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Volumn 60, Issue 2, 2015, Pages 193-202

Production of amylases from Bacillus amyloliquefaciens under submerged fermentation using some agro-industrial by-products

Author keywords

Amylases activity; Bacillus amyloliquefaciens; Growth parameters; Starchy substrates; Submerged fermentation

Indexed keywords


EID: 85010655703     PISSN: 05701783     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.aoas.2015.06.001     Document Type: Article
Times cited : (113)

References (52)
  • 1
    • 84869482446 scopus 로고    scopus 로고
    • A potential new isolate for the production of a thermostable extracellular α-amylase
    • Alkando, A.A., Ibrahim, H.M., A potential new isolate for the production of a thermostable extracellular α-amylase. J. Bacteriol. Res. 3 (2011), 129–137.
    • (2011) J. Bacteriol. Res. , vol.3 , pp. 129-137
    • Alkando, A.A.1    Ibrahim, H.M.2
  • 2
    • 33745843330 scopus 로고    scopus 로고
    • Alpha amylase production by Bacillus cereus MTCC 1305 using solid-state fermentation
    • Anto, H., Trivedi, U., Patel, K., Alpha amylase production by Bacillus cereus MTCC 1305 using solid-state fermentation. Food Technol. Biotechnol. 44 (2006), 241–245.
    • (2006) Food Technol. Biotechnol. , vol.44 , pp. 241-245
    • Anto, H.1    Trivedi, U.2    Patel, K.3
  • 3
    • 33750157980 scopus 로고    scopus 로고
    • A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing
    • Asgher, M., Asad, M.J., Rahman, S.U., Legge, R.L., A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing. IJFE 79 (2007), 950–955.
    • (2007) IJFE , vol.79 , pp. 950-955
    • Asgher, M.1    Asad, M.J.2    Rahman, S.U.3    Legge, R.L.4
  • 4
    • 80054056475 scopus 로고    scopus 로고
    • Assay of population density of amylase producing bacteria from different soil samples contaminated with flowing effluents
    • Bahadure, R.B., Agnihotri, U.S., Akarte, S.R., Assay of population density of amylase producing bacteria from different soil samples contaminated with flowing effluents. Int. J. Parasitol. Res. 2 (2010), 09–13.
    • (2010) Int. J. Parasitol. Res. , vol.2 , pp. 09-13
    • Bahadure, R.B.1    Agnihotri, U.S.2    Akarte, S.R.3
  • 5
    • 40749093717 scopus 로고    scopus 로고
    • Production of α-amylase from Penicillium chrysogenum under solid state fermentation by using some agriculture by product
    • Balkan, B., Figen, E., Production of α-amylase from Penicillium chrysogenum under solid state fermentation by using some agriculture by product. Food Technol. Biotechnol. 44 (2007), 439–442.
    • (2007) Food Technol. Biotechnol. , vol.44 , pp. 439-442
    • Balkan, B.1    Figen, E.2
  • 6
    • 0041655017 scopus 로고    scopus 로고
    • Solid state fermentation for production of α-amylase by a thermotolerant Bacillus subtilis from hot-spring water
    • Baysal, Z., Uyar, F., Aytekin, C., Solid state fermentation for production of α-amylase by a thermotolerant Bacillus subtilis from hot-spring water. Proc. Biochem. 38 (2003), 1665–1668.
    • (2003) Proc. Biochem. , vol.38 , pp. 1665-1668
    • Baysal, Z.1    Uyar, F.2    Aytekin, C.3
  • 7
    • 78649966240 scopus 로고    scopus 로고
    • Production and properties of the highly efficient raw starch digesting α-amylase from a Bacillus licheniformis ATCC 9945a
    • Božić, N., Ruiz, J., López-Santín, J., Vujčić, Z., Production and properties of the highly efficient raw starch digesting α-amylase from a Bacillus licheniformis ATCC 9945a. Biochem. Eng. J. 53 (2011), 203–209.
    • (2011) Biochem. Eng. J. , vol.53 , pp. 203-209
    • Božić, N.1    Ruiz, J.2    López-Santín, J.3    Vujčić, Z.4
  • 8
    • 0142058329 scopus 로고    scopus 로고
    • Glucoamylase, α-amylase and β-amylase immobilization on acrylic carriers
    • Bryjak, J., Glucoamylase, α-amylase and β-amylase immobilization on acrylic carriers. Biochem. Eng. J. 16 (2003), 347–355.
    • (2003) Biochem. Eng. J. , vol.16 , pp. 347-355
    • Bryjak, J.1
  • 9
    • 22644444228 scopus 로고
    • Applied Microbiology
    • International Book Company New York
    • Clark, H.E., Bordner, G.E.F., Kabler, P.W., Huff, C.B., Applied Microbiology. 1958, International Book Company, New York pp. 27–53.
    • (1958) , pp. 27-53
    • Clark, H.E.1    Bordner, G.E.F.2    Kabler, P.W.3    Huff, C.B.4
  • 11
    • 27144471699 scopus 로고    scopus 로고
    • Application of a statistical design to the optimization of culture medium for α-amylase production by Aspergillus niger ATCC 16404 grown on orange waste powder
    • Djekrif-Dakhmouche, S., Gheribi-Aoulmi, Z., Meraihi, Z., Bennamoun, L., Application of a statistical design to the optimization of culture medium for α-amylase production by Aspergillus niger ATCC 16404 grown on orange waste powder. J. Food Eng. 73 (2006), 190–197.
    • (2006) J. Food Eng. , vol.73 , pp. 190-197
    • Djekrif-Dakhmouche, S.1    Gheribi-Aoulmi, Z.2    Meraihi, Z.3    Bennamoun, L.4
  • 12
    • 0003780199 scopus 로고
    • Bacterial Metabolism
    • second ed. Academic Press New York p. 738
    • Doelle, H.W., Bacterial Metabolism. second ed., 1975, Academic Press, New York p. 738.
    • (1975)
    • Doelle, H.W.1
  • 13
    • 0000130569 scopus 로고
    • Multiple range and multiple F test
    • Duncan, D.B., Multiple range and multiple F test. Biometrics 11 (1955), 1–42.
    • (1955) Biometrics , vol.11 , pp. 1-42
    • Duncan, D.B.1
  • 14
    • 34547468145 scopus 로고    scopus 로고
    • Bioprocess development for the production of alpha amylase by Bacillus amyloliquefaciens in batch and fed-batch cultures
    • Enhasy, H.A.E., Bioprocess development for the production of alpha amylase by Bacillus amyloliquefaciens in batch and fed-batch cultures. Res. J. Microb. 2 (2007), 560–568.
    • (2007) Res. J. Microb. , vol.2 , pp. 560-568
    • Enhasy, H.A.E.1
  • 15
    • 79960528286 scopus 로고    scopus 로고
    • Simultaneous production of raw starch degrading highly thermostable α-amylase and lactic acid by Lactobacillus fermentum 04BBA19
    • Fossi, B.T., Tavea, F., Jiwoua, C., Ndjouenkeu, R., Simultaneous production of raw starch degrading highly thermostable α-amylase and lactic acid by Lactobacillus fermentum 04BBA19. Afr. J. Biotechnol. 10 (2011), 6564–6574.
    • (2011) Afr. J. Biotechnol. , vol.10 , pp. 6564-6574
    • Fossi, B.T.1    Tavea, F.2    Jiwoua, C.3    Ndjouenkeu, R.4
  • 16
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline protease: molecular approaches and industrial applications
    • Gupta, R., Beg, Q.K., Lorenz, P., Bacterial alkaline protease: 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.K.2    Lorenz, P.3
  • 17
    • 0037332979 scopus 로고    scopus 로고
    • Production of alpha amylase by Bacillus licheniformis using an economical medium
    • Haq, I., Ashraf, H., Iqbal, J., Qadeer, M.A., Production of alpha amylase by Bacillus licheniformis using an economical medium. J. Biores. Technol. 87 (2003), 57–61.
    • (2003) J. Biores. Technol. , vol.87 , pp. 57-61
    • Haq, I.1    Ashraf, H.2    Iqbal, J.3    Qadeer, M.A.4
  • 18
    • 15944385267 scopus 로고    scopus 로고
    • Pearl millet, a source of alpha amylase production by Bacillus licheniformis
    • Haq, I., Ashraf, H., Qadeer, M.A., Iqbal, J., Pearl millet, a source of alpha amylase production by Bacillus licheniformis. J. Biores. Technol. 96 (2005), 1201–1204.
    • (2005) J. Biores. Technol. , vol.96 , pp. 1201-1204
    • Haq, I.1    Ashraf, H.2    Qadeer, M.A.3    Iqbal, J.4
  • 19
    • 85024367976 scopus 로고    scopus 로고
    • Version 19.0, SPSS Inc., Chicago, Illinois.
    • IBM® SPSS® Statistics, 2011. Version 19.0, SPSS Inc., Chicago, Illinois.
    • (2011)
    • IBM® SPSS® Statistics1
  • 21
    • 1842610730 scopus 로고    scopus 로고
    • Biorefinery – systems
    • Kamm, B., Kamm, M., Biorefinery – systems. Chem. Biochem. Eng. 18 (2004), 1–6.
    • (2004) Chem. Biochem. Eng. , vol.18 , pp. 1-6
    • Kamm, B.1    Kamm, M.2
  • 22
    • 84937439449 scopus 로고    scopus 로고
    • Optimization and production of α -amylase from halophilic Bacillus species isolated from mangrove soil sources
    • Kanimozhi, M., Johny, M., Gayathri, N., Subashkumar, R., Optimization and production of α -amylase from halophilic Bacillus species isolated from mangrove soil sources. J. Appl. Environ. Microb. 3 (2014), 70–73.
    • (2014) J. Appl. Environ. Microb. , vol.3 , pp. 70-73
    • Kanimozhi, M.1    Johny, M.2    Gayathri, N.3    Subashkumar, R.4
  • 23
    • 85024386650 scopus 로고    scopus 로고
    • Production of amylase enzyme by isolated microorganisms and its application
    • Karnwal, A., Nigam, V., Production of amylase enzyme by isolated microorganisms and its application. IJPBS 3 (2013), 354–360.
    • (2013) IJPBS , vol.3 , pp. 354-360
    • Karnwal, A.1    Nigam, V.2
  • 24
    • 79953906323 scopus 로고    scopus 로고
    • Screening and isolation of thermostable α-amylase producing bacteria and optimization of physico-chemical parameters for increasing the yield
    • Kumarai, B.L., SaiRam, C.V.S., Kumar, T.S., Sudhakar, P., Vijetha, P., Screening and isolation of thermostable α-amylase producing bacteria and optimization of physico-chemical parameters for increasing the yield. Int. J. Pharm. Technol. 3 (2011), 1570–1583.
    • (2011) Int. J. Pharm. Technol. , vol.3 , pp. 1570-1583
    • Kumarai, B.L.1    SaiRam, C.V.S.2    Kumar, T.S.3    Sudhakar, P.4    Vijetha, P.5
  • 25
    • 27644531875 scopus 로고    scopus 로고
    • Amylase production in solid state fermentation by the thermophilic fungus Thermomyces funginosus
    • Kunamneni, A., Permaul, K., Singh, S., Amylase production in solid state fermentation by the thermophilic fungus Thermomyces funginosus. J. Biosci. Bioeng. 100 (2005), 168–171.
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 168-171
    • Kunamneni, A.1    Permaul, K.2    Singh, S.3
  • 26
    • 0004294399 scopus 로고    scopus 로고
    • Brock Biology of Microorganisms
    • thirteenth ed. Prentice Hall
    • Madigan, M.T., Martinko, J.M., Stahl, D.A., Clarck, D.P., Brock Biology of Microorganisms. thirteenth ed., 2011, Prentice Hall pp. 642–656.
    • (2011) , pp. 642-656
    • Madigan, M.T.1    Martinko, J.M.2    Stahl, D.A.3    Clarck, D.P.4
  • 27
    • 52949093513 scopus 로고    scopus 로고
    • Amylase activity of a starch degrading bacteria isolated from soil receiving kitchen wastes
    • Mishra, S., Behera, N., Amylase activity of a starch degrading bacteria isolated from soil receiving kitchen wastes. Afr. J. Biotechnol. 7 (2008), 3326–3331.
    • (2008) Afr. J. Biotechnol. , vol.7 , pp. 3326-3331
    • Mishra, S.1    Behera, N.2
  • 28
    • 1642283662 scopus 로고    scopus 로고
    • A thermostable maltose-tolerant α-amylase from Aspergillus tamari
    • Moreira, F.G., Lenartovicz, V.L., Peralta, R.M., A thermostable maltose-tolerant α-amylase from Aspergillus tamari. J. Basic Microbiol. 44 (2004), 29–35.
    • (2004) J. Basic Microbiol. , vol.44 , pp. 29-35
    • Moreira, F.G.1    Lenartovicz, V.L.2    Peralta, R.M.3
  • 29
    • 84856157367 scopus 로고    scopus 로고
    • Screening of various raw starches on production of thermostable amylopullulanase by Clostridium thermosulfurogenes SVM17
    • Mrudula, S., Reddy, G., Seenayya, G., Screening of various raw starches on production of thermostable amylopullulanase by Clostridium thermosulfurogenes SVM17. J. Appl. Sci. 15 (2011), 996–1001.
    • (2011) J. Appl. Sci. , vol.15 , pp. 996-1001
    • Mrudula, S.1    Reddy, G.2    Seenayya, G.3
  • 30
    • 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 DM03 in solid-state fermentation and exploration of feasibility for inclusion of α-amylase in laundry detergent formulations
    • Mukherjee, A.K., Borah, M., Rai, S.K., To study the influence of different components of fermentable substrates on induction of extracellular α-amylase synthesis by Bacillus subtilis DM03 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
  • 31
    • 49749105587 scopus 로고    scopus 로고
    • Purification and characterization of five alkaline, thermotolerant, and maltotetraose-producing α-amylases from Bacillus halodurans MS-2-5, and production of recombinant enzymes in Escherichia coli
    • Murakami, S., Nagasaki, K., Nishimoto, H., Shigematu, R., Umesakia, J., Takenaka, S., Kaulpiboon, J., Prousoontorn, M., Limpaseni, T., Pongsawasdi, P., Aoki, K., Purification and characterization of five alkaline, thermotolerant, and maltotetraose-producing α-amylases from Bacillus halodurans MS-2-5, and production of recombinant enzymes in Escherichia coli. Enzyme Microb. Technol. 43 (2008), 321–328.
    • (2008) Enzyme Microb. Technol. , vol.43 , pp. 321-328
    • Murakami, S.1    Nagasaki, K.2    Nishimoto, H.3    Shigematu, R.4    Umesakia, J.5    Takenaka, S.6    Kaulpiboon, J.7    Prousoontorn, M.8    Limpaseni, T.9    Pongsawasdi, P.10    Aoki, K.11
  • 32
    • 18244408263 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20
    • Najafi, M.F., Deobagka, D., Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20. Protein Expr. Purif. 41 (2005), 349–354.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 349-354
    • Najafi, M.F.1    Deobagka, D.2
  • 33
    • 77956574369 scopus 로고    scopus 로고
    • Genus Bacillus
    • D.V. Paul M.G. George J. Dorothy R.K. Noel L. Wolfgang A.R. Fred S. Karl-Heinz B.W. William Springer New York
    • Niall, A.L., Paul, D.V., Genus Bacillus. Paul, D.V., George, M.G., Dorothy, J., Noel, R.K., Wolfgang, L., Fred, A.R., Karl-Heinz, S., William, B.W., (eds.) Bergey's Manual of Systematic Bacteriology, second ed., vol. 3, 2009, Springer, New York, 21–128.
    • (2009) Bergey's Manual of Systematic Bacteriology, second ed. , vol.3 , pp. 21-128
    • Niall, A.L.1    Paul, D.V.2
  • 34
    • 77958496541 scopus 로고    scopus 로고
    • Genetic diversity and community of endophytic actinomycetes within the roots of Aquilaria crassna Pierre ex Lec assessed by Actinomycetes-specific PCR and PCR-DGGE of 16S rRNA gene
    • Nimnoi, P., Pongsilp, N., Lumyong, S., Genetic diversity and community of endophytic actinomycetes within the roots of Aquilaria crassna Pierre ex Lec assessed by Actinomycetes-specific PCR and PCR-DGGE of 16S rRNA gene. Biochem. Syst. Ecol. 38 (2010), 595–601.
    • (2010) Biochem. Syst. Ecol. , vol.38 , pp. 595-601
    • Nimnoi, P.1    Pongsilp, N.2    Lumyong, S.3
  • 35
    • 84878034124 scopus 로고    scopus 로고
    • Isolation and characterization of a thermophilic Bacillus sp. with protease activity isolated from hot spring of Tarabalo, Odisha. India
    • Panda, M.K., Sahu, M.K., Tayung, K., Isolation and characterization of a thermophilic Bacillus sp. with protease activity isolated from hot spring of Tarabalo, Odisha. India. I.J.M. 5 (2013), 159–165.
    • (2013) I.J.M. , vol.5 , pp. 159-165
    • Panda, M.K.1    Sahu, M.K.2    Tayung, K.3
  • 36
    • 84966017382 scopus 로고    scopus 로고
    • Extracellular alpha amylase of Aspergillus niger
    • Pfueller, S.L., Elliot, W.H., Extracellular alpha amylase of Aspergillus niger. J. Biol. Chem. 244 (1999), 48–54.
    • (1999) J. Biol. Chem. , vol.244 , pp. 48-54
    • Pfueller, S.L.1    Elliot, W.H.2
  • 37
    • 73449117206 scopus 로고    scopus 로고
    • L-asparaginase production and molecular identification of marine Streptomyces sp. strain EPD 27
    • Poorani, E., Saseetharan, M., Dhevagi, P., L-asparaginase production and molecular identification of marine Streptomyces sp. strain EPD 27. Int. J. Integr. Biol. 7 (2009), 150–155.
    • (2009) Int. J. Integr. Biol. , vol.7 , pp. 150-155
    • Poorani, E.1    Saseetharan, M.2    Dhevagi, P.3
  • 38
    • 84897953488 scopus 로고    scopus 로고
    • Bacterial diversity of biofilm samples from deep mines in South Africa
    • Raji, A.I., Möller, C., Litthauer, D., van Heerden, E., Piater, L.A., Bacterial diversity of biofilm samples from deep mines in South Africa. Biokemist 20 (2008), 53–62.
    • (2008) Biokemist , vol.20 , pp. 53-62
    • Raji, A.I.1    Möller, C.2    Litthauer, D.3    van Heerden, E.4    Piater, L.A.5
  • 39
    • 70449126099 scopus 로고    scopus 로고
    • A thermostable α-amylase producing natural variant of Bacillus spp. isolated from soil in Iran
    • Rasooli, I., Astaneh, S.D.A., Borna, H., Barchini, K.A., A thermostable α-amylase producing natural variant of Bacillus spp. isolated from soil in Iran. Am. J. Agric. Biol. Sci. 3 (2008), 591–596.
    • (2008) Am. J. Agric. Biol. Sci. , vol.3 , pp. 591-596
    • Rasooli, I.1    Astaneh, S.D.A.2    Borna, H.3    Barchini, K.A.4
  • 40
    • 2342584768 scopus 로고    scopus 로고
    • Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles
    • Satyanarayana, T., Noorwez, S.M., Kumar, S., Rao, J.L., Ezhilvannan, M., Kaur, P., Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles. Biochem. Soc. Trans. 32 (2004), 276–278.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 276-278
    • Satyanarayana, T.1    Noorwez, S.M.2    Kumar, S.3    Rao, J.L.4    Ezhilvannan, M.5    Kaur, P.6
  • 41
    • 1642338863 scopus 로고    scopus 로고
    • Energy-saving direct ethanol production from low temperature cooked corn starch using a cell-surface engineered yeast strain co-displaying glucoamylase and α-amylase
    • Shigechi, H., Fujita, Y., Koh, J., Ueda, M., Fukuda, H., Kondo, A., Energy-saving direct ethanol production from low temperature cooked corn starch using a cell-surface engineered yeast strain co-displaying glucoamylase and α-amylase. Biochem. Eng. J. 18 (2004), 149–153.
    • (2004) Biochem. Eng. J. , vol.18 , pp. 149-153
    • Shigechi, H.1    Fujita, Y.2    Koh, J.3    Ueda, M.4    Fukuda, H.5    Kondo, A.6
  • 42
    • 33646567460 scopus 로고    scopus 로고
    • Potato peel as a solid state substrate for thermostable α-amylase production by thermophilic Bacillus isolates
    • Shukla, J., Kar, R., Potato peel as a solid state substrate for thermostable α-amylase production by thermophilic Bacillus isolates. J. Microbiol. Biotechnol. 22 (2006), 417–422.
    • (2006) J. Microbiol. Biotechnol. , vol.22 , pp. 417-422
    • Shukla, J.1    Kar, R.2
  • 43
    • 84918795123 scopus 로고    scopus 로고
    • Isolation and partial characterization of amylase producing Bacillus sp. from Soil
    • Singh, P., Rani, A., Isolation and partial characterization of amylase producing Bacillus sp. from Soil. Int. J. Pharm. Technol. Res. 6 (2014), 2064–2069.
    • (2014) Int. J. Pharm. Technol. Res. , vol.6 , pp. 2064-2069
    • Singh, P.1    Rani, A.2
  • 44
    • 33847404478 scopus 로고    scopus 로고
    • Physical and nutritional factors affecting the production of amylase from species of Bacillus isolated from spoiled food waste
    • Sudharhsan, S., Senthilkumar, S., Ranjith, K., Physical and nutritional factors affecting the production of amylase from species of Bacillus isolated from spoiled food waste. Afr. J. Biotechnol. 6 (2007), 430–435.
    • (2007) Afr. J. Biotechnol. , vol.6 , pp. 430-435
    • Sudharhsan, S.1    Senthilkumar, S.2    Ranjith, K.3
  • 45
    • 85037162479 scopus 로고    scopus 로고
    • Application of response surface methodology to the optimization of amylase production by Aspergillus oryzae MTCC 1847
    • Tamilarasan, K., Muthukumaran, C., Kumar, M.D., Application of response surface methodology to the optimization of amylase production by Aspergillus oryzae MTCC 1847. Afr. J. Biotechnol. 11 (2012), 4241–4247.
    • (2012) Afr. J. Biotechnol. , vol.11 , pp. 4241-4247
    • Tamilarasan, K.1    Muthukumaran, C.2    Kumar, M.D.3
  • 46
    • 33847035852 scopus 로고    scopus 로고
    • Isolation and identification of α- amylase producing Bacillus sp. from dhal industry waste
    • Thippeswamy, S., Girigowda, K., Mulimami, H.V., Isolation and identification of α- amylase producing Bacillus sp. from dhal industry waste. Ind. J. Biochem. Biophys. 43 (2006), 295–298.
    • (2006) Ind. J. Biochem. Biophys. , vol.43 , pp. 295-298
    • Thippeswamy, S.1    Girigowda, K.2    Mulimami, H.V.3
  • 48
    • 84888119851 scopus 로고    scopus 로고
    • Isolation and identification of a bacterial strain producing thermostable α- amylase
    • Vaseekaran, S., Balakumar, S., Arasaratnam, V., Isolation and identification of a bacterial strain producing thermostable α- amylase. Trop. Agric. Res. 22 (2010), 1–11.
    • (2010) Trop. Agric. Res. , vol.22 , pp. 1-11
    • Vaseekaran, S.1    Balakumar, S.2    Arasaratnam, V.3
  • 49
    • 20444401525 scopus 로고    scopus 로고
    • Microplate-based carboxymethyl-cellulose assay for endoglucanase activity
    • Xiao, Z.Z., Storms, R., Tsang, A., Microplate-based carboxymethyl-cellulose assay for endoglucanase activity. Anal. Biochem. 342 (2005), 176–178.
    • (2005) Anal. Biochem. , vol.342 , pp. 176-178
    • Xiao, Z.Z.1    Storms, R.2    Tsang, A.3
  • 51
    • 3142642544 scopus 로고    scopus 로고
    • Purification and properties of a maltotriose producing α-amylase from Thermobifida fusca
    • Yang, C.H., Liu, W.H., Purification and properties of a maltotriose producing α-amylase from Thermobifida fusca. Enzyme Microb. Technol. 35 (2004), 254–260.
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 254-260
    • Yang, C.H.1    Liu, W.H.2
  • 52
    • 0023384117 scopus 로고
    • Comparison of α-amylase activities from different assay methods
    • Yoo, Y.J., Hong, J., Hatch, R.T., Comparison of α-amylase activities from different assay methods. Biotechnol. Bioeng. 30 (1987), 147–151.
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 147-151
    • Yoo, Y.J.1    Hong, J.2    Hatch, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.