메뉴 건너뛰기




Volumn 36, Issue 6, 2013, Pages 737-747

Partial purification of saccharifying and cell wall-hydrolyzing enzymes from malt in waste from beer fermentation broth

Author keywords

Bioethanol; Cell matrix; Cell wall hydrolyzing enzymes; Cell free enzyme system; Waste from beer fermentation broth

Indexed keywords

BEER FERMENTATIONS; BIO-ETHANOL PRODUCTION; CARBOXY-METHYL CELLULOSE; CELL MATRIX; ENZYME SYSTEMS; SACCHARIFICATION ENZYMES; SIMULTANEOUS SACCHARIFICATION AND FERMENTATION; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 84878751173     PISSN: 16157591     EISSN: 16157605     Source Type: Journal    
DOI: 10.1007/s00449-013-0899-1     Document Type: Article
Times cited : (8)

References (60)
  • 1
    • 84869020456 scopus 로고    scopus 로고
    • Prospects of reusable endogenous hydrolyzing enzymes in bioethanol production by simultaneous saccharification and fermentation
    • 10.1007/s11814-012-0174-1 1:CAS:528:DC%2BC38Xhs1artL7L
    • Khattak WA, Ul-Islam M, Park JK (2012) Prospects of reusable endogenous hydrolyzing enzymes in bioethanol production by simultaneous saccharification and fermentation. Korean J Chem Eng 29(11):1467-1482
    • (2012) Korean J Chem Eng , vol.29 , Issue.11 , pp. 1467-1482
    • Khattak, W.A.1    Ul-Islam, M.2    Park, J.K.3
  • 2
    • 79960603147 scopus 로고    scopus 로고
    • Potential of the waste from beer fermentation broth for bio-ethanol production without any additional enzyme, microbial cells and carbohydrates
    • 10.1016/j.enzmictec.2011.04.016 1:CAS:528:DC%2BC3MXptlChtLo%3D
    • Ha JH, Shah N, Ul-Islam M, Park JK (2011) Potential of the waste from beer fermentation broth for bio-ethanol production without any additional enzyme, microbial cells and carbohydrates. Enzyme Microb Tech 49:298-304
    • (2011) Enzyme Microb Tech , vol.49 , pp. 298-304
    • Ha, J.H.1    Shah, N.2    Ul-Islam, M.3    Park, J.K.4
  • 3
    • 77951517765 scopus 로고    scopus 로고
    • Production of bacterial cellulose in static conditions by a simple fed-batch cultivation strategy
    • 10.1007/s11814-009-0232-5
    • Shehzad O, Khan S, Khan T, Park JK (2009) Production of bacterial cellulose in static conditions by a simple fed-batch cultivation strategy. Korean J Chem Eng 26:1689-1992
    • (2009) Korean J Chem Eng , vol.26 , pp. 1689-1992
    • Shehzad, O.1    Khan, S.2    Khan, T.3    Park, J.K.4
  • 4
    • 35148867450 scopus 로고    scopus 로고
    • Production of glucuronan oligosaccharides using the waste of beer fermentation broth as a basal medium
    • 10.1016/j.enzmictec.2007.08.007 1:CAS:528:DC%2BD2sXhtFGrtb3E
    • Khan T, Hyun SH, Park JK (2007) Production of glucuronan oligosaccharides using the waste of beer fermentation broth as a basal medium. Enzyme Microb Technol 42:89-92
    • (2007) Enzyme Microb Technol , vol.42 , pp. 89-92
    • Khan, T.1    Hyun, S.H.2    Park, J.K.3
  • 5
    • 84865811730 scopus 로고    scopus 로고
    • Evaluation of sediments of the waste from beer fermentation broth for bioethanol production
    • 10.1007/s11814-011-0293-0 1:CAS:528:DC%2BC38Xht12qtr7M
    • Ha JH, Gang MK, Khan T, Park JK (2012) Evaluation of sediments of the waste from beer fermentation broth for bioethanol production. Korean J Chem Eng 29:1224-1231
    • (2012) Korean J Chem Eng , vol.29 , pp. 1224-1231
    • Ha, J.H.1    Gang, M.K.2    Khan, T.3    Park, J.K.4
  • 6
    • 35148825192 scopus 로고    scopus 로고
    • Production of bacterial cellulose using waste of beer fermentation broth
    • 1:CAS:528:DC%2BD28XktVeqsbc%3D
    • Park JK, Hyun SH, Ahn WS (2006) Production of bacterial cellulose using waste of beer fermentation broth. Korean Chem Eng Res 44:52-57
    • (2006) Korean Chem Eng Res , vol.44 , pp. 52-57
    • Park, J.K.1    Hyun, S.H.2    Ahn, W.S.3
  • 7
    • 0001634864 scopus 로고
    • Fungal cellulases
    • C.H. Haigler (eds) et al. Macel Dekker Inc. New York
    • Wood TM (1991) Fungal cellulases. In: Haigler CH et al (eds) Biosynthesis and biodegradation of cellulose. Macel Dekker Inc., New York
    • (1991) Biosynthesis and Biodegradation of Cellulose
    • Wood, T.M.1
  • 8
    • 78650747030 scopus 로고    scopus 로고
    • Bioethanol production from optimized pretreatment of cassava stem
    • 10.1007/s11814-010-0330-4 1:CAS:528:DC%2BC3MXjslOhsb8%3D
    • Han M, Kim Y, Kim Y, Chung B, Choi GW (2011) Bioethanol production from optimized pretreatment of cassava stem. Korean J Chem Eng 28:119-125
    • (2011) Korean J Chem Eng , vol.28 , pp. 119-125
    • Han, M.1    Kim, Y.2    Kim, Y.3    Chung, B.4    Choi, G.W.5
  • 9
    • 0031830365 scopus 로고    scopus 로고
    • Cell wall architecture in yeast: New structure and new challenges
    • 1:CAS:528:DyaK1cXlt1Chs7k%3D
    • Lipke PN, Ovalle R (1998) Cell wall architecture in yeast: new structure and new challenges. J Bacteriol 180:3735-3740
    • (1998) J Bacteriol , vol.180 , pp. 3735-3740
    • Lipke, P.N.1    Ovalle, R.2
  • 10
    • 3042527880 scopus 로고    scopus 로고
    • Simultaneous saccharification and fermentation (SSF) of industrial wastes for the production of ethanol
    • 10.1016/j.indcrop.2003.12.015
    • Kádár Z, Szengyel Z, Réczey K (2004) Simultaneous saccharification and fermentation (SSF) of industrial wastes for the production of ethanol. Ind Crop Prod 20:103-110
    • (2004) Ind Crop Prod , vol.20 , pp. 103-110
    • Kádár, Z.1    Szengyel, Z.2    Réczey, K.3
  • 11
    • 0008883965 scopus 로고    scopus 로고
    • Fundamentals of immobilized yeast cells for continuous beer fermentation: A review
    • 10.1002/j.2050-0416.1998.tb00970.x
    • Pilkington PH, Margaritis A, Mensour NA, Russell I (1998) Fundamentals of immobilized yeast cells for continuous beer fermentation: a review. J Inst Brew 104:19-31
    • (1998) J Inst Brew , vol.104 , pp. 19-31
    • Pilkington, P.H.1    Margaritis, A.2    Mensour, N.A.3    Russell, I.4
  • 13
    • 84979145496 scopus 로고
    • Alkoholische Gährung ohne Hefezellen
    • 10.1002/cber.189703001215 1:CAS:528:DyaD28Xpt1Gguw%3D%3D
    • Buchner E (1897) Alkoholische Gährung ohne Hefezellen. Ber Dtsch Chem Ges 30(117-124):1110-1113
    • (1897) Ber Dtsch Chem Ges , vol.30 , Issue.117-124 , pp. 1110-1113
    • Buchner, E.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0012093419 scopus 로고
    • Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings
    • 10.1016/S0008-6215(00)90394-X 1:CAS:528:DyaL28XhvVahsL4%3D
    • Hatfield R, Nevins DJ (1986) Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings. Carbohyd Res 148:265-278
    • (1986) Carbohyd Res , vol.148 , pp. 265-278
    • Hatfield, R.1    Nevins, D.J.2
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 18
    • 0016177685 scopus 로고
    • Enzymatic hydrolysis of waste cellulose
    • 10.1002/bit.260161105 1:CAS:528:DyaE2MXmtVajsA%3D%3D
    • Mandels M, Hontz L, Nystrom J (1974) Enzymatic hydrolysis of waste cellulose. Biotechnol Bioeng 16:1471-1493
    • (1974) Biotechnol Bioeng , vol.16 , pp. 1471-1493
    • Mandels, M.1    Hontz, L.2    Nystrom, J.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 7:248-254
    • (1976) Anal Biochem , vol.7 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 70749158906 scopus 로고    scopus 로고
    • Current perspectives on the role of enzymes in brewing
    • 10.1016/j.jcs.2009.03.001 1:CAS:528:DC%2BD1MXhsFahu7vO
    • Bamforth CW (2009) Current perspectives on the role of enzymes in brewing. J Cereal Sci 50:353-357
    • (2009) J Cereal Sci , vol.50 , pp. 353-357
    • Bamforth, C.W.1
  • 21
    • 0020023025 scopus 로고
    • Purification and chemical properties of two β-glucan endohydrolases from germinating barley
    • 10.1111/j.1432-1033.1982.tb05837.x 1:CAS:528:DyaL38XpvFyqsA%3D%3D
    • Woodward JR, Fincher GB (1982) Purification and chemical properties of two β-glucan endohydrolases from germinating barley. Eur J Biochem 121:663-669
    • (1982) Eur J Biochem , vol.121 , pp. 663-669
    • Woodward, J.R.1    Fincher, G.B.2
  • 23
    • 43249111023 scopus 로고    scopus 로고
    • Characterization of purified xylanase from finger millet (Eleusine coracana-Indaf 15) malt
    • 10.1007/s00217-007-0760-3 1:CAS:528:DC%2BD1cXlsVClur4%3D
    • Chithra M, Muralikrishna G (2008) Characterization of purified xylanase from finger millet (Eleusine coracana-Indaf 15) malt. Eur Food Res Technol 227:587-597
    • (2008) Eur Food Res Technol , vol.227 , pp. 587-597
    • Chithra, M.1    Muralikrishna, G.2
  • 24
    • 84979448010 scopus 로고
    • A role for carboxypeptidase in the solubilization of barley β-glucan
    • 10.1002/j.2050-0416.1979.tb03937.x 1:CAS:528:DyaL3cXkt1CgtL0%3D
    • Bamforth CW, Martin HL, Wainwright T (1979) A role for carboxypeptidase in the solubilization of barley β-glucan. J Inst Brew 85:334-338
    • (1979) J Inst Brew , vol.85 , pp. 334-338
    • Bamforth, C.W.1    Martin, H.L.2    Wainwright, T.3
  • 25
    • 16744362660 scopus 로고
    • Primary structure of carboxypeptidase III from malted barley
    • 10.1007/BF02904473
    • Sørensen SB, Svendsen I, Breddam K (1989) Primary structure of carboxypeptidase III from malted barley. Carlsberg Res Commun 54:193-202
    • (1989) Carlsberg Res Commun , vol.54 , pp. 193-202
    • Sørensen, S.B.1    Svendsen, I.2    Breddam, K.3
  • 26
    • 0040020893 scopus 로고
    • α-Amylase, limit dextrinase and α-glucosidase enzymes in barley and malt
    • 10.3109/07388558709086972 1:CAS:528:DyaL2sXhslCmtb0%3D
    • MacGregor AW (1987) α-Amylase, limit dextrinase and α-glucosidase enzymes in barley and malt. CRC CR Rev Biotechnol 5:117-128
    • (1987) CRC CR Rev Biotechnol , vol.5 , pp. 117-128
    • MacGregor, A.W.1
  • 27
    • 79959610982 scopus 로고    scopus 로고
    • Cell wall polysaccharides hydrolysis of malting barley (Hordeum vulgare L.): A review
    • Jamar C, du Jardin P, Fauconnier ML (2011) Cell wall polysaccharides hydrolysis of malting barley (Hordeum vulgare L.): a review. Biotechnol Agron Soc Environ 15:301-313
    • (2011) Biotechnol Agron Soc Environ , vol.15 , pp. 301-313
    • Jamar, C.1    Du Jardin, P.2    Fauconnier, M.L.3
  • 28
    • 0031829114 scopus 로고    scopus 로고
    • Detection of enzymes active on various β-1,3-glucans after denaturing polyacrylamide gel electrophoresis
    • 10.1002/elps.1150191041 1:CAS:528:DyaK1cXlvVKktrs%3D
    • Trudel J, Grenier J, Asselin A (1998) Detection of enzymes active on various β-1,3-glucans after denaturing polyacrylamide gel electrophoresis. Electrophoresis 19:1788-1792
    • (1998) Electrophoresis , vol.19 , pp. 1788-1792
    • Trudel, J.1    Grenier, J.2    Asselin, A.3
  • 29
    • 24344477426 scopus 로고    scopus 로고
    • Thermal stability of alpha-amylase from malted jowar (Sorghum bicolor)
    • 10.1021/jf0501701 1:CAS:528:DC%2BD2MXmvFWjurc%3D
    • Kumar RS, Singh SA, Rao AG (2005) Thermal stability of alpha-amylase from malted jowar (Sorghum bicolor). J Agric Food Chem 53:6883-6888
    • (2005) J Agric Food Chem , vol.53 , pp. 6883-6888
    • Kumar, R.S.1    Singh, S.A.2    Rao, A.G.3
  • 30
    • 79952984265 scopus 로고    scopus 로고
    • Amylase modiWcation induced by the germination process in organic barley
    • 10.1007/s00217-011-1423-y 1:CAS:528:DC%2BC3MXjsFaitbY%3D
    • Acquistucci R, Turfani V, Aureli G (2011) Amylase modiWcation induced by the germination process in organic barley. Eur Food Res Technol 232:583-590
    • (2011) Eur Food Res Technol , vol.232 , pp. 583-590
    • Acquistucci, R.1    Turfani, V.2    Aureli, G.3
  • 31
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley
    • 10.1104/pp.119.3.859 1:CAS:528:DyaK1MXhvFymtb8%3D
    • Burton RA, Zhang XQ, Hrmova M, Fincher GB (1999) A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol 119:859-871
    • (1999) Plant Physiol , vol.119 , pp. 859-871
    • Burton, R.A.1    Zhang, X.Q.2    Hrmova, M.3    Fincher, G.B.4
  • 32
    • 0000023298 scopus 로고
    • A major gibberellic acid-induced barley aleurone cysteine proteinase which digests hordein
    • 10.1104/pp.94.1.251 1:CAS:528:DyaK3cXmt1Krtr4%3D
    • Koehler SM, Ho THD (1990) A major gibberellic acid-induced barley aleurone cysteine proteinase which digests hordein. Plant Physiol 94:251-258
    • (1990) Plant Physiol , vol.94 , pp. 251-258
    • Koehler, S.M.1    Ho, T.H.D.2
  • 33
    • 0001014396 scopus 로고
    • Purification and partial characterization of barley leucine aminopeptidase
    • 10.1104/pp.55.5.809 1:CAS:528:DyaE2MXkt1CisL0%3D
    • Sopanen T, Mikola J (1975) Purification and partial characterization of barley leucine aminopeptidase. Plant Physiol 55:809-814
    • (1975) Plant Physiol , vol.55 , pp. 809-814
    • Sopanen, T.1    Mikola, J.2
  • 34
    • 26244444477 scopus 로고    scopus 로고
    • The endogenous endoproteinase inhibitors of barley and malt and their roles in malting and brewing
    • 10.1016/j.jcs.2005.06.002 1:CAS:528:DC%2BD2MXhtVyms7zE
    • Jones BL (2005) The endogenous endoproteinase inhibitors of barley and malt and their roles in malting and brewing. J Cereal Sci 42:271-280
    • (2005) J Cereal Sci , vol.42 , pp. 271-280
    • Jones, B.L.1
  • 35
    • 0026815874 scopus 로고
    • Structure and expression of the barley lipid transfer protein gene Ltp 1
    • 10.1007/BF00040674 1:CAS:528:DyaK3sXhvVKjtro%3D
    • Skriver K, Leah R, Mulleruri F, Olsen FL, Mundy J (1992) Structure and expression of the barley lipid transfer protein gene Ltp 1. Plant Mol Biol 18:585-589
    • (1992) Plant Mol Biol , vol.18 , pp. 585-589
    • Skriver, K.1    Leah, R.2    Mulleruri, F.3    Olsen, F.L.4    Mundy, J.5
  • 36
    • 84979405346 scopus 로고
    • Recognition of two lipases from barley and green malt
    • 10.1002/j.2050-0416.1984.tb04273.x 1:CAS:528:DyaL2cXlsV2ks7o%3D
    • Baxter ED (1984) Recognition of two lipases from barley and green malt. J Inst Brew 90:277-281
    • (1984) J Inst Brew , vol.90 , pp. 277-281
    • Baxter, E.D.1
  • 39
    • 0031493703 scopus 로고    scopus 로고
    • Changes in the cationic isoenzymesof peroxidase during the malting of barley. I. Tissue location studies
    • 10.1002/j.2050-0416.1997.tb00949.x 1:CAS:528:DyaK2sXlsVeksr8%3D
    • Antrobus CJ, Large PJ, Bamforth CW (1997) Changes in the cationic isoenzymesof peroxidase during the malting of barley. I. Tissue location studies. J Inst Brewing 103:227-231
    • (1997) J Inst Brewing , vol.103 , pp. 227-231
    • Antrobus, C.J.1    Large, P.J.2    Bamforth, C.W.3
  • 40
    • 84892440916 scopus 로고    scopus 로고
    • http://www.natureclean.com/bacteria-enzymes.htm
  • 41
    • 0031394778 scopus 로고    scopus 로고
    • Purification and characterization of an endoglucanase from the marine rotifer, Brachionus plicatilis
    • 1:CAS:528:DyaK2sXnt1Ghs7k%3D
    • Chun CZ, Hur SB, Kim YT (1997) Purification and characterization of an endoglucanase from the marine rotifer, Brachionus plicatilis. Biochem Mol Biol Int 43:241-249
    • (1997) Biochem Mol Biol Int , vol.43 , pp. 241-249
    • Chun, C.Z.1    Hur, S.B.2    Kim, Y.T.3
  • 42
    • 79953090633 scopus 로고    scopus 로고
    • Evaluation of operational parameters on the precipitation of endoglucanase and xylanase produced by solid state fermentation of Aspergillus niger
    • 10.1590/S0104-66322011000100003 1:CAS:528:DC%2BC3MXkt1Cns74%3D
    • Farinas CS, Scarpelini LM, Miranda EA, Neto VB (2011) Evaluation of operational parameters on the precipitation of endoglucanase and xylanase produced by solid state fermentation of Aspergillus niger. Braz J Chem Eng 28:17-26
    • (2011) Braz J Chem Eng , vol.28 , pp. 17-26
    • Farinas, C.S.1    Scarpelini, L.M.2    Miranda, E.A.3    Neto, V.B.4
  • 43
    • 84055187898 scopus 로고    scopus 로고
    • Fermentative production of endoglucanse - Kinetics and modeling
    • Kavitha S, Nagarajan P (2011) Fermentative production of endoglucanse - kinetics and modeling. Int J Eng Sci Tech 3:1894-1898
    • (2011) Int J Eng Sci Tech , vol.3 , pp. 1894-1898
    • Kavitha, S.1    Nagarajan, P.2
  • 44
    • 77952589691 scopus 로고    scopus 로고
    • Purification and properties of endoglucanase from a sugar cane bagasse hydrolyzing strain, Aspergillus glaucus XC9
    • 10.1021/jf1003896 1:CAS:528:DC%2BC3cXltVymur4%3D
    • Tao YM, Zhu XZ, Huang JZ, Ma SJ, Wu XB, Long MN, Chen QX (2010) Purification and properties of endoglucanase from a sugar cane bagasse hydrolyzing strain, Aspergillus glaucus XC9. J Agric Food Chem 58:6126-6130
    • (2010) J Agric Food Chem , vol.58 , pp. 6126-6130
    • Tao, Y.M.1    Zhu, X.Z.2    Huang, J.Z.3    Ma, S.J.4    Wu, X.B.5    Long, M.N.6    Chen, Q.X.7
  • 45
    • 84878761775 scopus 로고
    • Purification of cellulase from Trichoderma viride and properties of its component enzymes
    • 1:CAS:528:DyaK2MXhvVyltbg%3D
    • Kim DW, Kim TS (1994) Purification of cellulase from Trichoderma viride and properties of its component enzymes. Bull Korean Chem Soc 15:719-724
    • (1994) Bull Korean Chem Soc , vol.15 , pp. 719-724
    • Kim, D.W.1    Kim, T.S.2
  • 46
    • 34848921744 scopus 로고    scopus 로고
    • Purification and characterization of a new endoglucanase from Aspergillus aculeatus
    • 10.1021/jf070710p
    • Gajendra SN, Kaul P, Prakash V (2007) Purification and characterization of a new endoglucanase from Aspergillus aculeatus. J Agric Food Chem 55:7566-7572
    • (2007) J Agric Food Chem , vol.55 , pp. 7566-7572
    • Gajendra, S.N.1    Kaul, P.2    Prakash, V.3
  • 47
    • 18244370777 scopus 로고    scopus 로고
    • Identification of over producer strain of endo-β-1,4-glucanase in Aspergillus species: Characterization of crude carboxymethyl cellulose
    • 1:CAS:528:DC%2BD2MXivFygurs%3D
    • Onsori H, Zamani MR, Motallebi M, Zarghami N (2005) Identification of over producer strain of endo-β-1,4-glucanase in Aspergillus species: characterization of crude carboxymethyl cellulose. African J Biotechnol 4:26-30
    • (2005) African J Biotechnol , vol.4 , pp. 26-30
    • Onsori, H.1    Zamani, M.R.2    Motallebi, M.3    Zarghami, N.4
  • 49
    • 56249140989 scopus 로고    scopus 로고
    • Production and partial purification of cellulase by Aspergillus niger and A. fumigatus fermented in coir waste and sawdust
    • Immanuel G, Bhagavath CMA, Raj PI, Esakkiraj P, Palavesam A (2007) Production and partial purification of cellulase by Aspergillus niger and A. fumigatus fermented in coir waste and sawdust. Int J Microbiol 3:1-20
    • (2007) Int J Microbiol , vol.3 , pp. 1-20
    • Immanuel, G.1    Bhagavath, C.M.A.2    Raj, P.I.3    Esakkiraj, P.4    Palavesam, A.5
  • 50
    • 0034877077 scopus 로고    scopus 로고
    • Polysaccharide hydrolases from Boscia senegalensis: Purification and characterization of endo-1,3-beta-glucanase
    • 10.1385/ABAB:94:3:225 1:CAS:528:DC%2BD3MXmsFyrt74%3D
    • Dicko MH, Leeuwen MJFSV, Traore AS, Hilhorst R, Beldman G (2001) Polysaccharide hydrolases from Boscia senegalensis: purification and characterization of endo-1,3-beta-glucanase. Appl Biochem Biotech 94:225-241
    • (2001) Appl Biochem Biotech , vol.94 , pp. 225-241
    • Dicko, M.H.1    Leeuwen, M.2    Traore, A.S.3    Hilhorst, R.4    Beldman, G.5
  • 51
    • 0036728274 scopus 로고    scopus 로고
    • The genomics of yeast responses to environmental stress and starvation
    • 10.1007/s10142-002-0058-2 1:CAS:528:DC%2BD38Xnt1elsLs%3D
    • Gasch AP, Werner-Washburne M (2002) The genomics of yeast responses to environmental stress and starvation. Funct Integr Genomics 2:181-192
    • (2002) Funct Integr Genomics , vol.2 , pp. 181-192
    • Gasch, A.P.1    Werner-Washburne, M.2
  • 53
    • 0031057735 scopus 로고    scopus 로고
    • Membrane fatty acid composition and membrane fluidity as parameters of stress tolerance in yeast
    • 10.1139/m97-010 1:CAS:528:DyaK2sXhtVKltbs%3D
    • Swan TM, Watson K (1997) Membrane fatty acid composition and membrane fluidity as parameters of stress tolerance in yeast. Can J Microbiol 43:70-77
    • (1997) Can J Microbiol , vol.43 , pp. 70-77
    • Swan, T.M.1    Watson, K.2
  • 54
    • 64049092699 scopus 로고    scopus 로고
    • Slow growth induces heat-shock resistance in normal and respiratory-deficient yeast
    • 10.1091/mbc.E08-08-0852 1:CAS:528:DC%2BD1MXisVSnsLY%3D
    • Lu C, Brauer MJ, Botstein D (2009) Slow growth induces heat-shock resistance in normal and respiratory-deficient yeast. Mol Biol Cell 20:891-903
    • (2009) Mol Biol Cell , vol.20 , pp. 891-903
    • Lu, C.1    Brauer, M.J.2    Botstein, D.3
  • 55
    • 0032423438 scopus 로고    scopus 로고
    • Review: Ethanol production at elevated temperatures and alcohol concentrations: Part I-yeasts in general
    • 10.1023/A:1008802704374 1:CAS:528:DyaK1MXhvVGntLk%3D
    • Banat IM, Nigam P, Singh D, Marchant R, McHale AP (1998) Review: ethanol production at elevated temperatures and alcohol concentrations: part I-yeasts in general. World J Microbiol Biotechnol 14:809-821
    • (1998) World J Microbiol Biotechnol , vol.14 , pp. 809-821
    • Banat, I.M.1    Nigam, P.2    Singh, D.3    Marchant, R.4    McHale, A.P.5
  • 56
    • 0029268667 scopus 로고
    • The phylogenetic position of the pterobranch Hemichordates based on 18S rDNA sequence data
    • 10.1006/mpev.1995.1007 1:CAS:528:DyaK2MXlvFCltr4%3D
    • Halanych KM (1995) The phylogenetic position of the pterobranch Hemichordates based on 18S rDNA sequence data. Mol Phylogenet Evol 4:72-76
    • (1995) Mol Phylogenet Evol , vol.4 , pp. 72-76
    • Halanych, K.M.1
  • 57
    • 31344479544 scopus 로고    scopus 로고
    • Ethanol fermentation from biomass resources: Current state and prospects
    • 10.1007/s00253-005-0229-x 1:CAS:528:DC%2BD28XmtlOhtA%3D%3D
    • Lin Y, Tanaka S (2006) Ethanol fermentation from biomass resources: current state and prospects. Appl Microbiol Biotechnol 69:627-642
    • (2006) Appl Microbiol Biotechnol , vol.69 , pp. 627-642
    • Lin, Y.1    Tanaka, S.2
  • 58
    • 0032882779 scopus 로고    scopus 로고
    • Solid-substrate fermentation of soybeans with Rhizopus spp.: Comparison of discontinuous rotation with stationery bed fermentation
    • 10.1016/S1389-1723(99)80203-5 1:CAS:528:DyaK1MXmvFeqs78%3D
    • Han B, Kiers JL, Nout RM (1999) Solid-substrate fermentation of soybeans with Rhizopus spp.: comparison of discontinuous rotation with stationery bed fermentation. J Biosci Bioeng 88:205-209
    • (1999) J Biosci Bioeng , vol.88 , pp. 205-209
    • Han, B.1    Kiers, J.L.2    Nout, R.M.3
  • 60
    • 33847657398 scopus 로고    scopus 로고
    • Perspective Cell-free ethanol production: The future of fuel ethanol?
    • 10.1002/jctb.1649 1:CAS:528:DC%2BD2sXis1yrtrw%3D
    • Allain EJ (2007) Perspective Cell-free ethanol production: the future of fuel ethanol? Chem Technol Biotechnol 82:117-120
    • (2007) Chem Technol Biotechnol , vol.82 , pp. 117-120
    • Allain, E.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.