    • 32044458811 scopus 로고    scopus 로고
    • Cutinase-like enzyme from the yeast Cryptococcus sp. strain S-2 hydrolyzes polylactic acid and other biodegradable plastics
    • Masaki K., Kamini N.R., Ikeda H., Iefuji H. Cutinase-like enzyme from the yeast Cryptococcus sp. strain S-2 hydrolyzes polylactic acid and other biodegradable plastics. Appl. Environ. Microbiol. 2005, 71:7548-7550.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7548-7550
    • Masaki, K.1    Kamini, N.R.2    Ikeda, H.3    Iefuji, H.4
  • 6
    • 0027431031 scopus 로고
    • Characterization of a chelator-resistant proteinase from Thermus strain Rt4A2
    • Freeman S.A., Peek K., Prescott M., Daniel R. Characterization of a chelator-resistant proteinase from Thermus strain Rt4A2. Biochem. J. 1993, 295:463-469.
    • (1993) Biochem. J. , vol.295 , pp. 463-469
    • Freeman, S.A.1    Peek, K.2    Prescott, M.3    Daniel, R.4
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 0029002927 scopus 로고
    • A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp.
    • Toogood H.S., Prescott M., Daniel R.M. A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp. Biochem. J. 1995, 307:783-789.
    • (1995) Biochem. J. , vol.307 , pp. 783-789
    • Toogood, H.S.1    Prescott, M.2    Daniel, R.M.3
  • 9
    • 0001442231 scopus 로고
    • Milk-clotting enzyme from Mucor pusillus var. Lindt
    • Arima K., Yu J., Iwasaki S. Milk-clotting enzyme from Mucor pusillus var. Lindt. Methods Enzymol. 1970, 19:446-460.
    • (1970) Methods Enzymol. , vol.19 , pp. 446-460
    • Arima, K.1    Yu, J.2    Iwasaki, S.3
  • 10
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin
    • Anson M.L. The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin. J. Gen. Physiol. 1938, 22:79-89.
    • (1938) J. Gen. Physiol. , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 11
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases
    • Knight C.G., Willenbrock F., Murphy G. A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett. 1992, 296:263-266.
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 12
    • 0031818725 scopus 로고    scopus 로고
    • Substrate specificities and kinetic properties of proteinase A from the yeast Saccharomyces cerevisiae and the development of a novel substrate
    • Kondo H., Shibano Y., Amachi T., Cronin N., Oda K., Dunn B.M. Substrate specificities and kinetic properties of proteinase A from the yeast Saccharomyces cerevisiae and the development of a novel substrate. J. Biochem. 1998, 124:141-147.
    • (1998) J. Biochem. , vol.124 , pp. 141-147
    • Kondo, H.1    Shibano, Y.2    Amachi, T.3    Cronin, N.4    Oda, K.5    Dunn, B.M.6
  • 13
    • 0026087180 scopus 로고
    • Preparation of high molecular weight RNA
    • Kohrer K., Domdey H. Preparation of high molecular weight RNA. Methods Enzymol. 1991, 194:398-405.
    • (1991) Methods Enzymol. , vol.194 , pp. 398-405
    • Kohrer, K.1    Domdey, H.2
  • 14
    • 84959581195 scopus 로고
    • Milk-clotting and proteolytic activities of rennet and of bovine pepsin and porcine pepsin
    • Fox P.F. Milk-clotting and proteolytic activities of rennet and of bovine pepsin and porcine pepsin. J. Dairy Res. 1969, 36:427-433.
    • (1969) J. Dairy Res. , vol.36 , pp. 427-433
    • Fox, P.F.1
  • 15
    • 0032790483 scopus 로고    scopus 로고
    • Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D
    • Yasuda Y., Kageyama T., Akamine A., Shibata M., Kominami E., Uchiyama Y., Yamamoto K. Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D. J. Biochem. 1999, 125:1137-1143.
    • (1999) J. Biochem. , vol.125 , pp. 1137-1143
    • Yasuda, Y.1    Kageyama, T.2    Akamine, A.3    Shibata, M.4    Kominami, E.5    Uchiyama, Y.6    Yamamoto, K.7
  • 16
    • 16844381919 scopus 로고    scopus 로고
    • A new selective substrate for cathepsin E based on the cleavage site sequence of α2-macroglobulin
    • Yasuda Y., Kohmura K., Kadowaki T., Tsukuba T., Yamamoto K. A new selective substrate for cathepsin E based on the cleavage site sequence of α2-macroglobulin. Biol. Chem. 2005, 386:299-305.
    • (2005) Biol. Chem. , vol.386 , pp. 299-305
    • Yasuda, Y.1    Kohmura, K.2    Kadowaki, T.3    Tsukuba, T.4    Yamamoto, K.5
  • 17
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apopotosis
    • Enari M., Talanian R.V., Wong W.W., Nagata S. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apopotosis. Nature 1996, 380:723-726.
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 18
    • 0025832503 scopus 로고
    • Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites
    • Nakayama K., Hosaka M., Hatsuzawa K., Murakami K. Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites. J. Biochem. 1991, 109:803-806.
    • (1991) J. Biochem. , vol.109 , pp. 803-806
    • Nakayama, K.1    Hosaka, M.2    Hatsuzawa, K.3    Murakami, K.4
  • 19
    • 0036181085 scopus 로고    scopus 로고
    • Pepsinogens, progastricsins and prochymosins: structure, function, evolution and development
    • Kageyama T. Pepsinogens, progastricsins and prochymosins: structure, function, evolution and development. Cell. Mol. Life Sci. 2002, 59:288-306.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 288-306
    • Kageyama, T.1
  • 20
    • 0026742960 scopus 로고
    • Purification and characterization of furin, a kex2-like processing endoprotease, produced in Chinese hamster ovary cells
    • Hatsuzawa K., Nagahama M., Takahashi S., Takada K., Murakami K., Nakayama K. Purification and characterization of furin, a kex2-like processing endoprotease, produced in Chinese hamster ovary cells. J. Biol. Chem. 1992, 267:16094-16099.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16094-16099
    • Hatsuzawa, K.1    Nagahama, M.2    Takahashi, S.3    Takada, K.4    Murakami, K.5    Nakayama, K.6
  • 21
    • 0014544546 scopus 로고
    • The sites of action of human and swine pepsins on the B chain of oxidized insulin
    • Etherington D.J., Taylor W.H. The sites of action of human and swine pepsins on the B chain of oxidized insulin. Biochem. J. 1969, 113:29-30.
    • (1969) Biochem. J. , vol.113 , pp. 29-30
    • Etherington, D.J.1    Taylor, W.H.2
  • 22
    • 0018418281 scopus 로고
    • Action of human pepsins 1, 2, 3 and 5 on the oxidized B-chain of insulin
    • Roberts N.B., Taylor W.H. Action of human pepsins 1, 2, 3 and 5 on the oxidized B-chain of insulin. Biochem. J. 1979, 179:183-189.
    • (1979) Biochem. J. , vol.179 , pp. 183-189
    • Roberts, N.B.1    Taylor, W.H.2
  • 23
    • 21744456591 scopus 로고
    • Studies on rennin. IX. On the limited proteolysis of a-rennin and the proteolytic activity of chromatographically purified fractions of rennin
    • Foltmann B. Studies on rennin. IX. On the limited proteolysis of a-rennin and the proteolytic activity of chromatographically purified fractions of rennin. C. R. Trav. Lab. Carlsberg 1964, 34:319-325.
    • (1964) C. R. Trav. Lab. Carlsberg , vol.34 , pp. 319-325
    • Foltmann, B.1
  • 25
    • 9844253714 scopus 로고
    • Studies on mold proteases part II substrate specificity of acid protease of Rhizopus chinensis
    • Tsuru D., Hattori A., Tsuji H., Yamamoto T., Fukumoto J. Studies on mold proteases part II substrate specificity of acid protease of Rhizopus chinensis. Agric. Biol. Chem. 1969, 33:1419-1426.
    • (1969) Agric. Biol. Chem. , vol.33 , pp. 1419-1426
    • Tsuru, D.1    Hattori, A.2    Tsuji, H.3    Yamamoto, T.4    Fukumoto, J.5
  • 27
    • 0015307419 scopus 로고
    • Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease
    • Williams D.C., Witaker J.R., Caldwell P.V. Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease. Arch. Biochem. Biophys. 1972, 149:52-61.
    • (1972) Arch. Biochem. Biophys. , vol.149 , pp. 52-61
    • Williams, D.C.1    Witaker, J.R.2    Caldwell, P.V.3
  • 28
    • 0040507540 scopus 로고
    • Substrate specificity of a carboxyl proteinase from Irpex lacteus
    • Kobayashi H., Kusakabe I., Murakami K. Substrate specificity of a carboxyl proteinase from Irpex lacteus. Agric. Biol. Chem. 1983, 47:1921-1923.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 1921-1923
    • Kobayashi, H.1    Kusakabe, I.2    Murakami, K.3
  • 30
    • 0017715612 scopus 로고
    • Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity
    • Tanaka N., Takeuchi M., Ichishima E. Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity. Biochim. Biophys. Acta 1977, 485:406-416.
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 406-416
    • Tanaka, N.1    Takeuchi, M.2    Ichishima, E.3
  • 33
    • 0028158795 scopus 로고
    • Mutation of a fungal aspartic proteinase, Mucor pusillus rennin, to decrease thermostability for use as a milk coagulant
    • Yamashita T., Higashi S., Higashi T., Machida H., Iwasaki S., Nishiyama M., Beppu T. Mutation of a fungal aspartic proteinase, Mucor pusillus rennin, to decrease thermostability for use as a milk coagulant. J. Biotechnol. 1994, 32:17-28.
    • (1994) J. Biotechnol. , vol.32 , pp. 17-28
    • Yamashita, T.1    Higashi, S.2    Higashi, T.3    Machida, H.4    Iwasaki, S.5    Nishiyama, M.6    Beppu, T.7


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