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Volumn 47, Issue 1-3, 2009, Pages 71-79

Alkaline proteases and thermostable α-amylase co-produced by Bacillus licheniformis NH1: Characterization and potential application as detergent additive

Author keywords

Amylase; Alkaline proteases; Bacillus licheniformis NH1; Crude enzyme; Detergent

Indexed keywords

ALKALINE PROTEASE; ALKALINE PROTEASES; ALKALOPHILIC; AMYLOLYTIC ACTIVITY; BACILLUS LICHENIFORMIS; BACILLUS LICHENIFORMIS NH1; CRUDE ENZYME; CRUDE ENZYMES; DETERGENT ADDITIVE; EXTRACELLULAR PROTEASE; LIQUID DETERGENTS; NONIONIC; OPTIMUM PH; OXIDIZING AGENTS; POTENTIAL APPLICATIONS; PRE-INCUBATION; PROCESSING INDUSTRY; PROTEOLYTIC ACTIVITIES; RELATIVE STABILITIES; WASH PERFORMANCE; ZYMOGRAPHY;

EID: 69349083943     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2009.07.005     Document Type: Article
Times cited : (161)

References (55)
  • 1
    • 33645975174 scopus 로고    scopus 로고
    • Enzymatic detergent formulation containing amylase from Aspergillus niger: a comparative study with commercial detergent formulations
    • Mitidieri S., Martinelli A.H.S., Schrank A., and Vainstein M.H. Enzymatic detergent formulation containing amylase from Aspergillus niger: a comparative study with commercial detergent formulations. Bioresour. Technol. 97 (2006) 1217-1224
    • (2006) Bioresour. Technol. , vol.97 , pp. 1217-1224
    • Mitidieri, S.1    Martinelli, A.H.S.2    Schrank, A.3    Vainstein, M.H.4
  • 2
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases from a bioindustrial viewpoint
    • Kumar C.G., and Takagi H. Microbial alkaline proteases from a bioindustrial viewpoint. Biotechnol. Adv. 17 (1999) 561-594
    • (1999) Biotechnol. Adv. , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 4
    • 0032950882 scopus 로고    scopus 로고
    • Bleach-stable, alkaline protease from Bacillus sp.
    • Gupta R., Gupta K., Saxena R.K., and Khan S. Bleach-stable, alkaline protease from Bacillus sp. Biotechnol. Lett. 21 (1999) 135-138
    • (1999) Biotechnol. Lett. , vol.21 , pp. 135-138
    • Gupta, R.1    Gupta, K.2    Saxena, R.K.3    Khan, S.4
  • 5
    • 0034714147 scopus 로고    scopus 로고
    • Thermal stable and oxidation resistant variant of subtilisin E
    • Yang Y., Jiang L., Zhu L., Wu Y., and Yang S. Thermal stable and oxidation resistant variant of subtilisin E. J. Biotechnol. 81 (2000) 113-118
    • (2000) J. Biotechnol. , vol.81 , pp. 113-118
    • Yang, Y.1    Jiang, L.2    Zhu, L.3    Wu, Y.4    Yang, S.5
  • 6
    • 0037415288 scopus 로고    scopus 로고
    • Purification and characterization of an oxidation-stable, thiol-dependent serine alkaline protease from Bacillus mojavensis
    • Beg Q.K., and Gupta R. Purification and characterization of an oxidation-stable, thiol-dependent serine alkaline protease from Bacillus mojavensis. Enzyme Microb. Technol. 32 (2003) 294-304
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 294-304
    • Beg, Q.K.1    Gupta, R.2
  • 8
    • 27844533545 scopus 로고    scopus 로고
    • Production of an oxidant and SDS-stable alkaline protease from an alkalophilic Bacillus clausii I-52 by submerged fermentation: feasibility as a laundry detergent additive
    • Joo H.S., and Chang C.S. Production of an oxidant and SDS-stable alkaline protease from an alkalophilic Bacillus clausii I-52 by submerged fermentation: feasibility as a laundry detergent additive. Enzyme Microb. Technol. 38 (2006) 176-183
    • (2006) Enzyme Microb. Technol. , vol.38 , pp. 176-183
    • Joo, H.S.1    Chang, C.S.2
  • 9
    • 64249165670 scopus 로고    scopus 로고
    • Characterization of amylase and protease produced by Aspergillus awamori in a single bioreactor
    • Negi S., and Banerjee R. Characterization of amylase and protease produced by Aspergillus awamori in a single bioreactor. Food Res. Int. 42 (2009) 443-448
    • (2009) Food Res. Int. , vol.42 , pp. 443-448
    • Negi, S.1    Banerjee, R.2
  • 10
    • 0032719428 scopus 로고    scopus 로고
    • Protease and amylase production of Streptomyces rimosus in submerged and solid state cultivations
    • Yang S.S., and Wang J.Y. Protease and amylase production of Streptomyces rimosus in submerged and solid state cultivations. Bot. Bull. Acad. Sin. 40 (1999) 259-265
    • (1999) Bot. Bull. Acad. Sin. , vol.40 , pp. 259-265
    • Yang, S.S.1    Wang, J.Y.2
  • 11
    • 33847265270 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated Bacillus licheniformis NH1
    • El Hadj-Ali N., Agrebi R., Ghorbel-Frikha B., Sellami-Kamoun A., Kanoun S., and Nasri M. Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated Bacillus licheniformis NH1. Enzyme Microb. Technol. 40 (2007) 515-523
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 515-523
    • El Hadj-Ali, N.1    Agrebi, R.2    Ghorbel-Frikha, B.3    Sellami-Kamoun, A.4    Kanoun, S.5    Nasri, M.6
  • 13
    • 0027352759 scopus 로고
    • Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64
    • Kembhavi A.A., Kulkarni A., and Pant A. Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64. Appl. Biochem. Biotechnol. 38 (1993) 83-92
    • (1993) Appl. Biochem. Biotechnol. , vol.38 , pp. 83-92
    • Kembhavi, A.A.1    Kulkarni, A.2    Pant, A.3
  • 14
    • 84907129352 scopus 로고
    • Isolation of an extracellular proteinase (keratinase) from Microsporum canis
    • Takiuchi I., Higuchi D., Sei Y., and Koga M. Isolation of an extracellular proteinase (keratinase) from Microsporum canis. Sabouraudia 20 (1982) 281-288
    • (1982) Sabouraudia , vol.20 , pp. 281-288
    • Takiuchi, I.1    Higuchi, D.2    Sei, Y.3    Koga, M.4
  • 15
    • 33747333106 scopus 로고
    • Use of dinitrosalycilic acid reagent for determination of reducing sugars
    • Miller G.L. Use of dinitrosalycilic acid reagent for determination of reducing sugars. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 16
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors
    • Garcia-Carreno F.L., Dimes L.E., and Haard N.F. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Anal. Biochem. 214 (1993) 65-69
    • (1993) Anal. Biochem. , vol.214 , pp. 65-69
    • Garcia-Carreno, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 17
    • 0019139168 scopus 로고
    • Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate
    • Lacks S.A., and Springhorn S.S. Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. J. Biol. Chem. 255 (1980) 7467-7473
    • (1980) J. Biol. Chem. , vol.255 , pp. 7467-7473
    • Lacks, S.A.1    Springhorn, S.S.2
  • 18
  • 19
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: molecular approaches and industrial applications
    • Gupta R., Beg Q., and Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 59 (2002) 15-32
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.2    Lorenz, P.3
  • 20
    • 57649176803 scopus 로고    scopus 로고
    • To study the influence of different components of fermentable substrates on induction of extracellular α-amylase synthesis by Bacillus subtilis DM-03 in solid-state fermentation and exploration of feasibility for inclusion of α-amylase in laundry detergent formulations
    • Mukherjee A.K., Borah M., and Rai S.K. To study the influence of different components of fermentable substrates on induction of extracellular α-amylase synthesis by Bacillus subtilis DM-03 in solid-state fermentation and exploration of feasibility for inclusion of α-amylase in laundry detergent formulations. Biochem. Eng. J. 43 (2009) 149-156
    • (2009) Biochem. Eng. J. , vol.43 , pp. 149-156
    • Mukherjee, A.K.1    Borah, M.2    Rai, S.K.3
  • 21
    • 41549139096 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a novel α-amylase from Bacillus licheniformis NH1. Cloning, nucleotide sequence and expression of amyN gene in E. coli
    • Hmidet N., Bayoudh A., Berrin J.G., Kanoun S., Juge N., and Nasri M. Purification and biochemical characterization of a novel α-amylase from Bacillus licheniformis NH1. Cloning, nucleotide sequence and expression of amyN gene in E. coli. Process Biochem. 43 (2008) 499-510
    • (2008) Process Biochem. , vol.43 , pp. 499-510
    • Hmidet, N.1    Bayoudh, A.2    Berrin, J.G.3    Kanoun, S.4    Juge, N.5    Nasri, M.6
  • 22
    • 0035214560 scopus 로고    scopus 로고
    • Fermentation characteristics and secretion of proteases of a new keratinolytic strain of Bacillus licheniformis
    • Rozs M., Manczinger L., Vagvölgyi Cs., Kevei F., Hochkoeppler A., and Rodri{dotless}guez A.G.V. Fermentation characteristics and secretion of proteases of a new keratinolytic strain of Bacillus licheniformis. Biotechnol. Lett. 23 (2001) 1925-1929
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1925-1929
    • Rozs, M.1    Manczinger, L.2    Vagvölgyi, Cs.3    Kevei, F.4    Hochkoeppler, A.5    Rodriguez, A.G.V.6
  • 23
    • 0029948243 scopus 로고    scopus 로고
    • Thermostable alkaline proteases of Bacillus licheniformis MIR 29: isolation, production and characterization
    • Ferrero M.A., Castro G.R., Abate C.M., Baigorõ M.D., and Sineriz F. Thermostable alkaline proteases of Bacillus licheniformis MIR 29: isolation, production and characterization. Appl. Microbiol. Biotechnol. 45 (1996) 327-332
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 327-332
    • Ferrero, M.A.1    Castro, G.R.2    Abate, C.M.3    Baigorõ, M.D.4    Sineriz, F.5
  • 24
    • 58049217428 scopus 로고    scopus 로고
    • A novel surfactant-stable alkaline serine-protease from a newly isolated Bacillus mojavensis A21. Purification and characterization
    • Haddar A., Bougatef A., Agrebi R., Sellami-Kamoun A., and Nasri M. A novel surfactant-stable alkaline serine-protease from a newly isolated Bacillus mojavensis A21. Purification and characterization. Process Biochem. 44 (2009) 29-35
    • (2009) Process Biochem. , vol.44 , pp. 29-35
    • Haddar, A.1    Bougatef, A.2    Agrebi, R.3    Sellami-Kamoun, A.4    Nasri, M.5
  • 25
    • 63449085549 scopus 로고    scopus 로고
    • Purification and characterization of two surfactant-stable alkaline serine-proteases from Bacillus mojavensis A21
    • Haddar A., Agrebi R., Bougatef A., Hmidet N., Sellami-Kamoun A., and Nasri M. Purification and characterization of two surfactant-stable alkaline serine-proteases from Bacillus mojavensis A21. Bioresour. Technol. 100 (2009) 3366-3373
    • (2009) Bioresour. Technol. , vol.100 , pp. 3366-3373
    • Haddar, A.1    Agrebi, R.2    Bougatef, A.3    Hmidet, N.4    Sellami-Kamoun, A.5    Nasri, M.6
  • 26
    • 0036304510 scopus 로고    scopus 로고
    • Characterization of a salt-tolerant extracellular α-amylase from Bacillus dipsosauri
    • Deutch C.E. Characterization of a salt-tolerant extracellular α-amylase from Bacillus dipsosauri. Lett. Appl. Microbiol. 35 (2002) 78-84
    • (2002) Lett. Appl. Microbiol. , vol.35 , pp. 78-84
    • Deutch, C.E.1
  • 27
    • 0038613858 scopus 로고    scopus 로고
    • Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6
    • Burhan A., Nisa U., Gokhan C., Omer C., Ashabil A., and Osman G. Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6. Process Biochem. 38 (2003) 1397-1403
    • (2003) Process Biochem. , vol.38 , pp. 1397-1403
    • Burhan, A.1    Nisa, U.2    Gokhan, C.3    Omer, C.4    Ashabil, A.5    Osman, G.6
  • 28
    • 18244408263 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20
    • Najafi M.F., Deobagkar D., and Deobagkar D. Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20. Protein Exp. Purif. 41 (2005) 349-354
    • (2005) Protein Exp. Purif. , vol.41 , pp. 349-354
    • Najafi, M.F.1    Deobagkar, D.2    Deobagkar, D.3
  • 29
    • 0032803951 scopus 로고    scopus 로고
    • Effect of cultivation conditions on growth and alpha amylase production by a thermophilic Bacillus sp.
    • Mamo G., and Gessesse A. Effect of cultivation conditions on growth and alpha amylase production by a thermophilic Bacillus sp. Lett. Appl. Microbiol. 29 (1999) 61-65
    • (1999) Lett. Appl. Microbiol. , vol.29 , pp. 61-65
    • Mamo, G.1    Gessesse, A.2
  • 30
    • 0029119475 scopus 로고
    • Purification and characterisation of a maltotetraose-forming alkaline α-amylase from an alkaliphilic Bacillus strain GM8901
    • Kim T.U., Gu B.G., Jeong J.Y., Byun S.M., and Shin Y.C. Purification and characterisation of a maltotetraose-forming alkaline α-amylase from an alkaliphilic Bacillus strain GM8901. Appl. Environ. Microbiol. 61 (1995) 3105-3112
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3105-3112
    • Kim, T.U.1    Gu, B.G.2    Jeong, J.Y.3    Byun, S.M.4    Shin, Y.C.5
  • 31
    • 9944220238 scopus 로고
    • Cloning and expression of the maltohexaose-forming amylase gene from alkalophilic Bacillus sp. H-167 in Escherichia coli
    • Shirokizawa O., Akiba T., and Horikoshi K. Cloning and expression of the maltohexaose-forming amylase gene from alkalophilic Bacillus sp. H-167 in Escherichia coli. Agric. Biol. Chem. 53 (1989) 491-495
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 491-495
    • Shirokizawa, O.1    Akiba, T.2    Horikoshi, K.3
  • 33
    • 3042633826 scopus 로고    scopus 로고
    • Laundry detergent compatibility of the alkaline protease from Bacillus cereus
    • Banik R.M., and Prakash M. Laundry detergent compatibility of the alkaline protease from Bacillus cereus. Microbiol. Res. 159 (2004) 135-140
    • (2004) Microbiol. Res. , vol.159 , pp. 135-140
    • Banik, R.M.1    Prakash, M.2
  • 34
    • 57449096150 scopus 로고    scopus 로고
    • A novel organic solvent-stable alkaline protease from organic solvent-tolerant Bacillus licheniformis YP1A
    • Li S., He B., Bai Z., and Ouyang P. A novel organic solvent-stable alkaline protease from organic solvent-tolerant Bacillus licheniformis YP1A. J. Mol. Catal. B: Enzym. 56 (2009) 85-88
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 85-88
    • Li, S.1    He, B.2    Bai, Z.3    Ouyang, P.4
  • 35
    • 0027416966 scopus 로고
    • Purification and characterization of a thermostable alpha-amylase from Bacillus licheniformis
    • Ivanova V.N., Dobreva E.P., and Emanuilova E.I. Purification and characterization of a thermostable alpha-amylase from Bacillus licheniformis. J. Biotechnol. 28 (1993) 277-289
    • (1993) J. Biotechnol. , vol.28 , pp. 277-289
    • Ivanova, V.N.1    Dobreva, E.P.2    Emanuilova, E.I.3
  • 36
    • 0030321729 scopus 로고    scopus 로고
    • Thermostable alpha-amylase production using Bacillus licheniformis NRRL B14368
    • Bose K., and Das D. Thermostable alpha-amylase production using Bacillus licheniformis NRRL B14368. Indian J. Exp. Biol. 34 (1996) 1279-1282
    • (1996) Indian J. Exp. Biol. , vol.34 , pp. 1279-1282
    • Bose, K.1    Das, D.2
  • 37
    • 33746870417 scopus 로고    scopus 로고
    • Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis α-amylases and insights into engineering α-amylase variants active under acidic conditions
    • Lee S., Oneda H., Minoda M., Tanaka A., and Inouye K. Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis α-amylases and insights into engineering α-amylase variants active under acidic conditions. J. Biochem. 39 (2006) 997-1005
    • (2006) J. Biochem. , vol.39 , pp. 997-1005
    • Lee, S.1    Oneda, H.2    Minoda, M.3    Tanaka, A.4    Inouye, K.5
  • 38
    • 0019350138 scopus 로고
    • Characterization of a thermostable α-amylase from Bacillus licheniformis NCIB 6346
    • Morgan F.J., and Priest F.G. Characterization of a thermostable α-amylase from Bacillus licheniformis NCIB 6346. J. Appl. Bacteriol. 50 (1981) 107-114
    • (1981) J. Appl. Bacteriol. , vol.50 , pp. 107-114
    • Morgan, F.J.1    Priest, F.G.2
  • 39
    • 0024961629 scopus 로고
    • High-temperature alkaline α-amylase from Bacillus licheniformis TCRDC-B13
    • Bajpai P., and Bajpai P.K. High-temperature alkaline α-amylase from Bacillus licheniformis TCRDC-B13. Biotechnol. Bioeng. 33 (1989) 72-78
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 72-78
    • Bajpai, P.1    Bajpai, P.K.2
  • 40
    • 0034769033 scopus 로고    scopus 로고
    • Characterization and wash performance analysis of an SDS-stable alkaline protease from a Bacillus sp.
    • Oberoi R., Beg Q.K., Puri S., Saxena R.K., and Gupta R. Characterization and wash performance analysis of an SDS-stable alkaline protease from a Bacillus sp. World J. Microbiol. Biotechnol. 17 (2001) 493-497
    • (2001) World J. Microbiol. Biotechnol. , vol.17 , pp. 493-497
    • Oberoi, R.1    Beg, Q.K.2    Puri, S.3    Saxena, R.K.4    Gupta, R.5
  • 41
    • 0023661282 scopus 로고
    • Three dimensional structure of porcin pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity
    • Buisson G., Duee D., Haser R., and Payan F. Three dimensional structure of porcin pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity. EMBO J. 6 (1987) 3909-3916
    • (1987) EMBO J. , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duee, D.2    Haser, R.3    Payan, F.4
  • 44
    • 0023134530 scopus 로고
    • Production and activation of an SDS-resistant alkaline serine exoprotease of Vibrio alginolyticus
    • Deane S.M., Robb F.T., and Woods D.R. Production and activation of an SDS-resistant alkaline serine exoprotease of Vibrio alginolyticus. J. Gen. Microbiol. 133 (1987) 391-398
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 391-398
    • Deane, S.M.1    Robb, F.T.2    Woods, D.R.3
  • 45
    • 34047118808 scopus 로고    scopus 로고
    • Purification and characterization of an alkaline serine-protease produced by a newly isolated Aspergillus clavatus ES1
    • Hajji M., Kanoun S., Nasri M., and Gharsallah N. Purification and characterization of an alkaline serine-protease produced by a newly isolated Aspergillus clavatus ES1. Process Biochem. 42 (2007) 791-797
    • (2007) Process Biochem. , vol.42 , pp. 791-797
    • Hajji, M.1    Kanoun, S.2    Nasri, M.3    Gharsallah, N.4
  • 46
    • 41649114336 scopus 로고    scopus 로고
    • Stability of thermostable alkaline protease from Bacillus licheniformis RP1 in commercial solid laundry detergent formulations
    • Sellami-Kamoun A., Haddar A., El-Hadj Ali N., Ghorbel-Frikha B., Kanoun S., and Nasri M. Stability of thermostable alkaline protease from Bacillus licheniformis RP1 in commercial solid laundry detergent formulations. Microbiol. Res. 163 (2008) 299-306
    • (2008) Microbiol. Res. , vol.163 , pp. 299-306
    • Sellami-Kamoun, A.1    Haddar, A.2    El-Hadj Ali, N.3    Ghorbel-Frikha, B.4    Kanoun, S.5    Nasri, M.6
  • 47
    • 0035066633 scopus 로고    scopus 로고
    • Enzymatic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli
    • Lo H.F., Lin L.L., Chen H.L., Hsu W.H., and Chang C.T. Enzymatic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli. Process Biochem. 36 (2001) 743-750
    • (2001) Process Biochem. , vol.36 , pp. 743-750
    • Lo, H.F.1    Lin, L.L.2    Chen, H.L.3    Hsu, W.H.4    Chang, C.T.5
  • 48
    • 0035069423 scopus 로고    scopus 로고
    • Serine alkaline protease from a newly isolated Bacillus sp. SSR1
    • Singh J., Batra N., and Sobti R.C. Serine alkaline protease from a newly isolated Bacillus sp. SSR1. Process Biochem. 36 (2001) 781-785
    • (2001) Process Biochem. , vol.36 , pp. 781-785
    • Singh, J.1    Batra, N.2    Sobti, R.C.3
  • 49
    • 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., and Srinivasan M.C. Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20). Enzyme Microb. Technol. 17 (1995) 136-139
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 136-139
    • Bhosale, S.H.1    Rao, M.B.2    Deshpande, V.V.3    Srinivasan, M.C.4
  • 50
    • 40049103299 scopus 로고    scopus 로고
    • Production of alkaline protease by a thermophilic Bacillus subtilis under solid-state fermentation (SSF) condition using Imperata cylindrical grass and potato peel as low-cost medium: characterization and application of enzyme in detergent formulation
    • Mukherjee A.K., Adhikari H., and Rai S.K. Production of alkaline protease by a thermophilic Bacillus subtilis under solid-state fermentation (SSF) condition using Imperata cylindrical grass and potato peel as low-cost medium: characterization and application of enzyme in detergent formulation. Biochem. Eng. J. 39 (2008) 353-361
    • (2008) Biochem. Eng. J. , vol.39 , pp. 353-361
    • Mukherjee, A.K.1    Adhikari, H.2    Rai, S.K.3
  • 52
    • 0031052318 scopus 로고    scopus 로고
    • Alkaline pH acting digestive enzymes of the polyphagous insect pest Spilosoma obliqua: stability and potential as detergent additives
    • Anwar A., and Saleemuddin M. Alkaline pH acting digestive enzymes of the polyphagous insect pest Spilosoma obliqua: stability and potential as detergent additives. Biotechnol. Appl. Biochem. 25 (1997) 43-46
    • (1997) Biotechnol. Appl. Biochem. , vol.25 , pp. 43-46
    • Anwar, A.1    Saleemuddin, M.2
  • 53
    • 0032716420 scopus 로고    scopus 로고
    • Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive
    • Banerjee U.C., Sani R.K., Azmi W., and Soni R. Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive. Process Biochem. 35 (1999) 213-219
    • (1999) Process Biochem. , vol.35 , pp. 213-219
    • Banerjee, U.C.1    Sani, R.K.2    Azmi, W.3    Soni, R.4
  • 54
    • 58249140685 scopus 로고    scopus 로고
    • Characterization of thermo- and detergent stable serine protease from isolated Bacillus circulans and evaluation of eco-friendly applications
    • Rao C.S., Sathish T., Ravichandra P., and Prakasham R.S. Characterization of thermo- and detergent stable serine protease from isolated Bacillus circulans and evaluation of eco-friendly applications. Process Biochem. 44 (2009) 262-268
    • (2009) Process Biochem. , vol.44 , pp. 262-268
    • Rao, C.S.1    Sathish, T.2    Ravichandra, P.3    Prakasham, R.S.4
  • 55
    • 53049083724 scopus 로고    scopus 로고
    • Production of alkaline proteases by Botrytis cinerea using economic raw materials: assay as biodetergent
    • Abidi F., Limam F., and Marzouki M.N. Production of alkaline proteases by Botrytis cinerea using economic raw materials: assay as biodetergent. Process Biochem. 43 (2008) 1202-1208
    • (2008) Process Biochem. , vol.43 , pp. 1202-1208
    • Abidi, F.1    Limam, F.2    Marzouki, M.N.3


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