메뉴 건너뛰기




Volumn 67, Issue 3-4, 2015, Pages 255-266

Production and characterization of raw starch degrading enzyme from a newly isolated thermophilic filamentous bacterium, Laceyella sacchari LP175

Author keywords

Optimization and characterization; Raw starch degrading enzyme; Response surface methodology; Thermophilic filamentous bacterium Laceyella sacchari LP175

Indexed keywords

BACTERIA; ENZYME ACTIVITY; HYDROLYSIS; MALTOSE; SURFACE PROPERTIES; YEAST;

EID: 84924247324     PISSN: 00389056     EISSN: 1521379X     Source Type: Journal    
DOI: 10.1002/star.201400150     Document Type: Article
Times cited : (30)

References (38)
  • 1
    • 77950368090 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a novel SDS and surfactant stable, raw starch digesting, and halophilic a-amylase from a moderately halophilic bacterium
    • Shafiei, M., Ziaee, A. A., Amoozegar, M. A., Purification and biochemical characterization of a novel SDS and surfactant stable, raw starch digesting, and halophilic a-amylase from a moderately halophilic bacterium, Nesterenkonia sp. strain F. Process Biochem. 2010, 45, 694-699.
    • (2010) Nesterenkonia Sp. Strain F Process Biochem. , vol.45 , pp. 694-699
    • Shafiei, M.1    Ziaee, A.A.2    Amoozegar, M.A.3
  • 2
    • 79953034675 scopus 로고    scopus 로고
    • Direct and efficient ethanol production from high-yielding rice using a Saccharomyces cerevisiae strain that express amylases
    • Yamada, R., Yamakawa, S. I., Tanaka, T., Ogino, C., et al., Direct and efficient ethanol production from high-yielding rice using a Saccharomyces cerevisiae strain that express amylases. Enzyme Microb. Technol. 2011, 48, 393-396.
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 393-396
    • Yamada, R.1    Yamakawa, S.I.2    Tanaka, T.3    Ogino, C.4
  • 3
    • 77949308816 scopus 로고    scopus 로고
    • Recent advances in microbial raw starch degrading enzymes
    • Sun, H., Zhao, P., Ge, X., Xia, Y., et al., Recent advances in microbial raw starch degrading enzymes. Appl. Biochem. Biotechnol. 2010, 160, 988-1003.
    • (2010) Appl. Biochem. Biotechnol. , vol.160 , pp. 988-1003
    • Sun, H.1    Zhao, P.2    Ge, X.3    Xia, Y.4
  • 4
    • 77949268947 scopus 로고    scopus 로고
    • Hydrolysis of granular starch at sub-gelatinization temperature using a mixture of amylolytic enzymes
    • Uthumporn, U., Sarker, M. Z. I., Al-Jashamy, K. A., Hydrolysis of granular starch at sub-gelatinization temperature using a mixture of amylolytic enzymes. Food Bioprod. Process. 2010, 88, 47-54.
    • (2010) Food Bioprod. Process. , vol.88 , pp. 47-54
    • Uthumporn, U.1    Sarker, M.Z.I.2    Al-Jashamy, K.A.3
  • 6
    • 84855412218 scopus 로고    scopus 로고
    • Enhanced production of a-amylase from Bacillus subtilis subsp spizizenii in solid state fermentation by response surface methodology and its evaluation in the hydrolysis of rawpotato starch
    • Soni, S. K., Goyal, N., Gupta, J. K., Soni, R., Enhanced production of a-amylase from Bacillus subtilis subsp. spizizenii in solid state fermentation by response surface methodology and its evaluation in the hydrolysis of rawpotato starch. Starch/Stärke 2012, 64, 64-77.
    • (2012) Starch/Stärke , vol.64 , pp. 64-77
    • Soni, S.K.1    Goyal, N.2    Gupta, J.K.3    Soni, R.4
  • 7
    • 84883221241 scopus 로고    scopus 로고
    • Cloning and overexpression of raw starch digesting a-amylase gene from Bacillus subtilis strain AS01a in Escherichia coli and application of the purified recombinant a-amylase (AmyBS-I) in raw starch digestion and baking industry
    • Roy, J. K., Borah, A., Mahanta, C. L., Mukherjee, A. K., Cloning and overexpression of raw starch digesting a-amylase gene from Bacillus subtilis strain AS01a in Escherichia coli and application of the purified recombinant a-amylase (AmyBS-I) in raw starch digestion and baking industry. J. Mol. Catal. B: Enzym. 2013, 97, 118-129.
    • (2013) J. Mol. Catal. B: Enzym. , vol.97 , pp. 118-129
    • Roy, J.K.1    Borah, A.2    Mahanta, C.L.3    Mukherjee, A.K.4
  • 8
    • 84880412920 scopus 로고    scopus 로고
    • Applications of a high maltose forming, thermo-stable a-amylase from an extremely alkalophilic Bacillus licheniformis strain AS08E in food and laundry detergent industries
    • Roy, J. K., Mukherjee, A. K., Applications of a high maltose forming, thermo-stable a-amylase from an extremely alkalophilic Bacillus licheniformis strain AS08E in food and laundry detergent industries. Biochem. Eng. J. 2013, 77, 220-230.
    • (2013) Biochem. Eng. J. , vol.77 , pp. 220-230
    • Roy, J.K.1    Mukherjee, A.K.2
  • 10
    • 77949731591 scopus 로고    scopus 로고
    • Production of alpha amylase from a randomly induced mutant strain of Bacillus amyloliquefaciens and its application as a desizer in textile industry
    • Haq, I.,Ali, S., Javed,M.M., Hameed,U., et al., Production of alpha amylase from a randomly induced mutant strain of Bacillus amyloliquefaciens and its application as a desizer in textile industry. Pak. J. Bot. 2010, 42, 473-484.
    • (2010) Pak. J. Bot. , vol.42 , pp. 473-484
    • Haq, I.1    Ali, S.2    Javed, M.M.3    Hameed, U.4
  • 11
    • 77956806266 scopus 로고    scopus 로고
    • Application ofmicrobial α-amylase in industry-A review
    • de Souza, P. M.,Magalhes, Pde. O., Application ofmicrobial α-amylase in industry-a review.Braz. J.Microbiol. 2010, 41, 850-861.
    • (2010) Braz J. Microbiol. , vol.41 , pp. 850-861
    • De Souza, P.1    Magalhes, M.2    Pde, O.3
  • 12
    • 79960184964 scopus 로고    scopus 로고
    • Rawstarch fermentation to ethanol by an industrial distiller's yeast strain of Saccharomyces cerevisiae expressing glucoamylase and α-amylase genes
    • Kim,H.R., Im,Y.K., Ko,H.M., Chin, J. E., et al., Rawstarch fermentation to ethanol by an industrial distiller's yeast strain of Saccharomyces cerevisiae expressing glucoamylase and α-amylase genes. Biotechnol. Lett. 2011, 33, 1643-1648.
    • (2011) Biotechnol. Lett. , vol.33 , pp. 1643-1648
    • Kim, H.R.1    Im, Y.K.2    Ko, H.M.3    Chin, J.E.4
  • 13
    • 80051670718 scopus 로고    scopus 로고
    • Production of raw cassava starch-degrading enzyme by Penicillium and its use in conversion of raw cassava flour to ethanol
    • Lin, H. J., Xian, L., Zhang, Q. J., Luo, X.M., et al., Production of raw cassava starch-degrading enzyme by Penicillium and its use in conversion of raw cassava flour to ethanol. J. Ind. Microbiol. Biotechnol. 2011, 38, 733-742.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 733-742
    • Lin, H.J.1    Xian, L.2    Zhang, Q.J.3    Luo, X.M.4
  • 14
    • 79952572982 scopus 로고    scopus 로고
    • Glucoamylases: Structural and biotechnological aspects
    • Marín-Navarro, J., Polaina, J., Glucoamylases: structural and biotechnological aspects. Appl. Microbiol. Biotechnol. 2011, 89, 1267-1273.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 1267-1273
    • Marín-Navarro, J.1    Polaina, J.2
  • 15
    • 84871118741 scopus 로고    scopus 로고
    • Raw starch-degrading α-amylase from Bacillus aquimaris MKSC 6.2: Isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme
    • Puspasari, F., Radjasa, O. K., Noer, A. S., Nurachman, Z., et al., Raw starch-degrading α-amylase from Bacillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme. J. Appl. Microbiol. 2013, 114, 108-120.
    • (2013) J. Appl. Microbiol. , vol.114 , pp. 108-120
    • Puspasari, F.1    Radjasa, O.K.2    Noer, A.S.3    Nurachman, Z.4
  • 16
    • 0035821999 scopus 로고    scopus 로고
    • Purification and properties of a novel raw starch degrading-cyclodextrin glycosyltransferase fromKlebsiella pneumoniae AS-22
    • Gawande, B. N., Patkar, A. Y., Purification and properties of a novel raw starch degrading-cyclodextrin glycosyltransferase fromKlebsiella pneumoniae AS-22. EnzymeMicrob. Technol. 2001, 28, 735-743.
    • (2001) EnzymeMicrob. Technol. , vol.28 , pp. 735-743
    • Gawande, B.N.1    Patkar, A.Y.2
  • 17
    • 84879842967 scopus 로고    scopus 로고
    • Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification
    • Nisha, M., Satyanarayana, T., Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification. Appl. Microbiol. Biotechnol. 2012, 97, 6279-6292.
    • (2012) Appl. Microbiol. Biotechnol. , vol.97 , pp. 6279-6292
    • Nisha, M.1    Satyanarayana, T.2
  • 19
    • 3543028109 scopus 로고    scopus 로고
    • Production and starch saccharification by a thermostable and neutral glucoamylase of a thermophilic mould Thermomucorindicae-seudaticae
    • Kaur, P., Satyanarayana, T., Production and starch saccharification by a thermostable and neutral glucoamylase of a thermophilic mould Thermomucorindicae-seudaticae. World J. Microbiol. Biotechnol. 2004, 20, 419-425.
    • (2004) World J. Microbiol. Biotechnol. , vol.20 , pp. 419-425
    • Kaur, P.1    Satyanarayana, T.2
  • 20
    • 25444445001 scopus 로고    scopus 로고
    • A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and its use in the direct hydrolysis of raw potato starch
    • Goyal, N., Gupta, J. K., Soni, S. K., A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and its use in the direct hydrolysis of raw potato starch. Enzyme Microb. Technol. 2005, 37, 723-734.
    • (2005) Enzyme Microb. Technol. , vol.37 , pp. 723-734
    • Goyal, N.1    Gupta, J.K.2    Soni, S.K.3
  • 21
    • 84896473825 scopus 로고    scopus 로고
    • Characterization of poly (L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175
    • Hanphakphoom, S., Maneewong, N., Sukkhum, S., Tokuyama, S., Kitpreechavanich, V., Characterization of poly (L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175. J. Gen. Appl. Microbiol. 2014, 60, 13-22.
    • (2014) J. Gen. Appl. Microbiol. , vol.60 , pp. 13-22
    • Hanphakphoom, S.1    Maneewong, N.2    Sukkhum, S.3    Tokuyama, S.4    Kitpreechavanich, V.5
  • 22
    • 84871622496 scopus 로고    scopus 로고
    • Production of thermostable, Ca+2-independent, maltose producing α-amylase by Streptomyces sp. MSC702 (MTCC 10772) in submerged fermentation using agro-residues as sole carbon source
    • Singh, R., Kapoor, V., Kumar, V., Production of thermostable, Ca+2-independent, maltose producing α-amylase by Streptomyces sp. MSC702 (MTCC 10772) in submerged fermentation using agro-residues as sole carbon source. Ann. Microbiol. 2011, 62, 1003-1012.
    • (2011) Ann. Microbiol. , vol.62 , pp. 1003-1012
    • Singh, R.1    Kapoor, V.2    Kumar, V.3
  • 23
    • 41849144871 scopus 로고    scopus 로고
    • Response surface methodology for the optimization of alpha amylase production by Bacillus amyloliquefaciens
    • Gangadharan, D., Sivaramakrishnan, S., Nampoothiri, K. M., Sukumaran, R. K., Pandey, A., Response surface methodology for the optimization of alpha amylase production by Bacillus amyloliquefaciens. Bioresour. Technol. 2008, 99, 4597-4602.
    • (2008) Bioresour. Technol. , vol.99 , pp. 4597-4602
    • Gangadharan, D.1    Sivaramakrishnan, S.2    Nampoothiri, K.M.3    Sukumaran, R.K.4    Pandey, A.5
  • 24
    • 38949098670 scopus 로고    scopus 로고
    • Optimization of alkaline protease production by batch culture of bacillus sp. RKY3 through plackett-burman and response surface methodological approaches
    • Reddy, L. V.,Wee,Y. J.,Yun, J. S.,Ryu,H.W.,Optimization of alkaline protease production by batch culture of Bacillus sp. RKY3 through Plackett-Burman and response surface methodological approaches. Bioresour. Technol. 2008, 99, 2242-2249.
    • (2008) Bioresour. Technol. , vol.99 , pp. 2242-2249
    • Reddy, L.V.1    Wee, Y.J.2    Yun, J.S.3    Ryu, H.W.4
  • 25
    • 1942438557 scopus 로고    scopus 로고
    • Optimization of medium composition for actinorhodin production by Streptomyces coelicolor A3 (2) with response surface methodology
    • Elibol, M., Optimization of medium composition for actinorhodin production by Streptomyces coelicolor A3 (2) with response surface methodology. Process Biochem. 2004, 39, 1057-1062.
    • (2004) Process Biochem. , vol.39 , pp. 1057-1062
    • Elibol, M.1
  • 26
    • 84986495514 scopus 로고
    • Screening potato starch for novel properties using differential scanning calorimetry
    • Kim, Y. S., Wiesenborn, D. P., Orr, P. H., Grant, L. A., Screening potato starch for novel properties using differential scanning calorimetry. J. Food Sci. 1995, 60, 1060-1065.
    • (1995) J. Food Sci. , vol.60 , pp. 1060-1065
    • Kim, Y.S.1    Wiesenborn, D.P.2    Orr, P.H.3    Grant, L.A.4
  • 27
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • Plackett, R. L., Burman, J. P., The design of optimum multifactorial experiments. Biometrika 1946, 33, 305-325.
    • (1946) Biometrika , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 28
    • 67651122758 scopus 로고    scopus 로고
    • Development of fermentation process for PLA-degrading enzyme production by a new thermophilic Actinomadura sp. T16-1
    • Sukkhum, S., Tokuyama, S., Kitpreechavanich, V., Development of fermentation process for PLA-degrading enzyme production by a new thermophilic Actinomadura sp. T16-1. Biotechnol. Bioprocess Eng. 2009, 14, 302-306.
    • (2009) Biotechnol. Bioprocess Eng. , vol.14 , pp. 302-306
    • Sukkhum, S.1    Tokuyama, S.2    Kitpreechavanich, V.3
  • 29
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver, H., Burk, D., The determination of enzyme dissociation constants. J. Am. Chem. Soc. 1934, 56, 658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 30
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L., Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31, 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 31
    • 84878859204 scopus 로고    scopus 로고
    • Synergistic and antagonistic effects of α-amylase and amyloglucosidase on starch digestion
    • Zhang, B., Dhital, S., Gidley, M. J., Synergistic and antagonistic effects of α-amylase and amyloglucosidase on starch digestion. Biomacromolecules 2013, 14, 1945-1954.
    • (2013) Biomacromolecules , vol.14 , pp. 1945-1954
    • Zhang, B.1    Dhital, S.2    Gidley, M.J.3
  • 32
    • 33645811843 scopus 로고
    • A new method for micro determination of amylase activity by the use of amylose as the substrate
    • Fuwa, H., A new method for micro determination of amylase activity by the use of amylose as the substrate. J. Biochem. 1954, 41, 583-603.
    • (1954) J. Biochem. , vol.41 , pp. 583-603
    • Fuwa, H.1
  • 33
    • 66149164727 scopus 로고    scopus 로고
    • Comparison of glucose/xylose cofermentation of poplar hydrolysates processed by different pretreatment technologies
    • Lu, Y., Warner, R., Sedlak, M., Ho, N., Mosier, N. S., Comparison of glucose/xylose cofermentation of poplar hydrolysates processed by different pretreatment technologies. Biotechnol. Prog. 2009, 25, 349-356.
    • (2009) Biotechnol. Prog. , vol.25 , pp. 349-356
    • Lu, Y.1    Warner, R.2    Sedlak, M.3    Ho, N.4    Mosier, N.S.5
  • 34
    • 34250246166 scopus 로고
    • The peroxidase-glucose oxidase system: A new method to determine glucose liberated by carbohydrate degrading soil enzymes
    • Kapustka, L. A., Annala, A. E., Swanson, W. C., The peroxidase-glucose oxidase system: a new method to determine glucose liberated by carbohydrate degrading soil enzymes. Plant Soil 1981, 63, 487-490.
    • (1981) Plant Soil , vol.63 , pp. 487-490
    • Kapustka, L.A.1    Annala, A.E.2    Swanson, W.C.3
  • 35
    • 33746971932 scopus 로고    scopus 로고
    • Effect of the medium composition on formation of amylase by Bacillus sp
    • Santos, Ede. O., Martins, M. L. L., Effect of the medium composition on formation of amylase by Bacillus sp. Braz. Arch. Biol. Technol. 2003, 46, 129-134.
    • (2003) Braz. Arch. Biol. Technol. , vol.46 , pp. 129-134
    • Santos, E.O.1    Martins, M.L.L.2
  • 36
    • 84863473157 scopus 로고    scopus 로고
    • Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose
    • Chai, Y. Y., Rahman, R. N., Illias, R. M., Goh, K. M., Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose. J. Ind. Microbiol. Biotechnol. 2012, 39, 731-741.
    • (2012) J. Ind. Microbiol. Biotechnol. , vol.39 , pp. 731-741
    • Chai, Y.Y.1    Rahman, R.N.2    Illias, R.M.3    Goh, K.M.4
  • 37
    • 77951719922 scopus 로고    scopus 로고
    • Biochemical characterization of raw-starchdigesting alpha amylase purified from Bacillus amyloliquefaciens
    • Gangadharan, D., Nampoothiri, K. M., Sivaramakrishnan, S., Pandey, A., Biochemical characterization of raw-starchdigesting alpha amylase purified from Bacillus amyloliquefaciens. Appl. Biochem. Biotechnol. 2009, 158, 653-662.
    • (2009) Appl. Biochem. Biotechnol. , vol.158 , pp. 653-662
    • Gangadharan, D.1    Nampoothiri, K.M.2    Sivaramakrishnan, S.3    Pandey, A.4
  • 38
    • 40749092049 scopus 로고    scopus 로고
    • A novel raw starch digesting α-amylase from a newly isolated Bacillus sp. YX-1: Purification and characterization
    • Liu, X. D., Xu, Y., A novel raw starch digesting α-amylase from a newly isolated Bacillus sp. YX-1: purification and characterization. Bioresour. Technol. 2008, 99, 4315-4320.
    • (2008) Bioresour. Technol. , vol.99 , pp. 4315-4320
    • Liu, X.D.1    Xu, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.