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Volumn 117, Issue 1, 2009, Pages 94-98

Purification of soybean amylase by superparamagnetic particles

Author keywords

Amylase; Magnetic carrier technology; Soybean; Superparamagnetic particles

Indexed keywords

AMMONIUM SULFATE; AMYLASE; CROSS LINKING REAGENT; EPICHLOROHYDRIN; STARCH; SUPERPARAMAGNETIC IRON OXIDE;

EID: 67349160764     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.03.089     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 0034884917 scopus 로고    scopus 로고
    • Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres
    • Akgöl S., Kacar Y., Denizli A., and Ari{dotless}ca M.Y. Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres. Food Chemistry 74 (2001) 281-288
    • (2001) Food Chemistry , vol.74 , pp. 281-288
    • Akgöl, S.1    Kacar, Y.2    Denizli, A.3    Arica, M.Y.4
  • 2
    • 0034111128 scopus 로고    scopus 로고
    • Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment
    • Cesar M., Olga A., Roberto F.L., and Jose M.G. Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment. Enzyme and Microbial Technology 26 (2000) 509-515
    • (2000) Enzyme and Microbial Technology , vol.26 , pp. 509-515
    • Cesar, M.1    Olga, A.2    Roberto, F.L.3    Jose, M.G.4
  • 3
    • 33747133972 scopus 로고    scopus 로고
    • Synthesis and characterization of superparamagnetic composite nanorings
    • Cui L., Gu H., Xu H., and Shi D. Synthesis and characterization of superparamagnetic composite nanorings. Materials Letters 60 (2006) 2929-2932
    • (2006) Materials Letters , vol.60 , pp. 2929-2932
    • Cui, L.1    Gu, H.2    Xu, H.3    Shi, D.4
  • 4
    • 0032788365 scopus 로고    scopus 로고
    • Purification and characterization of two α-amylases from Toxoplasma gondii
    • Ferre A., Hoebeke J., and Bout D. Purification and characterization of two α-amylases from Toxoplasma gondii. Experimental Parasitology 92 (1999) 64-72
    • (1999) Experimental Parasitology , vol.92 , pp. 64-72
    • Ferre, A.1    Hoebeke, J.2    Bout, D.3
  • 5
    • 0024616281 scopus 로고
    • Purification of lingual amylase from serous glands of rat tongue and characterization of rat lingual amylase and lingual lipase
    • Field R.B., Spielman A.I., and Hand A.R. Purification of lingual amylase from serous glands of rat tongue and characterization of rat lingual amylase and lingual lipase. Journal of Dental Research 68 (1989) 139-145
    • (1989) Journal of Dental Research , vol.68 , pp. 139-145
    • Field, R.B.1    Spielman, A.I.2    Hand, A.R.3
  • 6
    • 27144440164 scopus 로고    scopus 로고
    • Isolation and characterization of amylase from fermented cassava (Manihot esculenta Crantz) wastewater
    • Ganiyu O. Isolation and characterization of amylase from fermented cassava (Manihot esculenta Crantz) wastewater. African Journal of Biotechnology 4 (2005) 1117-1123
    • (2005) African Journal of Biotechnology , vol.4 , pp. 1117-1123
    • Ganiyu, O.1
  • 7
    • 3743138412 scopus 로고
    • Purification and characterization of a β-amylase from soya beans
    • Gertler A., and Birk Y. Purification and characterization of a β-amylase from soya beans. Biochemical Journal 95 (1965) 621-627
    • (1965) Biochemical Journal , vol.95 , pp. 621-627
    • Gertler, A.1    Birk, Y.2
  • 8
    • 51249173269 scopus 로고
    • Multisubstrate specifics amylase from mushroom Termitomyces clypeatus
    • Ghosh A.K., and Sengupta S. Multisubstrate specifics amylase from mushroom Termitomyces clypeatus. Journal Bioscience 11 (1987) 275-285
    • (1987) Journal Bioscience , vol.11 , pp. 275-285
    • Ghosh, A.K.1    Sengupta, S.2
  • 12
    • 33749250158 scopus 로고    scopus 로고
    • Entrapment of α-amylase in alginate beads: Single step protocol for purification and thermal stabilization
    • Kumar R.S.S., Vishwanath K.S., Singh S.A., and Rao A.G.A. Entrapment of α-amylase in alginate beads: Single step protocol for purification and thermal stabilization. Process Biochemistry 41 (2006) 2282-2288
    • (2006) Process Biochemistry , vol.41 , pp. 2282-2288
    • Kumar, R.S.S.1    Vishwanath, K.S.2    Singh, S.A.3    Rao, A.G.A.4
  • 14
    • 22244470385 scopus 로고    scopus 로고
    • Immobilization of lipase onto micron-size magnetic beads
    • Liu X., Guan Y., Shen R., and Liu H. Immobilization of lipase onto micron-size magnetic beads. Journal of Chromatography B 822 (2005) 91-97
    • (2005) Journal of Chromatography B , vol.822 , pp. 91-97
    • Liu, X.1    Guan, Y.2    Shen, R.3    Liu, H.4
  • 15
    • 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
  • 16
    • 51249183453 scopus 로고
    • Isolation and partial characterisation of α-amylase components evolved during early wheat germination
    • Machaiah J.P., and Vakil U.K. Isolation and partial characterisation of α-amylase components evolved during early wheat germination. Journal of Biosciences 6 (1984) 47-59
    • (1984) Journal of Biosciences , vol.6 , pp. 47-59
    • Machaiah, J.P.1    Vakil, U.K.2
  • 17
    • 4444346220 scopus 로고    scopus 로고
    • Purification and characterization of alpha-amylase from infective juveniles of the nematode Heterohabditis bacterophora
    • Mohamed M.A. Purification and characterization of alpha-amylase from infective juveniles of the nematode Heterohabditis bacterophora. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 130 (2004) 1-9
    • (2004) Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology , vol.130 , pp. 1-9
    • Mohamed, M.A.1
  • 19
    • 0038262636 scopus 로고    scopus 로고
    • Three α-amylases from malted finger millet (Ragi, Eleusine coracana, Indaf-15)-purification and partial characterization
    • Nirmala M., and Muralikrishna G. Three α-amylases from malted finger millet (Ragi, Eleusine coracana, Indaf-15)-purification and partial characterization. Phytochemistry 62 (2003) 21-30
    • (2003) Phytochemistry , vol.62 , pp. 21-30
    • Nirmala, M.1    Muralikrishna, G.2
  • 21
    • 0031921463 scopus 로고    scopus 로고
    • Metabolic evolution in α-amylases from Drosophila virilis and D. repleta, two species with different ecological niches
    • Prigent S., Matoub M., Rouland C., and Cariou M.L. Metabolic evolution in α-amylases from Drosophila virilis and D. repleta, two species with different ecological niches. Comparative Biochemistry and Physiology 119 B (1998) 407-412
    • (1998) Comparative Biochemistry and Physiology , vol.119 , Issue.B , pp. 407-412
    • Prigent, S.1    Matoub, M.2    Rouland, C.3    Cariou, M.L.4
  • 24
    • 0344972983 scopus 로고    scopus 로고
    • DNA isolation using avidin-coated magnetic nanoclusters
    • Sonti S.V., and Bose A. DNA isolation using avidin-coated magnetic nanoclusters. Colloids and Surface Biointerfaces 8 (1997) 199-204
    • (1997) Colloids and Surface Biointerfaces , vol.8 , pp. 199-204
    • Sonti, S.V.1    Bose, A.2
  • 25
    • 0035822032 scopus 로고    scopus 로고
    • An efficient purification process for sweet potato beta-amylase by affinity precipitation with alginate
    • Teotia S., Khare S.K., and Gupta M.N. An efficient purification process for sweet potato beta-amylase by affinity precipitation with alginate. Enzyme and Microbial Technology 28 (2001) 792-795
    • (2001) Enzyme and Microbial Technology , vol.28 , pp. 792-795
    • Teotia, S.1    Khare, S.K.2    Gupta, M.N.3
  • 28
    • 0021334685 scopus 로고
    • Amylase from human serous ovarian tumors: purification and characterization
    • Zakowski J.J., Gregory M.R., and Bruns D.E. Amylase from human serous ovarian tumors: purification and characterization. Clinical Chemistry 30 (1984) 62-68
    • (1984) Clinical Chemistry , vol.30 , pp. 62-68
    • Zakowski, J.J.1    Gregory, M.R.2    Bruns, D.E.3
  • 29
    • 0034021261 scopus 로고    scopus 로고
    • Partial characterization of α-amylase in the salivary glands of Lygus hesperus and L. lineolaris
    • Zeng F., and Cohen A.C. Partial characterization of α-amylase in the salivary glands of Lygus hesperus and L. lineolaris. Comparative Biochemistry and Physiology Part B 126 (2000) 9-16
    • (2000) Comparative Biochemistry and Physiology Part B , vol.126 , pp. 9-16
    • Zeng, F.1    Cohen, A.C.2
  • 30
    • 0038397339 scopus 로고    scopus 로고
    • Preparation and characterization of immobilized lipase on magnetic hydrophobic microspheres
    • Zheng G., Shu B., and Yan S. Preparation and characterization of immobilized lipase on magnetic hydrophobic microspheres. Enzyme and Microbial Technology 32 (2003) 776-782
    • (2003) Enzyme and Microbial Technology , vol.32 , pp. 776-782
    • Zheng, G.1    Shu, B.2    Yan, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.