메뉴 건너뛰기




Volumn 99, Issue 3, 2006, Pages 444-449

Purification and some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuber

Author keywords

Amylase; Characterization; Glycoprotein; Pachyrhizus erosus L. tuber

Indexed keywords

AMYLASE; CADMIUM; CALCIUM ION; CELLULOSE; CHELATING AGENT; COPPER ION; EDETIC ACID; FERRIC ION; FERROUS ION; GLYCOPROTEIN; LITHIUM ION; MAGNESIUM ION; MANGANESE; MERCURY; PHENOL; POTASSIUM ION; SILVER; SODIUM ION; STARCH; SUGAR; SULFURIC ACID; ZINC ION;

EID: 33646500580     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2005.07.056     Document Type: Article
Times cited : (36)

References (23)
  • 1
    • 0346997314 scopus 로고    scopus 로고
    • Characterization of the functional module responsible for the low temperature optimum of rice α-amylase (Amy 3E)
    • Abe R., Chib A.Y., and Nakajima T. Characterization of the functional module responsible for the low temperature optimum of rice α-amylase (Amy 3E). Biologia Bratislava 57 Suppl. 11 (2002) 197-202
    • (2002) Biologia Bratislava , vol.57 , Issue.SUPPL. 11 , pp. 197-202
    • Abe, R.1    Chib, A.Y.2    Nakajima, T.3
  • 2
    • 0344662855 scopus 로고
    • Purification and partial characterization of α-amylase allozymes from the lesser grain borer Rhyzopertha dominica
    • Baker J.E. Purification and partial characterization of α-amylase allozymes from the lesser grain borer Rhyzopertha dominica. Insect Biochemistry 21 (1991) 303-311
    • (1991) Insect Biochemistry , vol.21 , pp. 303-311
    • Baker, J.E.1
  • 4
    • 0003341872 scopus 로고
    • Characterization of α-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings
    • Beers E., and Duke S. Characterization of α-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings. Plant Physiology 92 (1990) 1154
    • (1990) Plant Physiology , vol.92 , pp. 1154
    • Beers, E.1    Duke, S.2
  • 5
    • 0001879039 scopus 로고    scopus 로고
    • Purification and characterization of α-amylase from vine inter-nodes
    • Berbezy P., Legendre L., and Maujean A. Purification and characterization of α-amylase from vine inter-nodes. Plant Physiology and Biochemistry 34 (1996) 353-361
    • (1996) Plant Physiology and Biochemistry , vol.34 , pp. 353-361
    • Berbezy, P.1    Legendre, L.2    Maujean, A.3
  • 6
    • 0015350246 scopus 로고
    • Extracellular alkaline amylase from a Bacillus species
    • Boyer E., and Ingle M. Extracellular alkaline amylase from a Bacillus species. Journal of Bacteriology 110 (1972) 992
    • (1972) Journal of Bacteriology , vol.110 , pp. 992
    • Boyer, E.1    Ingle, M.2
  • 9
    • 0026673888 scopus 로고
    • Purification, characterization and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23
    • Feller G., Lonhienne T., Deroanne C., Libioulle C., Van Beeumen J., and Gerday C. Purification, characterization and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23. Journal of Biological Chemistry 267 (1992) 5217-5221
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Van Beeumen, J.5    Gerday, C.6
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0030767204 scopus 로고    scopus 로고
    • Purification of amylase secreted from Bifidobacterium adolescentis
    • Lee S.K., Kim Y.B., and Ji G.E. Purification of amylase secreted from Bifidobacterium adolescentis. Journal of Applied Microbiology 83 3 (1997) 267-272
    • (1997) Journal of Applied Microbiology , vol.83 , Issue.3 , pp. 267-272
    • Lee, S.K.1    Kim, Y.B.2    Ji, G.E.3
  • 12
    • 0031849201 scopus 로고    scopus 로고
    • Production and properties of a raw-starch-degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23
    • Lin L.L., Chyau C.C., and Hsu W.H. Production and properties of a raw-starch-degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23. Biotechnology and Applied Biochemistry 28 (1998) 61-68
    • (1998) Biotechnology and Applied Biochemistry , vol.28 , pp. 61-68
    • Lin, L.L.1    Chyau, C.C.2    Hsu, W.H.3
  • 13
    • 0000603887 scopus 로고
    • Purification and characterization of pea epicotyl β-amylase
    • Lizotte P.A., Henson C.A., and Duke S.H. Purification and characterization of pea epicotyl β-amylase. Plant Physiology 92 (1990) 615-621
    • (1990) Plant Physiology , vol.92 , pp. 615-621
    • Lizotte, P.A.1    Henson, C.A.2    Duke, S.H.3
  • 15
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for the determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for the determination of reducing sugar. Analytical Chemistry 31 (1959) 426-429
    • (1959) Analytical Chemistry , vol.31 , pp. 426-429
    • Miller, G.L.1
  • 16
    • 0023424403 scopus 로고
    • Purification and characterization of the extracellular α-amylase activity of the yeast Schwanniomyces alluvius
    • Moranelli F., Yaguchi M., Calleja G.B., and Nasim A. Purification and characterization of the extracellular α-amylase activity of the yeast Schwanniomyces alluvius. Biochemistry and Cell Biology 65 10 (1987) 899-908
    • (1987) Biochemistry and Cell Biology , vol.65 , Issue.10 , pp. 899-908
    • Moranelli, F.1    Yaguchi, M.2    Calleja, G.B.3    Nasim, A.4
  • 17
    • 0001283165 scopus 로고
    • Action patterns of various exo-amylases and the anomeric configurations of their products
    • Nakakuki T., Azuma K., and Kajnuma K. Action patterns of various exo-amylases and the anomeric configurations of their products. Carbohydrate Research 128 (1984) 297-310
    • (1984) Carbohydrate Research , vol.128 , pp. 297-310
    • Nakakuki, T.1    Azuma, K.2    Kajnuma, K.3
  • 18
    • 0030896082 scopus 로고    scopus 로고
    • Purification and characterization of β-amylase from leaves of potato (Solanum tuberosum)
    • Nielsen A.V., Christensen T.M.I.E., Bojko M., and Marcussen J. Purification and characterization of β-amylase from leaves of potato (Solanum tuberosum). Physiologia Plantarum 99 1 (1997) 190-196
    • (1997) Physiologia Plantarum , vol.99 , Issue.1 , pp. 190-196
    • Nielsen, A.V.1    Christensen, T.M.I.E.2    Bojko, M.3    Marcussen, J.4
  • 19
    • 0033874124 scopus 로고    scopus 로고
    • Purification and characterization of an endoamylase from tulip (Tulipa gesneriana) bulbs
    • Ranwala A.P., and Miller W.B. Purification and characterization of an endoamylase from tulip (Tulipa gesneriana) bulbs. Physiologia Plantarum 109 (2000) 388
    • (2000) Physiologia Plantarum , vol.109 , pp. 388
    • Ranwala, A.P.1    Miller, W.B.2
  • 20
    • 0015606538 scopus 로고
    • A thermophilic extracellular α-amylase from Bacillus licheniformis
    • Saito N. A thermophilic extracellular α-amylase from Bacillus licheniformis. Archives of Biochemistry and Biophysics 155 (1973) 290
    • (1973) Archives of Biochemistry and Biophysics , vol.155 , pp. 290
    • Saito, N.1
  • 21
    • 0037076543 scopus 로고    scopus 로고
    • Pyrococcus furiosus α- amylase is stabilized by calcium and zinc
    • Savchenko A., Vielle C., Kang S., and Zeikus G. Pyrococcus furiosus α- amylase is stabilized by calcium and zinc. Biochemistry 41 (2002) 6193-6201
    • (2002) Biochemistry , vol.41 , pp. 6193-6201
    • Savchenko, A.1    Vielle, C.2    Kang, S.3    Zeikus, G.4
  • 22
    • 33646496532 scopus 로고
    • Simultaneous purification of α-amylase β-amylase from germinated rice seeds and some factors affecting activities of the purified enzymes
    • Shaw J.F., and Ou-Lee T.M. Simultaneous purification of α-amylase β-amylase from germinated rice seeds and some factors affecting activities of the purified enzymes. Botanical Bulletin of Academia Sinica 25 (1984) 197-204
    • (1984) Botanical Bulletin of Academia Sinica , vol.25 , pp. 197-204
    • Shaw, J.F.1    Ou-Lee, T.M.2
  • 23
    • 0035822032 scopus 로고    scopus 로고
    • An efficient purification process for sweet potato β-amylase by affinity precipitation with alginate
    • Teotia S., Khare S.K., and Gupta M.N. An efficient purification process for sweet potato β-amylase by affinity precipitation with alginate. Enzyme Microbial Technology 28 9-10 (2001) 792-795
    • (2001) Enzyme Microbial Technology , vol.28 , Issue.9-10 , pp. 792-795
    • Teotia, S.1    Khare, S.K.2    Gupta, M.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.