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Volumn 34, Issue 5, 1999, Pages 441-449

Novel alkaline serine proteases from alkalophilic Bacillus spp.: Purification and some properties

Author keywords

Alkalinity; Alkalophile; Bacillus; Properties; Purification; Serine proteases

Indexed keywords

2 DIETHYLAMINOETHANOL; ACETONE; ALBUMIN; AMINO ACID; BENZYLSULFONYL FLUORIDE; CALCIUM ION; CASEIN; ELASTIN; KERATIN; PROTEIN; REAGENT; SEPHAROSE; SERINE PROTEINASE; SYNTHETIC PEPTIDE;

EID: 0033165969     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0032-9592(98)00110-1     Document Type: Article
Times cited : (91)

References (46)
  • 2
    • 0020810350 scopus 로고
    • The benefit of detergent enzymes under changing washing conditions
    • Masse F.W.J.L., Van Tilburg R. The benefit of detergent enzymes under changing washing conditions. J. Am. Oil Chem. Soc. 60:1983;1672-1675.
    • (1983) J. Am. Oil Chem. Soc. , vol.60 , pp. 1672-1675
    • Masse, F.W.J.L.1    Van Tilburg, R.2
  • 3
  • 4
    • 0026044870 scopus 로고
    • Utilization of a thermostable alkaline protease from an alkalophilic thermophile for the recovery of silver from used X-ray film
    • Fujiwara N., Yamamoto K., Masui A. Utilization of a thermostable alkaline protease from an alkalophilic thermophile for the recovery of silver from used X-ray film. J. Ferment. Bioeng. 72:1991;306-308.
    • (1991) J. Ferment. Bioeng. , vol.72 , pp. 306-308
    • Fujiwara, N.1    Yamamoto, K.2    Masui, A.3
  • 5
    • 0003136322 scopus 로고
    • Studies on the use of dehairing enzyme for its suitability in the preparation of improved animal feed
    • Dhar S.C., Sreenivasulu S. Studies on the use of dehairing enzyme for its suitability in the preparation of improved animal feed. Leather Sci. 4:1986;23-30.
    • (1986) Leather Sci. , vol.4 , pp. 23-30
    • Dhar, S.C.1    Sreenivasulu, S.2
  • 6
    • 0027991463 scopus 로고
    • Utilization of waste feathers from poultry slaughter for production of a protein concentrate
    • Dalev P.G. Utilization of waste feathers from poultry slaughter for production of a protein concentrate. Bioresource Technol. 48:1994;265-267.
    • (1994) Bioresource Technol. , vol.48 , pp. 265-267
    • Dalev, P.G.1
  • 9
    • 0000580816 scopus 로고
    • Crystalline bacterial proteinase. I. Preparation of crystalline proteinase from Bacillus subtilis
    • Hagihara B., Matsubara H., Nakai M., Okunuki K. Crystalline bacterial proteinase. I. Preparation of crystalline proteinase from Bacillus subtilis. J. Biochem. (Tokyo). 45:1958;185-194.
    • (1958) J. Biochem. (Tokyo) , vol.45 , pp. 185-194
    • Hagihara, B.1    Matsubara, H.2    Nakai, M.3    Okunuki, K.4
  • 11
    • 0028883655 scopus 로고
    • Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530
    • Böckle B., Galunsky B., Müller R. Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530. Appl. Environ. Microbiol. 61:1995;3705-3710.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3705-3710
    • Böckle, B.1    Galunsky, B.2    Müller, R.3
  • 12
    • 0016767575 scopus 로고
    • The use of the direct linear plot for determining initial velocities
    • Cornish-Bowden A. The use of the direct linear plot for determining initial velocities. Biochem. J. 149:1975;305-312.
    • (1975) Biochem. J. , vol.149 , pp. 305-312
    • Cornish-Bowden, A.1
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of protein using the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of protein using the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0014949207 scopus 로고
    • Clevage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Clevage of structural proteins during assembly of the head of bacteriophage T4. Nature (London). 277:1970;680-685.
    • (1970) Nature (London) , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0009570410 scopus 로고
    • Gel electrophoresen
    • S. Bertram, & H.G. Gassen. Stuttgart: Gustav Fischer Verlag
    • Jany K.D., Hahn H., Kahnt B. Gel electrophoresen. Bertram S., Gassen H.G. Gentechnische Methoden. 1991;15-46 Gustav Fischer Verlag, Stuttgart.
    • (1991) Gentechnische Methoden , pp. 15-46
    • Jany, K.D.1    Hahn, H.2    Kahnt, B.3
  • 16
    • 0015395355 scopus 로고
    • Proteolytic components of alkaline proteases of Bacillus strains. Zymograms and electrophoretic isolation
    • Zuidweg M.H.J., Bos C.J.K., van Welzen H. Proteolytic components of alkaline proteases of Bacillus strains. Zymograms and electrophoretic isolation. Biotechnol. Bioeng. 14:1972;685-714.
    • (1972) Biotechnol. Bioeng. , vol.14 , pp. 685-714
    • Zuidweg, M.H.J.1    Bos, C.J.K.2    Van Welzen, H.3
  • 17
    • 0023258971 scopus 로고
    • Utility of subtilisin GX as a detergent additive
    • Durham D.R., Stewart D.B., Stellwag E.J. Utility of subtilisin GX as a detergent additive. J. Bacteriol. 169:1987;2762-2768.
    • (1987) J. Bacteriol. , vol.169 , pp. 2762-2768
    • Durham, D.R.1    Stewart, D.B.2    Stellwag, E.J.3
  • 18
    • 0030959204 scopus 로고    scopus 로고
    • Purification and characterization of the protease enzymes of Streptomyces thermovulgaris grown in rapemeal-derived media
    • Yeoman K.H., Edwards C. Purification and characterization of the protease enzymes of Streptomyces thermovulgaris grown in rapemeal-derived media. J. Appl. Microbiol. 82:1997;149-156.
    • (1997) J. Appl. Microbiol. , vol.82 , pp. 149-156
    • Yeoman, K.H.1    Edwards, C.2
  • 19
    • 0028093835 scopus 로고
    • Production of a thermophilic extracellular alkaline protease by Bacillus stearothermophilus AP-4
    • Dhandapani R., Vijayaragavan R. Production of a thermophilic extracellular alkaline protease by Bacillus stearothermophilus AP-4. World J. Microbiol. Biotechnol. 10:1994;33-35.
    • (1994) World J. Microbiol. Biotechnol. , vol.10 , pp. 33-35
    • Dhandapani, R.1    Vijayaragavan, R.2
  • 21
    • 0029069911 scopus 로고
    • Subtilisin Sendai from alkalophilic Bacullus sp.: Molecular and enzymatic properties of the enzyme and molecular cloning and characterization of the gene apr S
    • Yamagata Y., Ishiki K., Ichishima E. Subtilisin Sendai from alkalophilic Bacullus sp.: Molecular and enzymatic properties of the enzyme and molecular cloning and characterization of the gene apr S. Enzyme Microbial Technol. 17:1995;653-663.
    • (1995) Enzyme Microbial Technol. , vol.17 , pp. 653-663
    • Yamagata, Y.1    Ishiki, K.2    Ichishima, E.3
  • 22
    • 0025004609 scopus 로고
    • Characterization of an alkaline protease from Bacillus sp. No. AH-101
    • Takami H., Akiba T., Horikoshi K. Characterization of an alkaline protease from Bacillus sp. No. AH-101. Appl. Microbiol. Biotechnol. 33:1990;519-523.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 519-523
    • Takami, H.1    Akiba, T.2    Horikoshi, K.3
  • 23
    • 0026721550 scopus 로고
    • Purification and characterization of a thermostable proteinase isolated from Thermus sp. strain Rt41A
    • Peek K., Daniel R.M., Monk C., Parker L., Coolbear T. Purification and characterization of a thermostable proteinase isolated from Thermus sp. strain Rt41A. Eur. J. Biochem. 207:1992;1035-1044.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 1035-1044
    • Peek, K.1    Daniel, R.M.2    Monk, C.3    Parker, L.4    Coolbear, T.5
  • 24
    • 0002396657 scopus 로고
    • Production of alkaline protease in a low-cost medium by alkalophilic Bacillus sp. and properties of the enzyme
    • Fujiwara N., Yamamoto K. Production of alkaline protease in a low-cost medium by alkalophilic Bacillus sp. and properties of the enzyme. J. Ferment. Technol. 65:1987;345-348.
    • (1987) J. Ferment. Technol. , vol.65 , pp. 345-348
    • Fujiwara, N.1    Yamamoto, K.2
  • 25
    • 0029239715 scopus 로고
    • Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20)
    • Bhosale S.H., Rao M.B., Deshpande V.V., Srinivasan M.C. Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20). Enzyme Microbial Technol. 17:1995;136-139.
    • (1995) Enzyme Microbial Technol. , vol.17 , pp. 136-139
    • Bhosale, S.H.1    Rao, M.B.2    Deshpande, V.V.3    Srinivasan, M.C.4
  • 26
    • 0016410805 scopus 로고
    • Chemical studies of enzyme active sites
    • Sigma D.S., Mooser G. Chemical studies of enzyme active sites. Ann. Rev. Biochem. 44:1975;889-931.
    • (1975) Ann. Rev. Biochem. , vol.44 , pp. 889-931
    • Sigma, D.S.1    Mooser, G.2
  • 27
    • 0001170762 scopus 로고
    • Sulfonyl fluorides as inhibitors of esterases. II. Formation and reactions of phenylmethanesulfonyl alpha-chymotrypsin
    • Gold A.M., Fahrney D. Sulfonyl fluorides as inhibitors of esterases. II. Formation and reactions of phenylmethanesulfonyl alpha-chymotrypsin. Biochemistry. 3:1964;783-791.
    • (1964) Biochemistry , vol.3 , pp. 783-791
    • Gold, A.M.1    Fahrney, D.2
  • 28
    • 0016376184 scopus 로고
    • Comparative specificity of microbial proteinases
    • Morihara K. Comparative specificity of microbial proteinases. Adv. Enzymol. 41:1974;179-243.
    • (1974) Adv. Enzymol. , vol.41 , pp. 179-243
    • Morihara, K.1
  • 29
    • 0000824687 scopus 로고
    • Site-specific reagents for chymotrypsin and trypsin
    • Shaw E. Site-specific reagents for chymotrypsin and trypsin. Methods Enzymol. 11:1967;677-686.
    • (1967) Methods Enzymol. , vol.11 , pp. 677-686
    • Shaw, E.1
  • 30
    • 0028644160 scopus 로고
    • Cation-induced thermal stability of an alkaline protease from a Bacillus sp
    • Paliwal N., Singh S.P., Garg S.K. Cation-induced thermal stability of an alkaline protease from a Bacillus sp. Bioresource Technol. 50:1994;209-211.
    • (1994) Bioresource Technol. , vol.50 , pp. 209-211
    • Paliwal, N.1    Singh, S.P.2    Garg, S.K.3
  • 31
    • 0003128640 scopus 로고
    • Fermentative production of alkaline protease as detergent additive
    • Pan T., Lin S. Fermentative production of alkaline protease as detergent additive. J. Chinese Biochem. Soc. 20:1991;49-60.
    • (1991) J. Chinese Biochem. Soc. , vol.20 , pp. 49-60
    • Pan, T.1    Lin, S.2
  • 32
    • 0026864101 scopus 로고
    • Production of a low molecular weight, alkaline active, thermostable protease by a novel spiral-shaped bacterium
    • Steele D.B., Fiske M.J., Steele B.P., Kelley V.C. Production of a low molecular weight, alkaline active, thermostable protease by a novel spiral-shaped bacterium. Enzyme Microbial Technol. 14:1992;358-360.
    • (1992) Enzyme Microbial Technol. , vol.14 , pp. 358-360
    • Steele, D.B.1    Fiske, M.J.2    Steele, B.P.3    Kelley, V.C.4
  • 33
    • 0027263138 scopus 로고
    • Production and properties of an alkaline protease by Aureobasidium pullulans
    • Donaghy J.A., McKay A.M. Production and properties of an alkaline protease by Aureobasidium pullulans. J. Appl. Bacteriol. 74:1993;662-666.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 662-666
    • Donaghy, J.A.1    McKay, A.M.2
  • 34
    • 0015462313 scopus 로고
    • Biochemical effects of mercury, cadmium and lead
    • Vallee B.L., Ulmer D.D. Biochemical effects of mercury, cadmium and lead. Ann. Rev. Biochem. 41:1972;91-128.
    • (1972) Ann. Rev. Biochem. , vol.41 , pp. 91-128
    • Vallee, B.L.1    Ulmer, D.D.2
  • 36
    • 0022432710 scopus 로고
    • Limited proteolysis of thermolysin by subtilisin: Isolation and characterization of a partially active enzyme derivative
    • Vita C., Dalzappo D., Fontana A. Limited proteolysis of thermolysin by subtilisin: isolation and characterization of a partially active enzyme derivative. Biochemistry. 24:1985;1798-1806.
    • (1985) Biochemistry , vol.24 , pp. 1798-1806
    • Vita, C.1    Dalzappo, D.2    Fontana, A.3
  • 37
    • 0031993440 scopus 로고    scopus 로고
    • Thermostable alkaline metalloprotease from newly isolated alkalophilic Streptomyces diastaticus strain SS1
    • Chaphalkar S.R., Dey S. Thermostable alkaline metalloprotease from newly isolated alkalophilic Streptomyces diastaticus strain SS1. Indian J. Biochem. Biophys. 35:1998;34-40.
    • (1998) Indian J. Biochem. Biophys. , vol.35 , pp. 34-40
    • Chaphalkar, S.R.1    Dey, S.2
  • 39
    • 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. 295:1993;463-469.
    • (1993) Biochem. J. , vol.295 , pp. 463-469
    • Freeman, S.A.1    Peek, K.2    Prescott, M.3    Daniel, R.4
  • 40
    • 0027391904 scopus 로고
    • High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): Enzyme production and compatibility with commercial detergents
    • Phadatare S.U., Deshpande V.V., Srinivasan M.C. High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): enzyme production and compatibility with commercial detergents. Enzyme Microbial Technol. 15:1993;72-76.
    • (1993) Enzyme Microbial Technol. , vol.15 , pp. 72-76
    • Phadatare, S.U.1    Deshpande, V.V.2    Srinivasan, M.C.3
  • 42
    • 0014077484 scopus 로고
    • Elastolytic properties of various proteinases from microbial origin
    • Morihara K., Tsuzuki H. Elastolytic properties of various proteinases from microbial origin. Arch. Biochem. Biophys. 120:1967;68-78.
    • (1967) Arch. Biochem. Biophys. , vol.120 , pp. 68-78
    • Morihara, K.1    Tsuzuki, H.2
  • 43
    • 3042941091 scopus 로고
    • Pseudomonas aeruginosa elastase. Isolation, crystallization and preliminary characterization
    • Morihara K., Tsuzuki H., Oka T., Inoue H., Ebata M. Pseudomonas aeruginosa elastase. Isolation, crystallization and preliminary characterization. J. Biol. Chem. 240:1965;3295-3304.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3295-3304
    • Morihara, K.1    Tsuzuki, H.2    Oka, T.3    Inoue, H.4    Ebata, M.5
  • 45
    • 0018280687 scopus 로고
    • Enzymatic and chemical properties of an endopeptidase from the larva of the hornet Vespa crabro
    • Jany K.D., Haug H., Pfleiderer G., Ishay J. Enzymatic and chemical properties of an endopeptidase from the larva of the hornet Vespa crabro. Biochemistry. 17:1978;4675-4682.
    • (1978) Biochemistry , vol.17 , pp. 4675-4682
    • Jany, K.D.1    Haug, H.2    Pfleiderer, G.3    Ishay, J.4
  • 46
    • 0021838193 scopus 로고
    • Proteinase K from Tritirachium album Limber. I. Molecular mass and sequence around the active site serine residue
    • Jany K.D., Mayer B. Proteinase K from Tritirachium album Limber. I. Molecular mass and sequence around the active site serine residue. Biol. Chem. Hoppe-Seyler. 366:1985;485-492.
    • (1985) Biol. Chem. Hoppe-Seyler , vol.366 , pp. 485-492
    • Jany, K.D.1    Mayer, B.2


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