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Volumn 4, Issue 4, 2008, Pages 354-366

Perspectives of solid state fermentation for production of food enzymes

Author keywords

Food enzymes; Production; Solid state culture

Indexed keywords

APPLICATION STUDIES; ECONOMIC SECTORS; FOOD ENZYMES; FOOD INDUSTRIES; PECTINASES; PHYTASES; PROCESS CHARACTERISTICS; SOLID STATE CULTURE; SOLID-STATE FERMENTATION; SUBMERGED CULTURES; SUBMERGED FERMENTATION; XYLANASES;

EID: 68249111211     PISSN: 15533468     EISSN: None     Source Type: Journal    
DOI: 10.3844/ajbbsp.2008.354.366     Document Type: Article
Times cited : (55)

References (124)
  • 4
    • 68249116544 scopus 로고    scopus 로고
    • Ed. Mexican Alhambra, México
    • Baduí, S., 1996. Chemistry of the Foods. Ed. Mexican Alhambra, México, pp: 281-326.
    • (1996) Chemistry of the Foods , pp. 281-326
    • Baduí, S.1
  • 7
    • 1842844848 scopus 로고    scopus 로고
    • Culture conditions dictate protease and tannase production in submerged and solid-state cultures by Aspergillus niger Aa-20
    • Aguilar, C.N., E. Favela-Torres, G. Viniegra-González and C. Augur, 2002. Culture conditions dictate protease and tannase production in submerged and solid-state cultures by Aspergillus niger Aa-20. Applied Biochem. Biotechnol., 102-103: 407-414.
    • (2002) Applied Biochem. Biotechnol. , vol.102-103 , pp. 407-414
    • Aguilar, C.N.1    Favela-Torres, E.2    Viniegra-González, G.3    Augur, C.4
  • 8
    • 0018884243 scopus 로고
    • Culture method to study fungal growth in solid fermentation
    • Raimbault, M. and Alazardd., 1980. Culture method to study fungal growth in solid fermentation. Eur. J. Applied Microbiol. Biotechnol., 9: 199-209.
    • (1980) Eur. J. Applied Microbiol. Biotechnol. , vol.9 , pp. 199-209
    • Raimbault, M.1    Alazardd2
  • 9
    • 0000224704 scopus 로고
    • Growth kinetics of Rhizopus arrhizus in solid state fermentation of treated cassava
    • Soccol, C., J.R. Leon, B. Marin, S. Roussos and M. Raimbault, 1993. Growth kinetics of Rhizopus arrhizus in solid state fermentation of treated cassava. Biotechnology Techniques, 7: 563-568.
    • (1993) Biotechnology Techniques , vol.7 , pp. 563-568
    • Soccol, C.1    Leon, J.R.2    Marin, B.3    Roussos, S.4    Raimbault, M.5
  • 10
    • 0001896452 scopus 로고    scopus 로고
    • General and microbiological aspects of solid state fermentation
    • Raimbault, M., 1998. General and microbiological aspects of solid state fermentation. Electronic. J. Biotechnol., 1: 3-21.
    • (1998) Electronic. J. Biotechnol. , vol.1 , pp. 3-21
    • Raimbault, M.1
  • 11
  • 13
    • 0027262844 scopus 로고
    • New approach for selecting pectinases producing mutants of Aspergillus niger well adapted to solid state fermentation
    • Antier, P., A. Minjares, S. Roussos and G. Viniegra-González, 1993. New approach for selecting pectinases producing mutants of Aspergillus niger well adapted to solid state fermentation. Biotechnol. Adv., 11: 429-440.
    • (1993) Biotechnol. Adv. , vol.11 , pp. 429-440
    • Antier, P.1    Minjares, A.2    Roussos, S.3    Viniegra-González, G.4
  • 14
    • 0027510675 scopus 로고
    • Effects of different coal sources on the synthesis of pectinases by Aspergillus niger in submerged and solid state fermentations
    • Sólis-Pereíra, S., E. Favela-Torres, G. Viniegra- González and M. Gutiérrez-Rojas, 1993. Effects of different coal sources on the synthesis of pectinases by Aspergillus niger in submerged and solid state fermentations. Applied Microbiol. Biotechnol., 39: 36-41.
    • (1993) Applied Microbiol. Biotechnol. , vol.39 , pp. 36-41
    • Sólis-Pereíra, S.1    Favela-Torres, E.2    Viniegra-González, G.3    Gutiérrez-Rojas, M.4
  • 15
    • 15444346453 scopus 로고    scopus 로고
    • Produciton of pectinesterase and polygalacturonase by Aspergillus niger in submerged and solid state systems
    • Maldonado, M.C. and A.M. Strasser Of Saad, 1998. Produciton of pectinesterase and polygalacturonase by Aspergillus niger in submerged and solid state systems. J. Ind. Microbiol. Biotechnol., 20: 34-38.
    • (1998) J. Ind. Microbiol. Biotechnol. , vol.20 , pp. 34-38
    • Maldonado, M.C.1    Strasser Of Saad, A.M.2
  • 16
  • 17
    • 0032694326 scopus 로고    scopus 로고
    • Caffeine degradation in solid state fermentation by Aspergillus tamarii: Effects of additional nitrogen sources
    • Hakil, M., F. Voisinet, G. Viniegra-González and C. Augur, 1999. Caffeine degradation in solid state fermentation by Aspergillus tamarii: Effects of additional nitrogen sources. Process Bioch., 35: 103-109.
    • (1999) Process Bioch. , vol.35 , pp. 103-109
    • Hakil, M.1    Voisinet, F.2    Viniegra-González, G.3    Augur, C.4
  • 19
    • 0013249985 scopus 로고    scopus 로고
    • Lipase production by Penicillium restrictum using solid waste of industrial babassu oil production as substrate
    • Palma, M.B., A.L. Pinto, A.K. Gombert, K.H. Seitz, L.R. Castilho and D.M.G. Freire, 2000. Lipase production by Penicillium restrictum using solid waste of industrial babassu oil production as substrate. Applied Biochem. Biotechnol., 84/86: 1137-1145.
    • (2000) Applied Biochem. Biotechnol. , vol.84-86 , pp. 1137-1145
    • Palma, M.B.1    Pinto, A.L.2    Gombert, A.K.3    Seitz, K.H.4    Castilho, L.R.5    Freire, D.M.G.6
  • 21
    • 0030943531 scopus 로고    scopus 로고
    • Comparative study of protease production in solid substrate fermentation versus submerged fermentation
    • DOI 10.1007/s004490050339
    • George, S., V. Raju, V. Subramanian and K. Jayaraman, 1997. Comparative study of protease production in solid substrate fermentation versus submerged fermentation. Bioprocess Eng., 16: 381-382. (Pubitemid 27230964)
    • (1997) Bioprocess Engineering , vol.16 , Issue.6 , pp. 381-382
    • George, S.1    Raju, V.2    Subramanian, T.V.3    Jayaraman, K.4
  • 22
    • 0000504092 scopus 로고
    • Principles of solid state fermentation
    • Smith, J., D. Berry and B. Kristiansen (Eds.). Edward Arnold Publishers, London
    • Moo-Young, M., A. Moreira and R. Tengerdy, 1983. Principles of solid state fermentation. In: Fungal Biotechnology, Smith, J., D. Berry and B. Kristiansen (Eds.). Edward Arnold Publishers, London, pp: 117-144.
    • (1983) Fungal Biotechnology , pp. 117-144
    • Moo-Young, M.1    Moreira, A.2    Tengerdy, R.3
  • 24
    • 0002858605 scopus 로고
    • Demain, A. and N. Solomon (Eds.). American Society for Microbiology, Washington, AD
    • Mudgett, R., 1986. Manual of Industrial Microbiology and Biotechnology. Demain, A. and N. Solomon (Eds.). American Society for Microbiology, Washington, AD., pp: 66-83.
    • (1986) Manual of Industrial Microbiology and Biotechnology , pp. 66-83
    • Mudgett, R.1
  • 25
    • 0031952248 scopus 로고    scopus 로고
    • Overproduction of rifamycin B by Amycolatopsis mediterranei and its relationship with the toxic effect of barbital on growth
    • Mejia, A., J. Barrios-González and G. Viniegra-González, 1998. Overproduction of rifamycin B by Amycolatopsis mediterranei and its relationship with the toxic effect of barbital on growth. J. Antibiotics, 51: 58-63.
    • (1998) J. Antibiotics , vol.51 , pp. 58-63
    • Mejia, A.1    Barrios-González, J.2    Viniegra-González, G.3
  • 26
    • 0032005104 scopus 로고    scopus 로고
    • Kinetics of growth of Aspergillus niger during submerged, agar surface and solid state fermentations
    • Favela-Tores, E., J. Córdova-López, M. García- Rivero and M. Gutierrez-Rojas, 1998. Kinetics of growth of Aspergillus niger during submerged, agar surface and solid state fermentations. Process Biochem., 33: 103-107.
    • (1998) Process Biochem. , vol.33 , pp. 103-107
    • Favela-Tores, E.1    Córdova-López, J.2    García-Rivero, M.3    Gutierrez-Rojas, M.4
  • 27
    • 0033812885 scopus 로고    scopus 로고
    • Production of 6-pentyl-a-pyrone by Trichoderma harzianum in liquid and solid state cultures
    • Shary-Bagnon, V., P. Lozano, G. Saucedo- Castañeda and S. Roussos, 2000. Production of 6-pentyl-a-pyrone by Trichoderma harzianum in liquid and solid state cultures. Process Biochem., 36: 103-109.
    • (2000) Process Biochem. , vol.36 , pp. 103-109
    • Shary-Bagnon, V.1    Lozano, P.2    Saucedo-Castañeda, G.3    Roussos, S.4
  • 28
    • 0002827194 scopus 로고
    • Solid-state fermentation
    • Hesseltine, C.W., 1977. Solid-state fermentation. Process Biochem., 12: 22-24.
    • (1977) Process Biochem. , vol.12 , pp. 22-24
    • Hesseltine, C.W.1
  • 29
    • 0035143223 scopus 로고    scopus 로고
    • Induction and repression patterns of fungal tannase in solid-state and submerged cultures
    • Aguilar, C.N., C. Augur, E. Favela-Torres and G. Viniegra- González, 2001. Induction and repression patterns of fungal tannase in solid-state and submerged cultures. Process Biochem., 36: 565-570.
    • (2001) Process Biochem. , vol.36 , pp. 565-570
    • Aguilar, C.N.1    Augur, C.2    Favela-Torres, E.3    Viniegra-González, G.4
  • 30
    • 68249095714 scopus 로고
    • Microbial basis of procedures
    • Doelle, H., D. Mitchell and C. Rolz (Eds.). Elsevier, London
    • Mitchell D.A., 1992. Microbial basis of procedures. In: Solid state cultivation, Doelle, H., D. Mitchell and C. Rolz (Eds.). Elsevier, London.
    • (1992) Solid State Cultivation
    • Mitchell, D.A.1
  • 31
    • 0025738415 scopus 로고
    • Ability of to solid state fermentation technique to significantly minimize catabolic repression of ά-amilase production by Bacillus licheniformis M27
    • Ramesh, M.V. and B.K. Lonsane, 1991. Ability of to solid state fermentation technique to significantly minimize catabolic repression of (ά-amilase production by Bacillus licheniformis M27. Applied Microbiol. Biotechnol., 35: 591-593.
    • (1991) Applied Microbiol. Biotechnol. , vol.35 , pp. 591-593
    • Ramesh, M.V.1    Lonsane, B.K.2
  • 32
    • 0028154325 scopus 로고
    • Comparative titres, location and properties of tannin acyl hydrolase produced by Aspergillus niger PKL104 in solid-state, liquid surface and submerged fermentations
    • Lekha, P.K. and B.K. Lonsane, 1994. Comparative titres, location and properties of tannin acyl hydrolase produced by Aspergillus niger PKL104 in solid-state, liquid surface and submerged fermentations. Proceeding Biochem., 29: 497-503.
    • (1994) Proceeding Biochem. , vol.29 , pp. 497-503
    • Lekha, P.K.1    Lonsane, B.K.2
  • 34
    • 0030773429 scopus 로고    scopus 로고
    • Production and application of tannin acyl hydrolase: State of the art
    • Lekha, P.K. and B.K. Lonsane, 1997. Production and application of tannin acyl hydrolase: State of the art. Adv. Applied Microbiol., 44: 215-260.
    • (1997) Adv. Applied Microbiol. , vol.44 , pp. 215-260
    • Lekha, P.K.1    Lonsane, B.K.2
  • 35
    • 0007103038 scopus 로고    scopus 로고
    • Partial purification of tanasa taken place by Aspergillus niger in fermentation between solid
    • Prado, A., S. Huerta, S. Rodríguez and G. Saucedo, (Eds.). Edition UAMI., Mexico, DF
    • García-Peña, I., E. Favela-Torres and C. Augur, 1999. Partial purification of tanasa taken place by Aspergillus niger in fermentation between solid. In: Advance in purification and application of enzymes in biotechnology, Prado, A., S. Huerta, S. Rodríguez and G. Saucedo, (Eds.). Edition UAMI., Mexico, DF., pp: 247-261.
    • (1999) Advance in Purification and Application of Enzymes in Biotechnology , pp. 247-261
    • García-Peña, I.1    Favela-Torres, E.2    Augur, C.3
  • 36
    • 0034902542 scopus 로고    scopus 로고
    • Production of tannase by Aspergillus niger Aa-20 in submerged and solid-state fermentation: Influence of glucose and tannic acid
    • Aguilar, C.N., C. Augur, E. Favela-Torres and G. Viniegra- González, 2001. Production of tannase by Aspergillus niger Aa-20 in submerged and solid-state fermentation: Influence of glucose and tannic acid. J. Ind. Microbiol. Biotechnol., 26: 296-302.
    • (2001) J. Ind. Microbiol. Biotechnol. , vol.26 , pp. 296-302
    • Aguilar, C.N.1    Augur, C.2    Favela-Torres, E.3    Viniegra-González, G.4
  • 37
    • 0035886013 scopus 로고    scopus 로고
    • Solid-state fermentation and bioremediation: Development of a continuous process for the production of fungal tannase
    • Van De Lagemaat, J. and D.L. Pyle, 2001. Solid-state fermentation and bioremediation: Development of a continuous process for the production of fungal tannase. Chemical Eng. J., 84: 115-123.
    • (2001) Chemical Eng. J. , vol.84 , pp. 115-123
    • Van De Lagemaat, J.1    Pyle, D.L.2
  • 38
    • 68249095970 scopus 로고
    • Cold water-soluble firebrand
    • U.K. Patent no 2610533
    • Coggon, P., N. Graham and G. Syerson, 1975. Cold water-soluble firebrand. U.K. Patent no 2610533.
    • (1975)
    • Coggon, P.1    Graham, N.2    Syerson, G.3
  • 39
    • 0000642380 scopus 로고
    • Experimental it manufactures of acorn wine by fungal tannase
    • Chae, S. and T. Yu, 1983. Experimental it manufactures of acorn wine by fungal tannase. Hanguk Sipkum Kwahakoechi, 15: 326-332.
    • (1983) Hanguk Sipkum Kwahakoechi , vol.15 , pp. 326-332
    • Chae, S.1    Yu, T.2
  • 40
    • 0000341792 scopus 로고
    • Production of gallic acid from hangup tannin by to strain of A. niger
    • Pourrat H., F. Regerat, A. Pourrat and D. Jean, 1985. Production of gallic acid from hangup tannin by to strain of A. niger. J. Ferment. Technol., 63: 401-403.
    • (1985) J. Ferment. Technol. , vol.63 , pp. 401-403
    • Pourrat, H.1    Regerat, F.2    Pourrat, A.3    Jean, D.4
  • 42
    • 0002696053 scopus 로고
    • Strategies for isolation of potent culture capable of producing tannin acyl hydrolase in higher titres
    • Lekha P., M. Ramakrishna and B. Lonsane, 1993. Strategies for isolation of potent culture capable of producing tannin acyl hydrolase in higher titres. Chem. Mikrobiol.Technol. Lebensmitt., 15: 5-10.
    • (1993) Chem. Mikrobiol.Technol. Lebensmitt. , vol.15 , pp. 5-10
    • Lekha, P.1    Ramakrishna, M.2    Lonsane, B.3
  • 43
    • 0001180472 scopus 로고
    • Interpretation chimique de la couleur des vines rouges
    • Ribereau-Gayon, P., 1973. Interpretation chimique de la couleur des vines rouges. Vitis., 12: 119-142.
    • (1973) Vitis. , vol.12 , pp. 119-142
    • Ribereau-Gayon, P.1
  • 44
    • 0032184349 scopus 로고    scopus 로고
    • Lemon albedo cell walls contain dinstinct populations of pectic hairy regions
    • Schols, H.A., J.M. Ros and A.G.J. Voragen, 1998. Lemon albedo cell walls contain dinstinct populations of pectic hairy regions. Carbohydrate Polymer., 37: 159-166.
    • (1998) Carbohydrate Polymer. , vol.37 , pp. 159-166
    • Schols, H.A.1    Ros, J.M.2    Voragen, A.G.J.3
  • 46
    • 0002271025 scopus 로고    scopus 로고
    • Pectin
    • Dumitriu and Severian, (Eds.). Dekker Publisher, New York
    • Rolin, C., B.U. Nielsen and P.E. Glahn, 1998. Pectin. In: Polysaccharides, Dumitriu and Severian, (Eds.). Dekker Publisher, New York, pp: 377-431.
    • (1998) Polysaccharides , pp. 377-431
    • Rolin, C.1    Nielsen, B.U.2    Glahn, P.E.3
  • 50
    • 0000086821 scopus 로고
    • Pectic enzymes Extraction and clarification of fruit juices and grape musts, citrus fruit juice and wine technology, maceration of vegetables and fruits and in the extraction of olive oil
    • Fogarty, W.M., (Eds.). Applied Science Publishers, London
    • Fogarty, W. and T.C. Kelly, 1983. Pectic enzymes Extraction and clarification of fruit juices and grape musts, citrus fruit juice and wine technology, maceration of vegetables and fruits and in the extraction of olive oil. Microbial enzymes and biotechnology, Fogarty, W.M., (Eds.). Applied Science Publishers, London, pp: 131-182.
    • (1983) Microbial Enzymes and Biotechnology , pp. 131-182
    • Fogarty, W.1    Kelly, T.C.2
  • 51
    • 0027818642 scopus 로고
    • Pectin, pectinase and protopectinase: Production, properties and applications
    • Sakai, T., T. Sakamoto, J. Hallaert and E.J. Vandamme, 1993. Pectin, pectinase and protopectinase: Production, properties and applications. Adv. Applied Microbiol., 39: 213-294.
    • (1993) Adv. Applied Microbiol. , vol.39 , pp. 213-294
    • Sakai, T.1    Sakamoto, T.2    Hallaert, J.3    Vandamme, E.J.4
  • 52
    • 0012608088 scopus 로고
    • Cassava fibrous waste residue: A substitute to wheat bran in solid state fermentation
    • Budiatman, S. and B.K. Lonsane, 1987. Cassava fibrous waste residue: A substitute to wheat bran in solid state fermentation. Biotechnol. Lett., 9: 597-600.
    • (1987) Biotechnol. Lett. , vol.9 , pp. 597-600
    • Budiatman, S.1    Lonsane, B.K.2
  • 53
    • 0028810288 scopus 로고
    • Production and properties of three pectinolytic activites produced by Aspergillus niger by submerged and solid state fermentation
    • Acuña-Argüelles, M., M. Gutierrez-Rojas, G. Viniegra-González and E. Favela-Torres, 1995. Production and properties of three pectinolytic activites produced by Aspergillus niger by submerged and solid state fermentation. Appl. Microbiol. Biotechnology, 43: 808-814.
    • (1995) Appl. Microbiol. Biotechnology , vol.43 , pp. 808-814
    • Acuña-Argüelles, M.1    Gutierrez-Rojas, M.2    Viniegra-González, G.3    Favela-Torres, E.4
  • 55
    • 0023844106 scopus 로고
    • Apple pomace as raw material for pectinases production in solid state culture
    • Hours, R.A., C.E. Voget and R.J. Ertola, 1988. Apple pomace as raw material for pectinases production in solid state culture. Biological Wastes, 23: 221-228.
    • (1988) Biological Wastes , vol.23 , pp. 221-228
    • Hours, R.A.1    Voget, C.E.2    Ertola, R.J.3
  • 56
    • 0023844678 scopus 로고
    • Some factors affecting pectinase production from apple pomace in solid-state cultures
    • Hours, R.A., C.E. Voget and R.J. Ertola, 1988. Some factors affecting pectinase production from apple pomace in solid-state cultures. Biological Wastes., 24: 147-157.
    • (1988) Biological Wastes , vol.24 , pp. 147-157
    • Hours, R.A.1    Voget, C.E.2    Ertola, R.J.3
  • 57
    • 0343683352 scopus 로고    scopus 로고
    • Production of Aspergillus niger pectolytic enzymes by solid state bioprocessing of apple pomace
    • Berovic, M. and H. Ostroversnik, 1997. Production of Aspergillus niger pectolytic enzymes by solid state bioprocessing of apple pomace. J. Biotechnol., 53: 47-53.
    • (1997) J. Biotechnol. , vol.53 , pp. 47-53
    • Berovic, M.1    Ostroversnik, H.2
  • 58
    • 0000518388 scopus 로고
    • Genetic manipulation of Aspergillus niger for increased synthesis of pectinolytic enzymes
    • Couri, S. and A.X. Farias, 1995. Genetic manipulation of Aspergillus niger for increased synthesis of pectinolytic enzymes. Rev. Microbiol., 26: 314-317.
    • (1995) Rev. Microbiol. , vol.26 , pp. 314-317
    • Couri, S.1    Farias, A.X.2
  • 59
    • 0000758827 scopus 로고
    • Production of pectinases by Aspergillus sp. using differently pretreated lemon peel as the carbon source
    • Maldonado, M.C., A. Navarro and D.A.S. Callieri, 1986. Production of pectinases by Aspergillus sp. using differently pretreated lemon peel as the carbon source. Biotechnol. Lett., 8: 501-504.
    • (1986) Biotechnol. Lett. , vol.8 , pp. 501-504
    • Maldonado, M.C.1    Navarro, A.2    Callieri, D.A.S.3
  • 60
    • 0001050214 scopus 로고
    • Pectic enzymes production in solid-state fermentation using citrus pulp pellets by Talaromyces flavus, Tubercularia vulgaris and Penicillium charlessi
    • Siessere V., Said S., 1989. Pectic enzymes production in solid-state fermentation using citrus pulp pellets by Talaromyces flavus, Tubercularia vulgaris and Penicillium charlessi. Biotechnol. Lett., 11: 343-344.
    • (1989) Biotechnol. Lett. , vol.11 , pp. 343-344
    • Siessere, V.1    Said, S.2
  • 61
    • 0026792770 scopus 로고
    • Citrus waste: An alternative substrate for pectinase production in solid-state culture
    • Garzon, C.G. and R.A. Hours, 1992. Citrus waste: An alternative substrate for pectinase production in solid-state culture. Bioresource Technol., 39: 93-95.
    • (1992) Bioresource Technol. , vol.39 , pp. 93-95
    • Garzon, C.G.1    Hours, R.A.2
  • 65
    • 0032948170 scopus 로고    scopus 로고
    • Recovery of pectolytic enzymes produced by solid state culture of Aspergillus niger
    • Castilho, I.R., T.L.M. Alves and R.A. Medronho, 1999. Recovery of pectolytic enzymes produced by solid state culture of Aspergillus niger. Process Biochem., 34: 181-186.
    • (1999) Process Biochem. , vol.34 , pp. 181-186
    • Castilho, I.R.1    Alves, T.L.M.2    Medronho, R.A.3
  • 66
    • 0025405470 scopus 로고
    • Characterization of an endopolygalacturonase produced by solid-state cultures of the aerobic fungus Penicillium capsulatum
    • Gillespie, A.M., K. Cook and M.P. Coughlan, 1990. Characterization of an endopolygalacturonase produced by solid-state cultures of the aerobic fungus Penicillium capsulatum. J. Biotechnol., 13: 279-292.
    • (1990) J. Biotechnol. , vol.13 , pp. 279-292
    • Gillespie, A.M.1    Cook, K.2    Coughlan, M.P.3
  • 67
    • 0016906505 scopus 로고
    • Hemicellulases: Their ocurrence purification, properties and mode of action
    • Dekker, R. and G. Richards, 1976. Hemicellulases: Their ocurrence purification, properties and mode of action. Adv. Carbohydrates Chem. Biochem., 32: 277-352.
    • (1976) Adv. Carbohydrates Chem. Biochem. , vol.32 , pp. 277-352
    • Dekker, R.1    Richards, G.2
  • 68
    • 68249090549 scopus 로고
    • The characterisation of to thermostable endo-1,4 -b -mannanase cloned from Caldocellum saccarolyticus
    • Bug, P., T. Clark, M. Mackie, M. Hugh and R. Daniel, 1991. The characterisation of to thermostable endo-1,4 -b -mannanase cloned from Caldocellum saccarolyticus. Applied Microbiol. Biotechnol., 131: 333-336.
    • (1991) Applied Microbiol. Biotechnol. , vol.131 , pp. 333-336
    • Bug, P.1    Clark, T.2    Mackie, M.3    Hugh, M.4    Daniel, R.5
  • 69
    • 0024377332 scopus 로고
    • Two Bacillus β-mannanases having different COOH termini plow produced in Escherichia coli carring pMAH5
    • Akino, T., C. Kato and K. Horikoshi, 1989. Two Bacillus β-mannanases having different COOH termini plow produced in Escherichia coli carring pMAH5. Applied Environ. Microbiol., 55: 3158-3183.
    • (1989) Applied Environ. Microbiol. , vol.55 , pp. 3158-3183
    • Akino, T.1    Kato, C.2    Horikoshi, K.3
  • 70
    • 0025300045 scopus 로고
    • Mannanase components from Bacillus pulmilus
    • Araujo, A. and O. Ward, 1990. Mannanase components from Bacillus pulmilus. Applied Environ. Microbio., 1954-1956.
    • (1990) Applied Environ. Microbio. , pp. 1954-1956
    • Araujo, A.1    Ward, O.2
  • 71
    • 0025602304 scopus 로고
    • Purification and some properties of the mannanases from Thielavia terrestris
    • Araujo, A. and O. Ward, 1990b. Purification and some properties of the mannanases from Thielavia terrestris. J. Ind. Microbiol, 6: 269-274.
    • (1990) J. Ind. Microbiol , vol.6 , pp. 269-274
    • Araujo, A.1    Ward, O.2
  • 72
    • 0025668755 scopus 로고
    • Production of mannanase by Trichoderma harzanium E58
    • Torrie, J.P. and D.J. Senoir, 1990. Production of mannanase by Trichoderma harzanium E58. Applied Microb. Biotechnol., 34: 303-307.
    • (1990) Applied Microb. Biotechnol. , vol.34 , pp. 303-307
    • Torrie, J.P.1    Senoir, D.J.2
  • 73
    • 84954880038 scopus 로고
    • Purification and some properties of endo-1,4-β-mannanase from Pseudomonas sp. P.T - 5
    • Yamura, Y., T. Matsumoto, M. Funatsu and Y. Funatsu, 1990. Purification and some properties of endo-1,4-β-mannanase from Pseudomonas sp. P.T - 5. Agric. Biol. Chem., 54: 2425-2427.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2425-2427
    • Yamura, Y.1    Matsumoto, T.2    Funatsu, M.3    Funatsu, Y.4
  • 75
    • 0029669431 scopus 로고    scopus 로고
    • Multiple forms of β-mannanase from Bacillus sp. KK01
    • Hossain, M.Z., J. Abe and S. Hizukuri, 1996. Multiple forms of β-mannanase from Bacillus sp. KK01. Enzyme Microb. Technol., 18: 95-98.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 95-98
    • Hossain, M.Z.1    Abe, J.2    Hizukuri, S.3
  • 76
    • 68249099967 scopus 로고    scopus 로고
    • Mananasas production for fermentation between solid of agroindustrial waste with filamentous mushrooms
    • Prado, A., S. Huerta Ochoa, S. Rodríguez and G. Saucedo (Eds.). Editions UAMI., Mexico, DF
    • Venegas, L.M., A. Téllez, C. Regalado, G. Rodríguez and S. Huerta Ochoa, 1999. Mananasas production for fermentation between solid of agroindustrial waste with filamentous mushrooms. In: Advance in purification and application of enzymes in biotechnology, Prado, A., S. Huerta Ochoa, S. Rodríguez and G. Saucedo (Eds.). Editions UAMI., Mexico, DF., pp: 263-285.
    • (1999) Advance in Purification and Application of Enzymes in Biotechnology , pp. 263-285
    • Venegas, L.M.1    Téllez, A.2    Regalado, C.3    Rodríguez, G.4    Huerta Ochoa, S.5
  • 78
    • 0029140981 scopus 로고
    • Phytase production and decrease of phytic acid content in canola meal by Aspergillus carbonarius in solid-state fermentation
    • Al-Asheh and Duvnjak, 1995. Phytase production and decrease of phytic acid content in canola meal by Aspergillus carbonarius in solid-state fermentation. World J. Microbiol. Biotechnol., 11: 228-231.
    • (1995) World J. Microbiol. Biotechnol. , vol.11 , pp. 228-231
    • Al-Asheh1    Duvnjak2
  • 79
    • 0029084052 scopus 로고
    • Effects of phosphate, surfactants and glucose on phytase production and hydrolysis of phytic acid in canola meal by Aspergillus ficuum during solidstate fermentation
    • Ebune, A., S. Al-Asheh and Z. Duvnjak, 1995. Effects of phosphate, surfactants and glucose on phytase production and hydrolysis of phytic acid in canola meal by Aspergillus ficuum during solidstate fermentation. Biores. Technol. 53: 7-12.
    • (1995) Biores. Technol. , vol.53 , pp. 7-12
    • Ebune, A.1    Al-Asheh, S.2    Duvnjak, Z.3
  • 80
    • 84981976048 scopus 로고
    • Xylan degrading enzyme systems: Biochemistry, molecular biology and applications
    • Coughlan, M.P. and G.P. Hazlewood, 1993. Xylan degrading enzyme systems: Biochemistry, molecular biology and applications. Biotechnol. Applied Biochem., 17: 259-289.
    • (1993) Biotechnol. Applied Biochem. , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 82
    • 0032524829 scopus 로고    scopus 로고
    • Bleach boosting effect of cellulose-free xylanases of Streptomyces thermoviolaceus and its comparison with two commercial enzyme preparations on birchwood karf pulp
    • Garg, A., J.C. Roberts and A.J. Mccarthy, 1998. Bleach boosting effect of cellulose-free xylanases of Streptomyces thermoviolaceus and its comparison with two commercial enzyme preparations on birchwood karf pulp. Enzyme Microb. Technol., 27: 594-598.
    • (1998) Enzyme Microb. Technol. , vol.27 , pp. 594-598
    • Garg, A.1    Roberts, J.C.2    Mccarthy, A.J.3
  • 84
    • 0030026181 scopus 로고    scopus 로고
    • Development of cellulase-free xylanase-producing anaerobic consortia for the uses of lignocellulolytic wastes
    • Rani, S. and K. Nand, 1996. Development of cellulase-free xylanase-producing anaerobic consortia for the uses of lignocellulolytic wastes. Enzyme. Micrb. Technol., 18: 23-28.
    • (1996) Enzyme. Micrb. Technol. , vol.18 , pp. 23-28
    • Rani, S.1    Nand, K.2
  • 85
    • 0030002331 scopus 로고    scopus 로고
    • Purification and characterization of two different xylanases from thermophilic actinomycete Microtetraspora flexuosa SIIX
    • Berens S., Kaspari H., Klemme J.H., 1996. Purification and characterization of two different xylanases from thermophilic actinomycete Microtetraspora flexuosa SIIX. Antonie Goes Leeuwenhoek, 69: 235-241.
    • (1996) Antonie Goes Leeuwenhoek , vol.69 , pp. 235-241
    • Berens, S.1    Kaspari, H.2    Klemme, J.H.3
  • 86
    • 0031209630 scopus 로고    scopus 로고
    • Purification and characterization of xylanases from Trichoderma
    • Gerber, P.J., J.A. Heitmann and T.W. Joyce, 1997. Purification and characterization of xylanases from Trichoderma. Biores. Technol., 61: 127-140.
    • (1997) Biores. Technol. , vol.61 , pp. 127-140
    • Gerber, P.J.1    Heitmann, J.A.2    Joyce, T.W.3
  • 87
    • 0032997851 scopus 로고    scopus 로고
    • Pectinase production by to diploid construct from two Aspergillus niger overproducing mutants: Isolation, mapping and biochemical characterization
    • Loera, O., J. Aguirre and G. Viniegra-González, 1999. Pectinase production by to diploid construct from two Aspergillus niger overproducing mutants: Isolation, mapping and biochemical characterization. Enzyme. Microbiol. Technol., 25: 103-108.
    • (1999) Enzyme. Microbiol. Technol. , vol.25 , pp. 103-108
    • Loera, O.1    Aguirre, J.2    Viniegra-González, G.3
  • 88
    • 0020410219 scopus 로고
    • Comparative biochemistry of the proteinases of eukariotic microorganisms
    • North, M.J., 1982. Comparative biochemistry of the proteinases of eukariotic microorganisms: Microbiol. Rev., 46: 308-340.
    • (1982) Microbiol. Rev. , vol.46 , pp. 308-340
    • North, M.J.1
  • 90
  • 91
    • 0001571153 scopus 로고
    • The diversity of proteolytic enzymes
    • Beynon, R.J. and J.S. Bond (Eds.). IRL Press, Oxford
    • Neurath, H., 1994. The diversity of proteolytic enzymes. In: Proteolytic enzymes a practical approach, Beynon, R.J. and J.S. Bond (Eds.). IRL Press, Oxford, pp: 1-12.
    • (1994) Proteolytic Enzymes a Practical Approach , pp. 1-12
    • Neurath, H.1
  • 92
    • 0033572187 scopus 로고    scopus 로고
    • Research review paper: Microbial alkaline proteases: From a bioindustrial viewpoint
    • Ganesh, K.C. and H. Takagi, 1999. Research review paper: Microbial alkaline proteases: From a bioindustrial viewpoint. Biotechnol. Adv., 17: 561-594.
    • (1999) Biotechnol. Adv. , vol.17 , pp. 561-594
    • Ganesh, K.C.1    Takagi, H.2
  • 94
    • 3543028083 scopus 로고
    • Proteinases and their inhibitors in biotechnology. Enzymes in biomass conversion
    • Fox, J.W., J.D. Shannon and J.B. Bjarnason, 1991. Proteinases and their inhibitors in biotechnology. Enzymes in biomass conversion. ACS Symp. Sr., 46: 62-79.
    • (1991) ACS Symp. Sr. , vol.46 , pp. 62-79
    • Fox, J.W.1    Shannon, J.D.2    Bjarnason, J.B.3
  • 95
    • 0026692792 scopus 로고
    • Synthesis and release of proteases by Bacteroides fragilis
    • Macfarlane, G., S. Macfarlane and G.R. Gibson, 1992. Synthesis and release of proteases by Bacteroides fragilis. Curr. Microbiol., 24: 55-59.
    • (1992) Curr. Microbiol. , vol.24 , pp. 55-59
    • Macfarlane, G.1    Macfarlane, S.2    Gibson, G.R.3
  • 96
    • 0025741201 scopus 로고
    • Production of alkaline protease with Bacillus licheniformis in a controlled fed-batch process
    • Bierbaum, G., 1991. Production of alkaline protease with Bacillus licheniformis in a controlled fed-batch process. Applied Microbiol. Biotechnol., 35: 720-724.
    • (1991) Applied Microbiol. Biotechnol. , vol.35 , pp. 720-724
    • Bierbaum, G.1
  • 97
    • 0026928538 scopus 로고
    • Production and degradation of alkaline proteases in batch cultures of Bacillus subtilis ATCC 14416
    • Chu, I.M., C. Lee and T.S. Li, 1992. Production and degradation of alkaline proteases in batch cultures of Bacillus subtilis ATCC 14416. Enzyme Microbiol. Technol., 14: 755-761.
    • (1992) Enzyme Microbiol. Technol. , vol.14 , pp. 755-761
    • Chu, I.M.1    Lee, C.2    Li, T.S.3
  • 98
    • 0030907606 scopus 로고    scopus 로고
    • Production of alkaline protease by an alkaliphilic cacteria isolated from an alkaline soda lake
    • Gessesse, A. and B. Gashe, 1997. Production of alkaline protease by an alkaliphilic cacteria isolated from an alkaline soda lake. Biotechnol. Lett., 19: 479-481.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 479-481
    • Gessesse, A.1    Gashe, B.2
  • 99
    • 0025118164 scopus 로고
    • Production of alkaline protease by Bacillus licheniformis in an aqueous two-phase systems
    • Lee, Y. and H. Chang, 1990. Production of alkaline protease by Bacillus licheniformis in an aqueous two-phase systems. J. Ferment. Bioeng., 69: 89-92.
    • (1990) J. Ferment. Bioeng. , vol.69 , pp. 89-92
    • Lee, Y.1    Chang, H.2
  • 100
    • 0030298055 scopus 로고    scopus 로고
    • Simultaneous Online Monitoring of Glucose and Total Malto Sugar in Fermentation Processes Using an FIA System
    • Umoh, E., 1996. Simultaneous Online Monitoring of Glucose and Total Malto Sugar in Fermentation Processes Using an FIA System J. Chem. Technol. Biotechnol., 67: 276-280.
    • (1996) J. Chem. Technol. Biotechnol. , vol.67 , pp. 276-280
    • Umoh, E.1
  • 101
    • 0027536550 scopus 로고
    • Comparison of fungal protease production by submerged and surface cultivation
    • DOI 10.1016/0168-1656(93)90097-7
    • Ramamurthy, V. and R.M. Kothari, 1993. Comparison of fungal protease production by submerged and surface cultivation. J. Biotechnol., 27: 349-354. (Pubitemid 23051678)
    • (1993) Journal of Biotechnology , vol.27 , Issue.3 , pp. 349-354
    • Ramamurthy, V.1    Kothari, R.M.2
  • 102
    • 0027391904 scopus 로고
    • High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): Enzyme production and compatibility with commercial detergents
    • Phadatare, S.U., M.C. Sroinivasan and V.V. Desphande, 1993. High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): Enzyme production and compatibility with commercial detergents. Enzyme. Microbiol. Technol., 15: 72-76.
    • (1993) Enzyme. Microbiol. Technol. , vol.15 , pp. 72-76
    • Phadatare, S.U.1    Sroinivasan, M.C.2    Desphande, V.V.3
  • 103
    • 0029239715 scopus 로고
    • Thermoestability of high activity alkaline protease from Conidiabolus coronatus (NCL 86.8.20)
    • Boshale S.H., M.B. Rao, V.V. Deshpanade and M.C. Srinivasan, 1995. Thermoestability of high activity alkaline protease from Conidiabolus coronatus (NCL 86.8.20). Enzyme Microbiol. Technol., 17: 136-139.
    • (1995) Enzyme Microbiol. Technol. , vol.17 , pp. 136-139
    • Boshale, S.H.1    Rao, M.B.2    Deshpanade, V.V.3    Srinivasan, M.C.4
  • 104
    • 0014724907 scopus 로고
    • The isolation and partial characterization of an acid protease produced by Mucor miehei
    • Ottsen, M. and W. Rickert, 1970. The isolation and partial characterization of an acid protease produced by Mucor miehei. Comp. Rend. Trav. Lab. Carlsberg., 37: 301-325.
    • (1970) Comp. Rend. Trav. Lab. Carlsberg. , vol.37 , pp. 301-325
    • Ottsen, M.1    Rickert, W.2
  • 105
    • 0028007673 scopus 로고
    • Protease production by Rhizopus oligosporus in solid-state fermentation
    • Ikasari, L.m and D.A. Mitchell, 1994. Protease production by Rhizopus oligosporus in solid-state fermentation. World . J. Microbiol. Biotechnol., 10: 320-324.
    • (1994) World. J. Microbiol. Biotechnol. , vol.10 , pp. 320-324
    • Ikasari, L.M.1    Mitchell, D.A.2
  • 106
    • 0025801075 scopus 로고
    • Production of alkaline protease by a new Asperguillus flavus isolated under solid-substrate fermentation conditions for use as a depilation agent
    • Malathi, S. and R. Chakraborty, 1991. Production of alkaline protease by a new Asperguillus flavus isolated under solid-substrate fermentation conditions for use as a depilation agent. Applied Environ. Microbiol., 57: 712-716.
    • (1991) Applied Environ. Microbiol. , vol.57 , pp. 712-716
    • Malathi, S.1    Chakraborty, R.2
  • 107
    • 0025766566 scopus 로고
    • Culture requirements for the production of protease by Aspergillus oryzae in solid state fermentation
    • Battaglino, R.A., M. Huergo, A.M. Pilosof and G.B. Bartholomai, 1991. Culture requirements for the production of protease by Aspergillus oryzae in solid state fermentation. Applied Microbiol. Biotechnol., 35: 292-296.
    • (1991) Applied Microbiol. Biotechnol. , vol.35 , pp. 292-296
    • Battaglino, R.A.1    Huergo, M.2    Pilosof, A.M.3    Bartholomai, G.B.4
  • 108
    • 0024591675 scopus 로고
    • Continuous protease production in a carbon-limited chemostat culture by salt tolerant Aspergillus oryzae
    • Fukushima, Y., H. Itoh, T. Fukase and H. Motai, 1989. Continuous protease production in a corbon-limited chemostat culture by salt tolerant Aspergillus oryzae. Applied Microbiol. Biotechnol., 30: 604-608. (Pubitemid 19133099)
    • (1989) Applied Microbiology and Biotechnology , vol.30 , Issue.6 , pp. 604-608
    • Fukushima, Y.1    Itoh, H.2    Fukase, T.3    Motai, H.4
  • 109
    • 0026073713 scopus 로고
    • Stimulation of protease production by Aspergillus oryzae with oils in continuous culture
    • Fukushima, Y., H. Itoh, T. Fukase and H. Motai, 1991. Stimulation of protease production by Aspergillus oryzae with oils in continuous culture. Applied Microbiol. Biotechnol., 34: 586-590.
    • (1991) Applied Microbiol. Biotechnol. , vol.34 , pp. 586-590
    • Fukushima, Y.1    Itoh, H.2    Fukase, T.3    Motai, H.4
  • 110
    • 0031680522 scopus 로고    scopus 로고
    • Optimizing some factors affecting protease production under solid state fermentation
    • DOI 10.1007/s004490050504
    • Tunga, R., R. Banerjee and B.C. Bhattacharyya, 1998. Optimizing some factors affecting protease production under solid state fermentation. Bioprocess Eng., 19: 187-190. (Pubitemid 28430353)
    • (1998) Bioprocess Engineering , vol.19 , Issue.3 , pp. 187-190
    • Tunga, R.1    Banerjee, R.2    Bhattacharyya, B.C.3
  • 111
    • 0033022339 scopus 로고    scopus 로고
    • Some studies on optimization of extraction process for protease production in SSF
    • DOI 10.1007/s004490050619
    • Tunga, R., R. Banerjee and B.C. Bhattacharyya, 1999a. Some studies on optimization of extraction process for protease production in SSF. Bioprocess Eng., 20: 485-489. (Pubitemid 29282444)
    • (1999) Bioprocess Engineering , vol.20 , Issue.6 , pp. 485-489
    • Tunga, R.1    Banerjee, R.2    Bhattacharya, B.C.3
  • 112
    • 0032769390 scopus 로고    scopus 로고
    • Studies of some physical parameters for large scale protease production by SSF
    • Tunga R., R. Banerjee and B.C. Bhattacharyya, 1999b. Studies of some physical parameters for large scale protease production by SSF. Bioprocess Eng., 21: 187-190.
    • (1999) Bioprocess Eng. , vol.21 , pp. 187-190
    • Tunga, R.1    Banerjee, R.2    Bhattacharyya, B.C.3
  • 113
    • 0027145016 scopus 로고
    • Potential of Asperguillus Oryzae CFTRI 1480 for producing proteinase in high titers by solid state fermentation
    • Padmanabhan, S., M.V. Ramana Murthy and B. Lonsane, 1993. Potential of Asperguillus Oryzae CFTRI 1480 for producing proteinase in high titers by solid state fermentation. Applied Microbiol. Biotechnol., 40: 308-340.
    • (1993) Applied Microbiol. Biotechnol. , vol.40 , pp. 308-340
    • Padmanabhan, S.1    Ramana Murthy, M.V.2    Lonsane, B.3
  • 114
    • 0030808167 scopus 로고
    • Adaptation of proteases and carbohydrates of saprophytic and entomopahogenic fungi to the requirements of the ecological niches
    • St. Leguer, R., L. Joshi and D. Roberts, 1994. Adaptation of proteases and carbohydrates of saprophytic and entomopahogenic fungi to the requirements of the ecological niches. Microbiology, 143: 1983-1992.
    • (1994) Microbiology , vol.143 , pp. 1983-1992
    • St Leguer, R.1    Joshi, L.2    Roberts, D.3
  • 115
    • 0026590357 scopus 로고
    • Extracellular alkaline protease of a newly isolated Rhizopus oryzae
    • Banerjee, R. and B.C. Bhattacharyya, 1992. Extracellular alkaline protease of a newly isolated Rhizopus oryzae. Biotechnol. Lett., 14: 301-304.
    • (1992) Biotechnol. Lett. , vol.14 , pp. 301-304
    • Banerjee, R.1    Bhattacharyya, B.C.2
  • 116
    • 0026509852 scopus 로고
    • Collagenolytic activity of a new semi-alkaline protease from Aspergillus niger
    • Barthomeuf, C., H. Pourrat and A. Pourrat, 1992. Collagenolytic activity of a new semi-alkaline protease from Aspergillus niger. J. Ferment. Bioeng., 73: 233-266.
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 233-266
    • Barthomeuf, C.1    Pourrat, H.2    Pourrat, A.3
  • 117
    • 0027141061 scopus 로고
    • Purification of alkaline protease of Rhizopus oryzae by foam fractionation
    • Banerjee, R., R. Agnihotri and B.C. Bhattacharyya, 1993. Purification of alkaline protease of Rhizopus oryzae by foam fractionation. Bioprocess. Eng., 9: 245-248.
    • (1993) Bioprocess. Eng. , vol.9 , pp. 245-248
    • Banerjee, R.1    Agnihotri, R.2    Bhattacharyya, B.C.3
  • 119
    • 0025847569 scopus 로고
    • Isolation and characterization of an extracellular alkaline protease of Aspergillus fumigatus
    • Monod, M., G. Togni, L. Rahalison and E. Frenk, 1991. Isolation and characterization of an extracellular alkaline protease of Aspergillus fumigatus. J. Medical. Microbiol., 35: 23-28
    • (1991) J. Medical. Microbiol. , vol.35 , pp. 23-28
    • Monod, M.1    Togni, G.2    Rahalison, L.3    Frenk, E.4
  • 120
    • 0026251941 scopus 로고
    • Isolation and characterization of the alkaline protease gene of Aspergillus oryzae
    • Murakami, K., Y. Ishida, A. Masaki and H. Tatsumi, 1991. Isolation and characterization of the alkaline protease gene of Aspergillus oryzae. Agric. Biol. Chem., 55: 807-2811.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 807-2811
    • Murakami, K.1    Ishida, Y.2    Masaki, A.3    Tatsumi, H.4
  • 121
    • 33645846965 scopus 로고
    • Effect of the composition of conidial inoculum development agar media on promoting production of proteinase by Aspergillus oryzae CFTRI 1480 in solid state fermentation system
    • Murthy, M.V.R. and B.K. Lonsane, 1993. Effect of the composition of conidial inoculum development agar media on promoting production of proteinase by Aspergillus oryzae CFTRI 1480 in solid state fermentation system. Chem. Mikrobiol. Technol. Lebensm., 15: 179-184.
    • (1993) Chem. Mikrobiol. Technol. Lebensm. , vol.15 , pp. 179-184
    • Murthy, M.V.R.1    Lonsane, B.K.2
  • 122
    • 0017251475 scopus 로고
    • Production, purification and characterization of thermomycolase, the extracellular serine protease from thermophilic fungus Malbranchea pulchella var. sulfurea
    • Ong, P.S. and M. Gaucher, 1976. Production, purification and characterization of thermomycolase, the extracellular serine protease from thermophilic fungus Malbranchea pulchella var. sulfurea. Can. J. Microbiol., 22: 165-176.
    • (1976) Can. J. Microbiol. , vol.22 , pp. 165-176
    • Ong, P.S.1    Gaucher, M.2
  • 123
    • 85047679803 scopus 로고    scopus 로고
    • Repeated batch production of alkaline protease by solid-state fermentation using urethane foam as carriers
    • DOI 10.1007/s004490050184
    • Osawa, S., K. Sato and I. Endo, 1996. Repeated batch production of alkaline protease by solidsatate fermentation using urethane foam as carriers. Bioprocess Eng., 14: 63-68. (Pubitemid 26032519)
    • (1996) Bioprocess Engineering , vol.14 , Issue.2 , pp. 63-68
    • Ozawa, S.1    Sato, K.2    Endo, I.3
  • 124
    • 0025253167 scopus 로고
    • Production of fungal rennet by Mucor miehei using solid state fermentation
    • Thakur, M.S., N.G. Karanth and K. Nand, 1990. Production of fungal rennet by Mucor miehei using solid state fermentation. Applied Microbiol. Biotechnol., 32: 409-413.
    • (1990) Applied Microbiol. Biotechnol. , vol.32 , pp. 409-413
    • Thakur, M.S.1    Karanth, N.G.2    Nand, K.3


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