메뉴 건너뛰기




Volumn 93, Issue 3, 2012, Pages 1127-1134

α-L-Rhamnosidase of Aspergillus terreus immobilized on ferromagnetic supports

Author keywords

l Rhamnosidase; Aspergillus terreus; Chitosan; Dacron; Immobilization; POS PVA

Indexed keywords

APPARENT K; ASPERGILLUS TERREUS; CHITOSAN DERIVATIVES; COPRECIPITATION METHOD; DACRON; FERROMAGNETIC SUPPORTS; FERROUS CHLORIDE; FREE ENZYME; GLUTARALDEHYDES; IMMOBILIZED ENZYME; MAXIMUM TEMPERATURE; POS/PVA; SOLUBLE ENZYMES; TEMPERATURE RANGE;

EID: 84856379677     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3469-y     Document Type: Article
Times cited : (29)

References (25)
  • 1
    • 33645231442 scopus 로고    scopus 로고
    • Fish trypsin immobilized on ferromagnetic Dacron
    • doi: 10.1016/j.procbio.2005.11.023
    • IPG Amaral MG Carneiro-da-Cunha LB Carvalho Jr RS Bezerra 2006 Fish trypsin immobilized on ferromagnetic Dacron Process Biochem 41 1213 1216 10.1016/j.procbio.2005.11.023 10.1016/j.procbio.2005.11.023 1:CAS:528: DC%2BD28XivVaqsLo%3D Amaral IPG, Carneiro-da-Cunha MG, Carvalho LB Jr, Bezerra RS (2006) Fish trypsin immobilized on ferromagnetic Dacron. Process Biochem 41:1213-1216. doi: 10.1016/j.procbio.2005.11.023
    • (2006) Process Biochem , vol.41 , pp. 1213-1216
    • Amaral, I.P.G.1    Carneiro-Da-Cunha, M.G.2    Carvalho Jr., L.B.3    Bezerra, R.S.4
  • 2
    • 0028414151 scopus 로고
    • Kinetic and immobilization studies on fungal glycosidases for aroma enhancement in wine
    • DOI 10.1016/0141-0229(94)90168-6
    • Caldini C, Bonomi F, Pifferi PG, Lanzarini G, Galante YM (1994) Kinetic and immobilization studies on fungal glycosidases for aroma enhancement in wine. Enzyme Microb Technol 16:286-291. doi: (Pubitemid 24128064)
    • (1994) Enzyme and Microbial Technology , vol.16 , Issue.4 , pp. 286-291
    • Caldini, C.1    Bonomi, F.2    Pifferi, P.G.3    Lanzarini, G.4    Galante, Y.M.5
  • 4
    • 0344897697 scopus 로고    scopus 로고
    • Preparation and characterization of magnetic duolite-polystyrene composite particles for enzyme immobilization
    • 10.1016/S0260-8774(03)00225-5
    • D Demirel A Ozdural M Mutlu 2004 Preparation and characterization of magnetic duolite-polystyrene composite particles for enzyme immobilization J Food Process Eng 62 3 203 208 10.1016/S0260-8774(03)00225-5 Demirel D, Ozdural A, Mutlu M (2004) Preparation and characterization of magnetic duolite-polystyrene composite particles for enzyme immobilization. J Food Eng 62(3):203-208. doi: 10.1016/S0260-8774(03)00225-5
    • (2004) J Food Process Eng , vol.62 , Issue.3 , pp. 203-208
    • Demirel, D.1    Ozdural, A.2    Mutlu, M.3
  • 5
    • 0030380628 scopus 로고    scopus 로고
    • Thermostabilization of naringinase from Penicillium decumbens by proteins in solution and immobilization on insoluble proteins
    • Ellenrieder G, Daz M (1996) Thermostabilization of naringinase from Penicillium decumbens by proteins in solution and immobilization on insoluble proteins. Biocatal Biotransform 14:113-123. doi: (Pubitemid 126714544)
    • (1996) Biocatalysis and Biotransformation , vol.14 , Issue.2 , pp. 113-123
    • Ellenrieder, G.1    Daz, M.2
  • 6
    • 0031887977 scopus 로고    scopus 로고
    • Hydrolysis of supersaturated naringin solutions by free and immobilized naringinase
    • DOI 10.1023/A:1008859627134
    • Ellenrieder G, Blanco S, Daz M (1998) Hydrolysis of supersaturated naringin solutions by free and immobilized naringinase. Biotechnol Tech 12:63-65. doi: (Pubitemid 28102196)
    • (1998) Biotechnology Techniques , vol.12 , Issue.1 , pp. 63-65
    • Ellenrieder, G.1    Blanco, S.2    Daz, M.3
  • 7
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin- and chitosan-based materials for enzyme immobilizations: A review
    • DOI 10.1016/j.enzmictec.2003.12.013, PII S0141022904001231
    • Krajewska B (2004) Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enzyme Microb Technol 35(2-3):126-139. doi: (Pubitemid 38906662)
    • (2004) Enzyme and Microbial Technology , vol.35 , Issue.2-3 , pp. 126-139
    • Krajewska, B.1
  • 8
    • 0031573765 scopus 로고    scopus 로고
    • Purification and characterization of an α-L-rhamnosidase from Aspergillus niger
    • DOI 10.1016/S0378-1097(97)00487-4, PII S0378109797004874
    • Manzanares P, Graaff LH, Visser J (1997) Purification and characterization of an α-l-rhamnosidase from Aspergillus niger. FEMS Microbiol Lett 157(2):279-283. doi: (Pubitemid 28248212)
    • (1997) FEMS Microbiology Letters , vol.157 , Issue.2 , pp. 279-283
    • Manzanares, P.1    De Graaff, L.H.2    Visser, J.3
  • 9
    • 0033813807 scopus 로고    scopus 로고
    • Purification and characterization of an α-l-rhamnosidase from Aspergillus nidulans
    • doi: 10.1046/j.1365-2672.2000.00788.x
    • P Manzanares M Orejas E Ibanez S Valles D Ramon 2000 Purification and characterization of an α-l-rhamnosidase from Aspergillus nidulans Lett Appl Microbiol 31 198 202 10.1046/j.1365-2672.2000.00788.x 10.1046/j.1365-2672. 2000.00788.x 1:CAS:528:DC%2BD3cXntFOmsb0%3D Manzanares P, Orejas M, Ibanez E, Valles S, Ramon D (2000) Purification and characterization of an α-l-rhamnosidase from Aspergillus nidulans. Lett Appl Microbiol 31:198-202. doi: 10.1046/j.1365-2672.2000.00788.x
    • (2000) Lett Appl Microbiol , vol.31 , pp. 198-202
    • Manzanares, P.1    Orejas, M.2    Ibanez, E.3    Valles, S.4    Ramon, D.5
  • 10
    • 0035348295 scopus 로고    scopus 로고
    • Purification and Characterization of Two Different α-L- Rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus
    • DOI 10.1128/AEM.67.5.2230-2234.2001
    • Manzanares P, van Den Broeck HC, de Graaff LH, Visser J (2001) Purification and characterization of two different α-l-rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus. Appl Environ Microbiol 67:2230-2234. doi: (Pubitemid 33641410)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.5 , pp. 2230-2234
    • Manzanares, P.1    Van Den Broeck, H.C.2    De Graaff, L.H.3    Visser, J.4
  • 11
    • 0142155532 scopus 로고    scopus 로고
    • Synthesis of alkyl-α-L-rhamnosides by water soluble alcohols enzymatic glycosylation
    • DOI 10.1016/S0960-8524(03)00131-7
    • Martearena MR, Blanco S, Ellenrieder G (2003) Synthesis of alkyl α-l-rhamnosides by water soluble alcohols enzymatic glycosylation. Bioresour Technol 90(3):297-303. doi: (Pubitemid 37324164)
    • (2003) Bioresource Technology , vol.90 , Issue.3 , pp. 297-303
    • Martearena, M.R.1    Blanco, S.2    Ellenrieder, G.3
  • 12
    • 4644338761 scopus 로고    scopus 로고
    • Generation of an α-L-rhamnosidase library and its application for the selective derhamnosylation of natural products
    • DOI 10.1002/bit.20187
    • Monti D, Pisvejcova A, Kren V, Lama M, Riva S (2004) Generation of an α-rhamnosidase library and its application for the selective derhamnosylation of natural products. Biotechnol Bioeng 87:763-771. doi: (Pubitemid 39264645)
    • (2004) Biotechnology and Bioengineering , vol.87 , Issue.6 , pp. 763-771
    • Monti, D.1    Pisvejcova, A.2    Kren, V.3    Lama, M.4    Riva, S.5
  • 13
  • 14
    • 84985246674 scopus 로고
    • Naringin bitterness of grapefruit juice debittered with naringinase immobilized in a hollow fiber
    • doi: 10.1111/j.1365-2621.1979.tb06438.x
    • AC Olson GM Gray DG Guadagni 1979 Naringin bitterness of grapefruit juice debittered with naringinase immobilized in a hollow fiber J Food Sci 44 5 1358 1361 10.1111/j.1365-2621.1979.tb06438.x 10.1111/j.1365-2621.1979.tb06438.x 1:CAS:528:DyaE1MXlslelsLg%3D Olson AC, Gray GM, Guadagni DG (1979) Naringin bitterness of grapefruit juice debittered with naringinase immobilized in a hollow fiber. J Food Sci 44(5):1358-1361. doi: 10.1111/j.1365-2621.1979.tb06438. x
    • (1979) J Food Sci , vol.44 , Issue.5 , pp. 1358-1361
    • Olson, A.C.1    Gray, G.M.2    Guadagni, D.G.3
  • 15
    • 0007659646 scopus 로고
    • Preparation and properties of naringinase immobilized by ionic binding to DEAE Sephadex
    • 1:CAS:528:DyaE1cXhvVamtA%3D%3D
    • Ono M, Tosa T, Chibata I (1977) Preparation and properties of naringinase immobilized by ionic binding to DEAE Sephadex. J Ferment Technol 55:493-500
    • (1977) J Ferment Technol , vol.55 , pp. 493-500
    • Ono, M.1    Tosa, T.2    Chibata, I.3
  • 16
    • 0029980622 scopus 로고    scopus 로고
    • Studies on the applicability of alginate-entrapped naringinase for the debittering of kinnow juice
    • DOI 10.1016/0141-0229(95)00100-X
    • Puri M, Marwaha SS, Kothari RM (1996) Studies on the applicability of alginate entrapped naringinase for the debittering of kinnow juice. Enzyme Microb Technol 18(4):281-285. doi: (Pubitemid 26077599)
    • (1996) Enzyme and Microbial Technology , vol.18 , Issue.4 , pp. 281-285
    • Puri, M.1    Marwaha, S.S.2    Kothari, R.M.3
  • 17
    • 0022339182 scopus 로고
    • A method for assaying the rhamnosidase activity of naringinase
    • DOI 10.1016/0003-2697(85)90614-1
    • Romero C, Manjon A, Bastida J, Iborra JL (1985) A method for assaying the rhamnosidase activity of naringinase. Anal Biochem 149(2):566-571. doi: (Pubitemid 16238642)
    • (1985) Analytical Biochemistry , vol.149 , Issue.2 , pp. 566-571
    • Romero, C.1    Manjon, A.2    Bastida, J.3    Iborra, J.L.4
  • 18
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using coomassie brilliant blue G250
    • Sedmak JJ, Grossberg SE (1977) A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal Biochem 79(1-2):544-552. doi: (Pubitemid 8105123)
    • (1977) Analytical Biochemistry , vol.79 , Issue.1-2 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 19
    • 0002511274 scopus 로고    scopus 로고
    • Naringinase immobilization in packaging films for reducing naringin concentrations in grapefruit juice
    • Soares NFF, Hotchkiss JH (1998) Naringinase immobilization in packaging films for reducing naringin concentration in grapefruit juice. J Food Sci 63:61-65. doi: (Pubitemid 28165272)
    • (1998) Journal of Food Science , vol.63 , Issue.1 , pp. 61-65
    • Soares, N.F.F.1    Hotchkiss, J.H.2
  • 20
    • 2042472158 scopus 로고    scopus 로고
    • Purification and some properties of α-l-rhamnosidase of Aspergillus terreus
    • 1:CAS:528:DC%2BD3cXlsFSitLk%3D
    • Soria F, Cuevas C, Ellenrieder G (1999) Purification and some properties of α-l-rhamnosidase of Aspergillus terreus. Appl Biol Sci 5:109-120
    • (1999) Appl Biol Sci , vol.5 , pp. 109-120
    • Soria, F.1    Cuevas, C.2    Ellenrieder, G.3
  • 21
    • 0008421832 scopus 로고
    • Factors affecting the inactivation of naringinase in chitin during debittering of fruit juice
    • 1:CAS:528:DyaL2cXkvV2iu70%3D
    • Tsen H-Y (1984) Factors affecting the inactivation of naringinase on chitin during debittering of fruit juice. J Ferment Technol 62:263-267
    • (1984) J Ferment Technol , vol.62 , pp. 263-267
    • Tsen, H.-Y.1
  • 22
    • 84985225803 scopus 로고
    • Limonin and naringin removal from grapefruit juice with naringinase entrapped in cellulose triacetate fibers
    • doi: 10.1111/j.1365-2621.1991.tb07968.x
    • HY Tsen GK Yu 1991 Limonin and naringin removal from grapefruit juice with naringinase entrapped in cellulose triacetate fibers J Food Sci 56 1 31 34 10.1111/j.1365-2621.1991.tb07968.x 10.1111/j.1365-2621.1991.tb07968.x 1:CAS:528:DyaK3MXktVOhu70%3D Tsen HY, Yu GK (1991) Limonin and naringin removal from grapefruit juice with naringinase entrapped in cellulose triacetate fibers. J Food Sci 56(1):31-34. doi: 10.1111/j.1365-2621.1991.tb07968.x
    • (1991) J Food Sci , vol.56 , Issue.1 , pp. 31-34
    • Tsen, H.Y.1    Yu, G.K.2
  • 23
    • 0001043747 scopus 로고
    • Fiber entrapment of naringinase from Penicillium sp. and application to fruit juice debittering
    • doi: 10.1016/0922-338X(89)90120-7
    • H-Y Tsen S-Y Tsai G-K Yu 1989 Fiber entrapment of naringinase from Penicillium sp. and application to fruit juice debittering J Ferment Bioeng 67 186 189 10.1016/0922-338X(89)90120-7 10.1016/0922-338X(89)90120-7 1:CAS:528:DyaL1MXitlSgsbs%3D Tsen H-Y, Tsai S-Y, Yu G-K (1989) Fiber entrapment of naringinase from Penicillium sp. and application to fruit juice debittering. J Ferment Bioeng 67:186-189. doi: 10.1016/0922-338X(89)90120-7
    • (1989) J Ferment Bioeng , vol.67 , pp. 186-189
    • Tsen, H.-Y.1    Tsai, S.-Y.2    Yu, G.-K.3
  • 24
    • 0023515692 scopus 로고
    • The application of immobilized α-l-rhamnosidase and l-rhamnose dehydrogenase in the analysis of l-rhamnose and α-l-rhamnosides
    • doi: 10.1007/BF02798352
    • PL Turecek F Pittner 1987 The application of immobilized α-l-rhamnosidase and l-rhamnose dehydrogenase in the analysis of l-rhamnose and α-l-rhamnosides Appl Biochem Biotechnol 16 15 24 10.1007/BF02798352 10.1007/BF02798352 Turecek PL, Pittner F (1987) The application of immobilized α-l-rhamnosidase and l-rhamnose dehydrogenase in the analysis of l-rhamnose and α-l-rhamnosides. Appl Biochem Biotechnol 16:15-24. doi: 10.1007/BF02798352
    • (1987) Appl Biochem Biotechnol , vol.16 , pp. 15-24
    • Turecek, P.L.1    Pittner, F.2
  • 25
    • 0035385065 scopus 로고    scopus 로고
    • Immobilisation of α-l-rhamnosidase of Aspergillus terreus on bagasse particles based matrix
    • 1:CAS:528:DC%2BD3MXlsFantL0%3D
    • Yadav S, Yadav KDS (2001) Immobilisation of α-l-rhamnosidase of Aspergillus terreus on bagasse particles based matrix. Indian J Chem Techn 8(4):314-318
    • (2001) Indian J Chem Techn , vol.8 , Issue.4 , pp. 314-318
    • Yadav, S.1    Yadav, K.D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.