메뉴 건너뛰기




Volumn 86, Issue 11, 2006, Pages 1636-1647

Recent progress in the assays of xylanolytic enzymes

Author keywords

glucuronidase; Acetylxylan esterase; Endo 1,4 xylanase; Enzyme assays; Feruloyl esterase

Indexed keywords

ANIMALIA;

EID: 33747412234     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.2519     Document Type: Conference Paper
Times cited : (12)

References (133)
  • 1
    • 0037623814 scopus 로고    scopus 로고
    • Hemicellulose bioconversion
    • Saha BC, Hemicellulose bioconversion. J Ind Microbiol Biotechnol 30:279-291 (2003).
    • (2003) J Ind Microbiol Biotechnol , vol.30 , pp. 279-291
    • Saha, B.C.1
  • 3
    • 0344732703 scopus 로고
    • Xylooligosaccharides
    • ed. by Nakakuki T. Gordon and Breach Science Publishers, Switzerland
    • Koga K and Fujikawa S, Xylooligosaccharides, in Oligosaccharides. Production, Properties, and Applications, ed. by Nakakuki T. Gordon and Breach Science Publishers, Switzerland, pp. 130-143 (1993).
    • (1993) Oligosaccharides. Production, Properties, and Applications , pp. 130-143
    • Koga, K.1    Fujikawa, S.2
  • 4
    • 0003034798 scopus 로고
    • Application of hemicellulases in the food, feed, and pulp and paper industries
    • ed. by Coughlan MP and Hazlewood GP. Portland Press, London and Chapel Hill
    • Wong KKY and Saddler JN, Application of hemicellulases in the food, feed, and pulp and paper industries, in Hemicellulose and hemicellulases, ed. by Coughlan MP and Hazlewood GP. Portland Press, London and Chapel Hill, pp. 127-143 (1993).
    • (1993) Hemicellulose and Hemicellulases , pp. 127-143
    • Wong, K.K.Y.1    Saddler, J.N.2
  • 5
    • 0027468318 scopus 로고
    • Bacterial cellulases and xylanases
    • Gilbert HJ and Hazlewood GP, Bacterial cellulases and xylanases. J Gen Microbiol 139:187-194 (1993).
    • (1993) J Gen Microbiol , vol.139 , pp. 187-194
    • Gilbert, H.J.1    Hazlewood, G.P.2
  • 6
    • 0001585391 scopus 로고
    • The role of wheat non-starch polysaccharides in broiler nutrition
    • Annison G, The role of wheat non-starch polysaccharides in broiler nutrition. Aust J Agric Res 44:405-422 (1993).
    • (1993) Aust J Agric Res , vol.44 , pp. 405-422
    • Annison, G.1
  • 7
    • 0010160592 scopus 로고
    • Plant polysaccharides - Their physiochemical properties and nutritional roles in monogastric animals
    • ed. by Lyons TP and Jacques KA. Alltech Inc., Nottingham
    • Annison G and Choct M, Plant polysaccharides - Their physiochemical properties and nutritional roles in monogastric animals, in Biotechnology in the Feed Industry, ed. by Lyons TP and Jacques KA. Alltech Inc., Nottingham, pp. 51-66 (1994).
    • (1994) Biotechnology in the Feed Industry , pp. 51-66
    • Annison, G.1    Choct, M.2
  • 8
    • 0001294606 scopus 로고
    • The influence of dietary xylanase on intestinal viscosity and molecular weight distribution of carbohydrates in rye-fed broiler chicks
    • ed. by Visser J, Beldman G, Kustersvan Someren MA and Voragen AGJ. Elsevier Science Publishers, Amsterdam
    • Bedford MR and Classen HL, The influence of dietary xylanase on intestinal viscosity and molecular weight distribution of carbohydrates in rye-fed broiler chicks, in Xylans and Xylanases, ed. by Visser J, Beldman G, Kustersvan Someren MA and Voragen AGJ. Elsevier Science Publishers, Amsterdam, pp. 361-370 (1992).
    • (1992) Xylans and Xylanases , pp. 361-370
    • Bedford, M.R.1    Classen, H.L.2
  • 9
    • 0009979733 scopus 로고
    • Xylanases improve wheat and rye diets by reducing chick gut viscosity
    • (Proceedings of the 1st symposium), ed. by Wenk C and Boessinger M. Institut für Nutztierwissenschaften, Gruppe Ernährung, Zürich
    • Morgan AJ, Graham H and Bedford MR, Xylanases improve wheat and rye diets by reducing chick gut viscosity, in Enzymes in Animal Nutrition (Proceedings of the 1st symposium), ed. by Wenk C and Boessinger M. Institut für Nutztierwissenschaften, Gruppe Ernährung, Zürich, pp. 73-77 (1993).
    • (1993) Enzymes in Animal Nutrition , pp. 73-77
    • Morgan, A.J.1    Graham, H.2    Bedford, M.R.3
  • 10
    • 0001017235 scopus 로고
    • Enzymatic modification of plant polysaccharides
    • McCleary BV, Enzymatic modification of plant polysaccharides. Int J Biol Macromol 8:349-354 (1986).
    • (1986) Int J Biol Macromol , vol.8 , pp. 349-354
    • McCleary, B.V.1
  • 11
    • 0000491882 scopus 로고
    • Xylanases and their application in bakery
    • ed. by Visser J, Beldman G, Kustersvan Someren MA and Voragen AGJ. Elsevier Science Publishers, Amsterdam
    • Maat J, Roza M, Verbakel J, Stam H, Santos da Silva MJ, Bosse M, et al, Xylanases and their application in bakery, in Xylans and Xylanases, ed. by Visser J, Beldman G, Kustersvan Someren MA and Voragen AGJ. Elsevier Science Publishers, Amsterdam, pp. 349-360 (1992).
    • (1992) Xylans and Xylanases , pp. 349-360
    • Maat, J.1    Roza, M.2    Verbakel, J.3    Stam, H.4    Santos Da Silva, M.J.5    Bosse, M.6
  • 12
    • 0001294896 scopus 로고
    • Investigations into the effects of an enzyme preparation for baking on wheat flour dough pentosans
    • Rouau X, Investigations into the effects of an enzyme preparation for baking on wheat flour dough pentosans. J Cereal Sci 18:145-157 (1993).
    • (1993) J Cereal Sci , vol.18 , pp. 145-157
    • Rouau, X.1
  • 13
    • 0001675314 scopus 로고
    • Modification of some physicochemical properties of wheat-flour pentosans by an enzyme complex recommended for baking
    • Rouau X and Moreau D, Modification of some physicochemical properties of wheat-flour pentosans by an enzyme complex recommended for baking. Cereal Chem 70:626-632 (1993).
    • (1993) Cereal Chem , vol.70 , pp. 626-632
    • Rouau, X.1    Moreau, D.2
  • 14
    • 0001665049 scopus 로고
    • Effect of an enzyme preparation containing pentosanases on the bread-making quality of flours in relation to changes in pentosan properties
    • Rouau X, El-Hayek M-L and Moreau D, Effect of an enzyme preparation containing pentosanases on the bread-making quality of flours in relation to changes in pentosan properties. J Cereal Sci 19:259-272 (1994).
    • (1994) J Cereal Sci , vol.19 , pp. 259-272
    • Rouau, X.1    El-Hayek, M.-L.2    Moreau, D.3
  • 16
    • 0029782017 scopus 로고    scopus 로고
    • Combined expression of Aspergillus nidulans endoxylanase X24 and Aspergillus oryzae α-amylase in industrial baker's yeasts and their use in bread making
    • Monfort A, Blasco A, Prieto JA and Sanz P, Combined expression of Aspergillus nidulans endoxylanase X24 and Aspergillus oryzae α-amylase in industrial baker's yeasts and their use in bread making. Appl Environ Microbiol 62:3712-3715 (1996).
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3712-3715
    • Monfort, A.1    Blasco, A.2    Prieto, J.A.3    Sanz, P.4
  • 17
    • 0019348717 scopus 로고
    • Xylanases: Structure and function
    • Reilly PJ, Xylanases: Structure and function. Basic Life Sci 18:111-129 (1981).
    • (1981) Basic Life Sci , vol.18 , pp. 111-129
    • Reilly, P.J.1
  • 18
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely P, Microbial xylanolytic systems. Trends Biotechnol 3:286-290 (1985).
    • (1985) Trends Biotechnol , vol.3 , pp. 286-290
    • Biely, P.1
  • 20
    • 0000303804 scopus 로고
    • The role of Trichoderma reesei xylanase and mannanase in treatment of softwood kraft pulp prior to bleaching
    • Buchert J, Salminen J, Siika-Aho M, Ranua M and Viikari L, The role of Trichoderma reesei xylanase and mannanase in treatment of softwood kraft pulp prior to bleaching. Holzforschung 47:473-478 (1993).
    • (1993) Holzforschung , vol.47 , pp. 473-478
    • Buchert, J.1    Salminen, J.2    Siika-Aho, M.3    Ranua, M.4    Viikari, L.5
  • 21
    • 0030308877 scopus 로고    scopus 로고
    • Roles for microbial enzymes in pulp and paper processing
    • Kirk TK and Jeffries TW, Roles for microbial enzymes in pulp and paper processing. ACS Symp Ser 655:2-14 (1996).
    • (1996) ACS Symp Ser , vol.655 , pp. 2-14
    • Kirk, T.K.1    Jeffries, T.W.2
  • 22
    • 0032965966 scopus 로고    scopus 로고
    • Application of enzymes in the pulp and paper industry
    • Bajpai P, Application of enzymes in the pulp and paper industry. Biotechnol Prog 15:147-157 (1999).
    • (1999) Biotechnol Prog , vol.15 , pp. 147-157
    • Bajpai, P.1
  • 23
    • 0021449279 scopus 로고
    • Removing hemicellulose from pulps by specific enzyme hydrolysis
    • Paice MG and Jurasek L, Removing hemicellulose from pulps by specific enzyme hydrolysis. J Wood Chem Technol 4:187-198 (1984).
    • (1984) J Wood Chem Technol , vol.4 , pp. 187-198
    • Paice, M.G.1    Jurasek, L.2
  • 24
    • 0031240034 scopus 로고    scopus 로고
    • Bleaching response of sulfite pulps to pretreatment with xylanases
    • Christov LP and Prior BA, Bleaching response of sulfite pulps to pretreatment with xylanases. Biotechnol Prog 13:695-698 (1997).
    • (1997) Biotechnol Prog , vol.13 , pp. 695-698
    • Christov, L.P.1    Prior, B.A.2
  • 25
    • 0028470886 scopus 로고
    • Production of xylanases from Penicillium janthinellum and its use in the recovery of cellulosic textile fibres
    • Milagres AMF and Prade RA, Production of xylanases from Penicillium janthinellum and its use in the recovery of cellulosic textile fibres. Enzyme Microb Technol 15:627-632 (1994).
    • (1994) Enzyme Microb Technol , vol.15 , pp. 627-632
    • Milagres, A.M.F.1    Prade, R.A.2
  • 26
    • 0030697820 scopus 로고    scopus 로고
    • Enzymatic deinking
    • Bajpai P, Enzymatic deinking. Adv Appl Microbiol 45:241-269 (1997).
    • (1997) Adv Appl Microbiol , vol.45 , pp. 241-269
    • Bajpai, P.1
  • 28
    • 0010785128 scopus 로고
    • A reagent for the copper-iodometric determination of very small amounts of sugar
    • Somogyi M, A reagent for the copper-iodometric determination of very small amounts of sugar. J Biol Chem 117:771-776 (1937).
    • (1937) J Biol Chem , vol.117 , pp. 771-776
    • Somogyi, M.1
  • 29
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • Nelson N, A photometric adaptation of the Somogyi method for the determination of glucose. J Biol Chem 153:375-380 (1944).
    • (1944) J Biol Chem , vol.153 , pp. 375-380
    • Nelson, N.1
  • 30
    • 0001089180 scopus 로고
    • Citric acid interference in the estimation of reducing sugars with alkaline copper reagent
    • Paleg LG, Citric acid interference in the estimation of reducing sugars with alkaline copper reagent. Anal Chem 31:1902-1904 (1959).
    • (1959) Anal Chem , vol.31 , pp. 1902-1904
    • Paleg, L.G.1
  • 31
    • 0002379474 scopus 로고
    • Dinitrosalicylic acid: A reagent for the estimation of sugar in normal diabetic urine
    • Sumner J, Dinitrosalicylic acid: A reagent for the estimation of sugar in normal diabetic urine. J Biol Chem 47:5-9 (1921).
    • (1921) J Biol Chem , vol.47 , pp. 5-9
    • Sumner, J.1
  • 32
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL, Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-428 (1959).
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 34
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey MJ, Biely P and Poutanen K, Interlaboratory testing of methods for assay of xylanase activity. J Biotechnol 23:257-270 (1992).
    • (1992) J Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 35
    • 0031829854 scopus 로고    scopus 로고
    • Comparative study of xylanase kinetics using dinitrosalicylic, arsenomolybdate, and ion chromatographic assays
    • Jeffries TW, Yang VW and Davis MW, Comparative study of xylanase kinetics using dinitrosalicylic, arsenomolybdate, and ion chromatographic assays. Appl Biochem Biotechnol 70-72:257-265 (1998).
    • (1998) Appl Biochem Biotechnol , vol.70-72 , pp. 257-265
    • Jeffries, T.W.1    Yang, V.W.2    Davis, M.W.3
  • 36
    • 34447620799 scopus 로고
    • Automated determination of glucose via reductive formation of lavender Cu(I)-2,2′-bicinchonate chelate
    • Gindler EM, Automated determination of glucose via reductive formation of lavender Cu(I)-2,2′-bicinchonate chelate. Clin Chem 16:519 (1970).
    • (1970) Clin Chem , vol.16 , pp. 519
    • Gindler, E.M.1
  • 37
    • 0023406022 scopus 로고
    • Assay of reducing sugars in the nanomole range with 2,2′- bicinchoninate
    • Waffenschmidt S and Jaenicke L, Assay of reducing sugars in the nanomole range with 2,2′-bicinchoninate. Anal Biochem 165:337-340 (1987).
    • (1987) Anal Biochem , vol.165 , pp. 337-340
    • Waffenschmidt, S.1    Jaenicke, L.2
  • 38
    • 0025766291 scopus 로고
    • Miniaturization of three carbohydrate analyses using a microscale plate reader
    • Fox JD and Robyt JF, Miniaturization of three carbohydrate analyses using a microscale plate reader. Anal Biochem 195:93-96 (1991).
    • (1991) Anal Biochem , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 39
    • 0012394141 scopus 로고
    • Some chemical and morphological changes induced by gibberellic acid in embryo-free wheat grain
    • Fincher GF and Stone AB, Some chemical and morphological changes induced by gibberellic acid in embryo-free wheat grain. Aust J Plant Physiol 1:297-311 (1974).
    • (1974) Aust J Plant Physiol , vol.1 , pp. 297-311
    • Fincher, G.F.1    Stone, A.B.2
  • 40
    • 0017400203 scopus 로고
    • Studies on xylan degrading enzymes. I. Purification and characterization of endo1,4-β-xylanase from Aspergillus niger, str. 14
    • Gorbacheva IV and Rodionova NA, Studies on xylan degrading enzymes. I. Purification and characterization of endo1,4-β-xylanase from Aspergillus niger, str. 14. Biochim Biophys Acta 484:79-93 (1977).
    • (1977) Biochim Biophys Acta , vol.484 , pp. 79-93
    • Gorbacheva, I.V.1    Rodionova, N.A.2
  • 41
    • 0011486042 scopus 로고
    • Assay of endo-β-D-xylanase activity with a soluble O-(carboxymethyl) derivative of larch-wood D-xylan
    • Sengupta S, Khowala S and Goswami PK, Assay of endo-β-D-xylanase activity with a soluble O-(carboxymethyl) derivative of larch-wood D-xylan. Carbohydr Res 168:156-161 (1987).
    • (1987) Carbohydr Res , vol.168 , pp. 156-161
    • Sengupta, S.1    Khowala, S.2    Goswami, P.K.3
  • 42
    • 0003026705 scopus 로고    scopus 로고
    • Simple approaches to identification of baking-active xylanases
    • ed. by Angelino SAGF, Hamer RJ, van Hartingsveldt W, Heidekamp F and van der Lugt JP. TNO Nutrition and Food Research Institute, Zeist, the Netherlands
    • Popper L, Simple approaches to identification of baking-active xylanases, in The first European Symposium on Enzymes and Grain Processing, ed. by Angelino SAGF, Hamer RJ, van Hartingsveldt W, Heidekamp F and van der Lugt JP. TNO Nutrition and Food Research Institute, Zeist, the Netherlands, pp. 110-120 (1997).
    • (1997) The First European Symposium on Enzymes and Grain Processing , pp. 110-120
    • Popper, L.1
  • 43
    • 0020580149 scopus 로고
    • The active site of an acidic endo-1,4-β-xylanase of Aspergillus niger
    • Biely P, Vršanská M and Gorbacheva IV, The active site of an acidic endo-1,4-β-xylanase of Aspergillus niger. Biochim Biophys Acta 743:155-161 (1983).
    • (1983) Biochim Biophys Acta , vol.743 , pp. 155-161
    • Biely, P.1    Vršanská, M.2    Gorbacheva, I.V.3
  • 44
    • 1042289392 scopus 로고    scopus 로고
    • XIP-I, a xylanase inhibitor protein from wheat: A novel protein function
    • Juge N, Payan F and Williamson G, XIP-I, a xylanase inhibitor protein from wheat: a novel protein function. Biochim Biophys Acta 1696:203-211 (2004).
    • (2004) Biochim Biophys Acta , vol.1696 , pp. 203-211
    • Juge, N.1    Payan, F.2    Williamson, G.3
  • 45
    • 0021982304 scopus 로고
    • Soluble chromogenic substrates for the assay of endo-1,4-β-xylanases and endo1,4-β-glucanases
    • Biely P, Mislovičová D and Toman R, Soluble chromogenic substrates for the assay of endo-1,4-β-xylanases and endo1,4-β- glucanases. Anal Biochem 144:142-146 (1985).
    • (1985) Anal Biochem , vol.144 , pp. 142-146
    • Biely, P.1    Mislovičová, D.2    Toman, R.3
  • 46
    • 0036684595 scopus 로고    scopus 로고
    • Interactions defining the specificity between fungal xylanases and the wheat proteinaceous inhibitor, XIP-I
    • Flatman R, McLauchlan WR, Juge N, Furniss CSM, Berrin JG, Hughes RK, et al, Interactions defining the specificity between fungal xylanases and the wheat proteinaceous inhibitor, XIP-I. Biochem J 365:773-781 (2003).
    • (2003) Biochem J , vol.365 , pp. 773-781
    • Flatman, R.1    McLauchlan, W.R.2    Juge, N.3    Furniss, C.S.M.4    Berrin, J.G.5    Hughes, R.K.6
  • 47
    • 0037677327 scopus 로고    scopus 로고
    • A screening method for endo-β-1,4-xylanase substrate selectivity
    • Moers K, Courtin CM, Brijs K and Delcour JA, A screening method for endo-β-1,4-xylanase substrate selectivity. Anal Biochem 319:73-77 (2003).
    • (2003) Anal Biochem , vol.319 , pp. 73-77
    • Moers, K.1    Courtin, C.M.2    Brijs, K.3    Delcour, J.A.4
  • 48
    • 0022039295 scopus 로고
    • Measurement of xylanase activity with insoluble xylan substrate
    • Nummi M, Perrin JM, Niku-Paavola ML and Enari TM, Measurement of xylanase activity with insoluble xylan substrate. Biochem J 226:617-620 (1985).
    • (1985) Biochem J , vol.226 , pp. 617-620
    • Nummi, M.1    Perrin, J.M.2    Niku-Paavola, M.L.3    Enari, T.M.4
  • 49
    • 0026677178 scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-β-1,4-glucanase and β-1,4-xylanase from bacterium Cellulomonas fimi
    • Badarkar S, Gilkes NR, Kilburn DG, Kwan E, Rose DS, Miller Jr RC, et al, Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-β-1,4-glucanase and β-1,4-xylanase from bacterium Cellulomonas fimi. J Mol Biol 228:693-695 (1992).
    • (1992) J Mol Biol , vol.228 , pp. 693-695
    • Badarkar, S.1    Gilkes, N.R.2    Kilburn, D.G.3    Kwan, E.4    Rose, D.S.5    Miller Jr., R.C.6
  • 50
    • 0002505638 scopus 로고
    • Identification and mode of action of endo-(1-4)-β-xylanases
    • ed. by Visser J, Beldman G, Kusters-van Someren MA and Voragen AGJ. Elsevier Science Publishers, Amsterdam
    • Biely P, Vršanská M and Kučár Š, Identification and mode of action of endo-(1-4)-β-xylanases, in Xylans and Xylanases, ed. by Visser J, Beldman G, Kusters-van Someren MA and Voragen AGJ. Elsevier Science Publishers, Amsterdam, pp. 81-95 (1992).
    • (1992) Xylans and Xylanases , pp. 81-95
    • Biely, P.1    Vršanská, M.2    Kučár, Š.3
  • 52
    • 0028761771 scopus 로고
    • A short synthesis of β-xylobiosides
    • Ziser L and Withers SG, A short synthesis of β-xylobiosides. Carbohydr Res 265:9-17 (1994).
    • (1994) Carbohydr Res , vol.265 , pp. 9-17
    • Ziser, L.1    Withers, S.G.2
  • 53
    • 0028834365 scopus 로고
    • Synthesis of 2- And 4-nitrophenyl β-glycosides of β-(1 → 4)-D-xylooligosaccharides of dp 2-4
    • Takeo K, Ohguchi Y, Hasegawa R and Kitamura S, Synthesis of 2- and 4-nitrophenyl β-glycosides of β-(1 → 4)-D-xylooligosaccharides of dp 2-4. Carbohydr Res 277:231-244 (1995).
    • (1995) Carbohydr Res , vol.277 , pp. 231-244
    • Takeo, K.1    Ohguchi, Y.2    Hasegawa, R.3    Kitamura, S.4
  • 54
    • 0031435059 scopus 로고    scopus 로고
    • An efficient chemical-enzymatic synthesis of 4-nitrophenyl β-D-xylobioside: A chromogenic substrate for xylanases
    • Mechaly A, Belakhov V, Shoham Y and Baasov T, An efficient chemical-enzymatic synthesis of 4-nitrophenyl β-D-xylobioside: a chromogenic substrate for xylanases. Carbohydr Res 304:111-115 (1997).
    • (1997) Carbohydr Res , vol.304 , pp. 111-115
    • Mechaly, A.1    Belakhov, V.2    Shoham, Y.3    Baasov, T.4
  • 55
    • 0032919461 scopus 로고    scopus 로고
    • Significant enhancement in the binding of p-nitrophenyl-β-D- xylobioside by the E128H mutant of F/10 xylanase from Streptomyces olivaceoviridis E-86
    • Kuno A, Shimizu D, Kaneko S, Hasegawa T, Gama Y, Hayashi K, et al, Significant enhancement in the binding of p-nitrophenyl-β-D-xylobioside by the E128H mutant of F/10 xylanase from Streptomyces olivaceoviridis E-86. FEBS Lett 450:299-305 (1999).
    • (1999) FEBS Lett , vol.450 , pp. 299-305
    • Kuno, A.1    Shimizu, D.2    Kaneko, S.3    Hasegawa, T.4    Gama, Y.5    Hayashi, K.6
  • 56
    • 0030298022 scopus 로고    scopus 로고
    • Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3
    • Christakopoulos P, Nerinckx W, Kekos D, Macris BJ and Claeyssens M, Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3. J Biotechnol 51:181-189 (1996).
    • (1996) J Biotechnol , vol.51 , pp. 181-189
    • Christakopoulos, P.1    Nerinckx, W.2    Kekos, D.3    Macris, B.J.4    Claeyssens, M.5
  • 58
    • 0031793845 scopus 로고    scopus 로고
    • Synthesis of 2,4-dinitrophenyl glycosides of D-xylobiose and D-mannobiose
    • Bolam DN, Charnwood SJ, Gilbert HJ and Hughes NA, Synthesis of 2,4-dinitrophenyl glycosides of D-xylobiose and D-mannobiose. Carbohydr Res 312:85-89 (1998).
    • (1998) Carbohydr Res , vol.312 , pp. 85-89
    • Bolam, D.N.1    Charnwood, S.J.2    Gilbert, H.J.3    Hughes, N.A.4
  • 59
    • 0032806993 scopus 로고    scopus 로고
    • Mode of action of a minor xylanase from Thermoascus aurantiacus on polysaccharides and model substrates
    • Kalogeris E, Christakopoulos P, Kekos D and Macris BJ, Mode of action of a minor xylanase from Thermoascus aurantiacus on polysaccharides and model substrates. J Biosci Bioeng 87:819-821 (1999).
    • (1999) J Biosci Bioeng , vol.87 , pp. 819-821
    • Kalogeris, E.1    Christakopoulos, P.2    Kekos, D.3    Macris, B.J.4
  • 60
    • 17844367347 scopus 로고    scopus 로고
    • Purification and characterization of two endo-β-1,4-xylanases of Schizophyllum commune
    • Kolenová K, Vršanská M and Biely P, Purification and characterization of two endo-β-1,4-xylanases of Schizophyllum commune. Enzyme Microb Technol 36:903-910 (2005).
    • (2005) Enzyme Microb Technol , vol.36 , pp. 903-910
    • Kolenová, K.1    Vršanská, M.2    Biely, P.3
  • 61
    • 0001085984 scopus 로고
    • Purification and properties of 2 xylanases from Aspergillus oryzae
    • Bailey M, Puls J and Poutanen K, Purification and properties of 2 xylanases from Aspergillus oryzae. Biotechnol Appl Biochem 13:380-389 (1991).
    • (1991) Biotechnol Appl Biochem , vol.13 , pp. 380-389
    • Bailey, M.1    Puls, J.2    Poutanen, K.3
  • 63
    • 0031777333 scopus 로고    scopus 로고
    • Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882
    • Bennett NA, Ryan J, Biely P, Vršanská M, Kremnický L, Macris BJ, et al, Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882. Carbohydr Res 306:445-455 (1998).
    • (1998) Carbohydr Res , vol.306 , pp. 445-455
    • Bennett, N.A.1    Ryan, J.2    Biely, P.3    Vršanská, M.4    Kremnický, L.5    Macris, B.J.6
  • 64
    • 0038553974 scopus 로고    scopus 로고
    • Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile
    • Katapodis P, Vršanská M, Kekos D, Nerinckx W, Biely P, Claeyssens M, et al, Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile. Carbohydr Res 338:1881-1890 (2003).
    • (2003) Carbohydr Res , vol.338 , pp. 1881-1890
    • Katapodis, P.1    Vršanská, M.2    Kekos, D.3    Nerinckx, W.4    Biely, P.5    Claeyssens, M.6
  • 65
    • 0002274797 scopus 로고
    • Aryl 4-thioxylobioside and 1,4-dithioxylobiosides as effectors of the enzyme activity for fungal D-xylanases
    • Comtat J, Defaye J, Driguez H and Ohleyer E, Aryl 4-thioxylobioside and 1,4-dithioxylobiosides as effectors of the enzyme activity for fungal D-xylanases. Carbohydr Res 144:33-44 (1985).
    • (1985) Carbohydr Res , vol.144 , pp. 33-44
    • Comtat, J.1    Defaye, J.2    Driguez, H.3    Ohleyer, E.4
  • 66
    • 0025908702 scopus 로고
    • The endo-1,4-β-glucanase I from Trichoderma reesei. Action on β-1,4-oligomers and polymers derived from D-glucose and D-xylose
    • Biely P, Vršanská M and Claeyssens M, The endo-1,4-β-glucanase I from Trichoderma reesei. Action on β-1,4-oligomers and polymers derived from D-glucose and D-xylose. Eur J Biochem 200:157-163 (1991).
    • (1991) Eur J Biochem , vol.200 , pp. 157-163
    • Biely, P.1    Vršanská, M.2    Claeyssens, M.3
  • 67
    • 0024763430 scopus 로고
    • Purification and characterization of an α-glucuronidase from a thermophilic fungus Thermoascus aurantiacus
    • Khandke KM, Vithayathil PJ and Murthy SK, Purification and characterization of an α-glucuronidase from a thermophilic fungus Thermoascus aurantiacus. Arch Biochem Biophys 274:511-517 (1989).
    • (1989) Arch Biochem Biophys , vol.274 , pp. 511-517
    • Khandke, K.M.1    Vithayathil, P.J.2    Murthy, S.K.3
  • 68
    • 0034629241 scopus 로고    scopus 로고
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • Tenkanen M and Siika-aho M, An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. J Biotechnol 78:149-161 (2000).
    • (2000) J Biotechnol , vol.78 , pp. 149-161
    • Tenkanen, M.1    Siika-aho, M.2
  • 69
    • 0343036237 scopus 로고    scopus 로고
    • Endo-β-1,4-xylanase families: Differences in catalytic properties
    • Biely P, Vršanská M, Tenkanen M and Kluepfel D, Endo-β-1,4-xylanase families: Differences in catalytic properties. J Biotechnol 57:151-166 (1997).
    • (1997) J Biotechnol , vol.57 , pp. 151-166
    • Biely, P.1    Vršanská, M.2    Tenkanen, M.3    Kluepfel, D.4
  • 71
    • 0003665610 scopus 로고
    • α-Glucuronidases in the hydrolysis of wood xylans
    • ed. by Visser J, Beldman G, Kusters-van Sommeren MA, Voragen AGJ. Elsevier Science Publishers, Amsterdam
    • Puls J, α-Glucuronidases in the hydrolysis of wood xylans, in Xylans and Xylanases, ed. by Visser J, Beldman G, Kusters-van Sommeren MA, Voragen AGJ. Elsevier Science Publishers, Amsterdam, pp. 213-224 (1992).
    • (1992) Xylans and Xylanases , pp. 213-224
    • Puls, J.1
  • 72
    • 0000854587 scopus 로고
    • A copper reagent for the determination of hexuronic acids and certain ketoses
    • Milner Y and Avigad G, A copper reagent for the determination of hexuronic acids and certain ketoses. Carbohydr Res 4:359-361 (1967).
    • (1967) Carbohydr Res , vol.4 , pp. 359-361
    • Milner, Y.1    Avigad, G.2
  • 73
    • 0028973509 scopus 로고
    • α-(4-O-Methyl)-D-glucuronidase activity produced by the rumen anaerobic fungus Piromonas communis: A study of selected properties
    • Wood TM and Wilson CA, α-(4-O-Methyl)-D-glucuronidase activity produced by the rumen anaerobic fungus Piromonas communis: a study of selected properties. Appl Microbiol Biotechnol 43:893-900 (1995).
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 893-900
    • Wood, T.M.1    Wilson, C.A.2
  • 74
    • 0028973385 scopus 로고
    • D-Xylan-degrading system from the fungus Phanerochaete chrysosporium: Isolation and partial characterisation of an α-(4-O-methyl)-D- glucuronidase
    • Castanares A, Hay AJ, Gordon AH, McCrae SI and Wood TM, D-Xylan-degrading system from the fungus Phanerochaete chrysosporium: isolation and partial characterisation of an α-(4-O-methyl)-D-glucuronidase. J Biotechnol 43:183-194 (1995).
    • (1995) J Biotechnol , vol.43 , pp. 183-194
    • Castanares, A.1    Hay, A.J.2    Gordon, A.H.3    McCrae, S.I.4    Wood, T.M.5
  • 75
    • 0023288603 scopus 로고
    • α-Glucuronidase in two microbial xylanolytic systems
    • Puls J, Schmidt O and Granzow C, α-Glucuronidase in two microbial xylanolytic systems. Enzyme Microb Technol 9:83-88 (1987).
    • (1987) Enzyme Microb Technol , vol.9 , pp. 83-88
    • Puls, J.1    Schmidt, O.2    Granzow, C.3
  • 77
    • 0025840476 scopus 로고
    • α-Glucuronidase and other hemicellulase activities of Fibrobacter succinogenes S85 grown on crystalline cellulose or ball-milled barley straw
    • Smith DC and Forsberg CW, α-Glucuronidase and other hemicellulase activities of Fibrobacter succinogenes S85 grown on crystalline cellulose or ball-milled barley straw. Appl Environ Microbiol 57:3552-3557 (1991).
    • (1991) Appl Environ Microbiol , vol.57 , pp. 3552-3557
    • Smith, D.C.1    Forsberg, C.W.2
  • 78
    • 0027048419 scopus 로고
    • Isolation of Clostridium acetobutylicum strains and the preliminary investigation of the hemicellulolytic activities of isolate 3BYR
    • Trudeau DG and Forsberg CW, Isolation of Clostridium acetobutylicum strains and the preliminary investigation of the hemicellulolytic activities of isolate 3BYR. Can J Microbiol 38:1120-1127 (1992).
    • (1992) Can J Microbiol , vol.38 , pp. 1120-1127
    • Trudeau, D.G.1    Forsberg, C.W.2
  • 79
    • 0031014417 scopus 로고    scopus 로고
    • Isolation and analysis of a gene encoding α-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan
    • Ruille P, Winterhalter C and Liebl W, Isolation and analysis of a gene encoding α-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan. Mol Microbiol 23:267-279 (1997).
    • (1997) Mol Microbiol , vol.23 , pp. 267-279
    • Ruille, P.1    Winterhalter, C.2    Liebl, W.3
  • 80
    • 0034669364 scopus 로고    scopus 로고
    • A chromogenic substrate for a β-xylosidase-coupled assay of β-glucuronidase
    • Biely P, Hirsch J, la Grange DC, van Zyl WH and Prior BA, A chromogenic substrate for a β-xylosidase-coupled assay of β-glucuronidase. Anal Biochem 286:289-294 (2000).
    • (2000) Anal Biochem , vol.286 , pp. 289-294
    • Biely, P.1    Hirsch, J.2    La Grange, D.C.3    Van Zyl, W.H.4    Prior, B.A.5
  • 81
    • 0037490140 scopus 로고    scopus 로고
    • The α-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants
    • Nagy T, Nurizzo D, Davies GJ, Biely P, Lakey JH and Bolam DN, et al, The α-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants. J Biol Chem 278:20286-20292 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 20286-20292
    • Nagy, T.1    Nurizzo, D.2    Davies, G.J.3    Biely, P.4    Lakey, J.H.5    Bolam, D.N.6
  • 82
    • 0021863774 scopus 로고
    • Acetylxylan esterases in fungal cellulolytic systems
    • Biely P, Puls J and Schneider H, Acetylxylan esterases in fungal cellulolytic systems. FEBS Lett 186:80-84 (1985).
    • (1985) FEBS Lett , vol.186 , pp. 80-84
    • Biely, P.1    Puls, J.2    Schneider, H.3
  • 83
    • 0027611199 scopus 로고
    • Esterases of xylan-degrading microorganisms: Production, properties, and significance
    • Christov LP and Prior BA, Esterases of xylan-degrading microorganisms: Production, properties, and significance. Enzyme Microb Technol 15:460-475 (1993).
    • (1993) Enzyme Microb Technol , vol.15 , pp. 460-475
    • Christov, L.P.1    Prior, B.A.2
  • 84
    • 0031662992 scopus 로고    scopus 로고
    • Hairy plant polysaccharides: A close shave with microbial esterases
    • Williamson G, Kroon PA and Faulds CB, Hairy plant polysaccharides: a close shave with microbial esterases. Microbiology 144:2011-2023 (1998).
    • (1998) Microbiology , vol.144 , pp. 2011-2023
    • Williamson, G.1    Kroon, P.A.2    Faulds, C.B.3
  • 85
    • 0023029475 scopus 로고
    • Cooperativity of esterases and xylanases in the enzymic degradation of acetyl xylan
    • Biely P, MacKenzie CR, Puls J and Schneider H, Cooperativity of esterases and xylanases in the enzymic degradation of acetyl xylan. Bio/Technology 4:731-733 (1986).
    • (1986) Bio/Technology , vol.4 , pp. 731-733
    • Biely, P.1    MacKenzie, C.R.2    Puls, J.3    Schneider, H.4
  • 86
  • 87
    • 0027415218 scopus 로고
    • Purification and characterization of an acetyl xylan esterase from Aspergillus niger
    • Kormelink FJM, Lefebvre B, Strozyk F and Voragen AGJ, Purification and characterization of an acetyl xylan esterase from Aspergillus niger. J Biotechnol 27:267-282 (1993).
    • (1993) J Biotechnol , vol.27 , pp. 267-282
    • Kormelink, F.J.M.1    Lefebvre, B.2    Strozyk, F.3    Voragen, A.G.J.4
  • 88
    • 0000834340 scopus 로고
    • Dimethylsulphoxide, a solvent for hemicelluloses
    • Hägglund E, Lindberg B and McPherson J, Dimethylsulphoxide, a solvent for hemicelluloses. Acta Chem Scand 10:1160-1164 (1956).
    • (1956) Acta Chem Scand , vol.10 , pp. 1160-1164
    • Hägglund, E.1    Lindberg, B.2    McPherson, J.3
  • 90
    • 45949126832 scopus 로고
    • Evaluation of different microbial xylanolytic systems
    • Poutanen K, Rättö M, Puls J and Viikari L, Evaluation of different microbial xylanolytic systems. J Biotechnol 6:49-60 (1987).
    • (1987) J Biotechnol , vol.6 , pp. 49-60
    • Poutanen, K.1    Rättö, M.2    Puls, J.3    Viikari, L.4
  • 91
    • 0025380341 scopus 로고
    • Comparison of natural hemicellulose and chemically acetylated xylan as substrates for the determination of acetyl-xylan esterase activity in Aspergilli
    • Khan AW, Lamb KA and Overend RP, Comparison of natural hemicellulose and chemically acetylated xylan as substrates for the determination of acetyl-xylan esterase activity in Aspergilli. Enzyme Microb Technol 12:127-131 (1990).
    • (1990) Enzyme Microb Technol , vol.12 , pp. 127-131
    • Khan, A.W.1    Lamb, K.A.2    Overend, R.P.3
  • 92
    • 0000090628 scopus 로고
    • Measurements of acetylxylan esterase in Streptomyces
    • Johnson KG, Fontana JD and MacKenzie CR, Measurements of acetylxylan esterase in Streptomyces. Methods Enzymol 160:551-560 (1988).
    • (1988) Methods Enzymol , vol.160 , pp. 551-560
    • Johnson, K.G.1    Fontana, J.D.2    MacKenzie, C.R.3
  • 93
    • 0000178854 scopus 로고
    • An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans
    • Tanen K and Sundberg M, An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans. Appl Microbiol Biotechnol 28:419-424 (1988).
    • (1988) Appl Microbiol Biotechnol , vol.28 , pp. 419-424
    • Tanen, K.1    Sundberg, M.2
  • 94
    • 0025017690 scopus 로고
    • Esterase activities of Fibrobacter succinogenes subsp. succinogenes S85
    • Dermid KP, MacKenzie CR and Forsberg CW, Esterase activities of Fibrobacter succinogenes subsp. succinogenes S85. Appl Environ Microbiol 56:127-132 (1990).
    • (1990) Appl Environ Microbiol , vol.56 , pp. 127-132
    • Dermid, K.P.1    MacKenzie, C.R.2    Forsberg, C.W.3
  • 96
    • 0038087618 scopus 로고    scopus 로고
    • Differences in catalytic properties of acetylxylan esterases and non-hemicellulolytic acetylesterases
    • ed. by Gilbert HJ, Davies GJ, Henrissat B and Svensson B. Royal Society of Chemistry, Cambridge
    • Biely P, Coté GL, Kremnicky L and Greene RV, Differences in catalytic properties of acetylxylan esterases and non-hemicellulolytic acetylesterases, in Recent Advances in Carbohydrate Bioengineering, ed. by Gilbert HJ, Davies GJ, Henrissat B and Svensson B. Royal Society of Chemistry, Cambridge, pp. 73-81 (1999).
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 73-81
    • Biely, P.1    Coté, G.L.2    Kremnicky, L.3    Greene, R.V.4
  • 97
    • 0012144539 scopus 로고    scopus 로고
    • Substrate specificity of acetylxylan esterase from Schizophyllum commune: Mode of action on acetylated carbohydrates
    • Biely P, Côté GL, Kremnický L, Weisleder D and Greene RV, Substrate specificity of acetylxylan esterase from Schizophyllum commune: mode of action on acetylated carbohydrates. Biochim Biophys Acta 1298:209-222 (1996).
    • (1996) Biochim Biophys Acta , vol.1298 , pp. 209-222
    • Biely, P.1    Côté, G.L.2    Kremnický, L.3    Weisleder, D.4    Greene, R.V.5
  • 98
    • 0030569312 scopus 로고    scopus 로고
    • Substrate specificity and mode of action of acetylxylan esterase from Streptomyces lividans
    • Biely P, Côté GL, Kremnický L, Greene RV, Dupont C and Kluepfel D, Substrate specificity and mode of action of acetylxylan esterase from Streptomyces lividans. FEBS Lett 396:257-260 (1996).
    • (1996) FEBS Lett , vol.396 , pp. 257-260
    • Biely, P.1    Côté, G.L.2    Kremnický, L.3    Greene, R.V.4    Dupont, C.5    Kluepfel, D.6
  • 99
    • 0141842967 scopus 로고    scopus 로고
    • Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families
    • ed. by Mansfield SD and Saddler JN. American Chemical Society, Washington, DC
    • Tenkanen M, Eyzaguirre J, Isoniemi R, Faulds CB, Biely P, Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families, in Applications of Enzymes to Lignocellulosics, ed. by Mansfield SD and Saddler JN. American Chemical Society, Washington, DC, pp. 211-229 (2003).
    • (2003) Applications of Enzymes to Lignocellulosics , pp. 211-229
    • Tenkanen, M.1    Eyzaguirre, J.2    Isoniemi, R.3    Faulds, C.B.4    Biely, P.5
  • 100
    • 0034465722 scopus 로고    scopus 로고
    • Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: Insight into the deacetylation mechanism
    • Hakulinen N, Tenkanen M and Rouvinen J, Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insight into the deacetylation mechanism. J Struct Biol 132:180-190 (2000).
    • (2000) J Struct Biol , vol.132 , pp. 180-190
    • Hakulinen, N.1    Tenkanen, M.2    Rouvinen, J.3
  • 101
    • 0035815705 scopus 로고    scopus 로고
    • Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 Å
    • Ghosh D, Sawicki M, Lala P, Erman M, Pangborn W, Eyzaguirre J, et al, Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 Å. J Biol Chem 276:11159-11166 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 11159-11166
    • Ghosh, D.1    Sawicki, M.2    Lala, P.3    Erman, M.4    Pangborn, W.5    Eyzaguirre, J.6
  • 102
    • 3342891457 scopus 로고    scopus 로고
    • Deoxy and deoxyfluoro analogues of acetylated methyl β-D- xylopyranoside - Substrates for acetylxylan esterases
    • Mastihubová M and Biely P, Deoxy and deoxyfluoro analogues of acetylated methyl β-D-xylopyranoside - substrates for acetylxylan esterases. Carbohydr Res 339:2101-2110 (2004).
    • (2004) Carbohydr Res , vol.339 , pp. 2101-2110
    • Mastihubová, M.1    Biely, P.2
  • 103
    • 2142715897 scopus 로고    scopus 로고
    • Lipase-catalysed preparation of acetates of 4-nitrophenyl β-D-xylopyranoside and their use in kinetic study of acetyl migration
    • Mastihubová M and Biely P, Lipase-catalysed preparation of acetates of 4-nitrophenyl β-D-xylopyranoside and their use in kinetic study of acetyl migration. Carbohydr Res 339:1353-1360 (2004).
    • (2004) Carbohydr Res , vol.339 , pp. 1353-1360
    • Mastihubová, M.1    Biely, P.2
  • 104
    • 4143116834 scopus 로고    scopus 로고
    • Enzyme-coupled assay of acetylxylan esterases on monoacetylated 4-nitrophenyl β-D-xylopyranosides
    • Biely P, Mastihubová M, la Grange DC, van Zyl WH and Prior BA, Enzyme-coupled assay of acetylxylan esterases on monoacetylated 4-nitrophenyl β-D-xylopyranosides. Anal Biochem 332:109-115 (2004).
    • (2004) Anal Biochem , vol.332 , pp. 109-115
    • Biely, P.1    Mastihubová, M.2    La Grange, D.C.3    Van Zyl, W.H.4    Prior, B.A.5
  • 105
    • 0025969260 scopus 로고
    • Purification and properties of two acetylxylan esterases of Trichoderma reesei
    • Sundberg M and Poutanen K, Purification and properties of two acetylxylan esterases of Trichoderma reesei. Biotechnol Appl Biochem 13:1-11 (1991).
    • (1991) Biotechnol Appl Biochem , vol.13 , pp. 1-11
    • Sundberg, M.1    Poutanen, K.2
  • 106
    • 0000990069 scopus 로고
    • Biodegradation of lignin-carbohydrate complexes
    • Jeffries T, Biodegradation of lignin-carbohydrate complexes. Biodegradation 1:163-176 (1990).
    • (1990) Biodegradation , vol.1 , pp. 163-176
    • Jeffries, T.1
  • 107
    • 0028712259 scopus 로고
    • Lignin-carbohydrate complexes in forages: Structure and consequences in the ruminal degradation of cell-wall carbohydrates
    • Cornu A, Besle JM, Mosoni P and Grenet E, Lignin-carbohydrate complexes in forages: structure and consequences in the ruminal degradation of cell-wall carbohydrates. Reprod Nutr Dev 34:385-398 (1994).
    • (1994) Reprod Nutr Dev , vol.34 , pp. 385-398
    • Cornu, A.1    Besle, J.M.2    Mosoni, P.3    Grenet, E.4
  • 108
    • 0030793569 scopus 로고    scopus 로고
    • Structure and functions of feruloylated polysaccharides
    • Ishii T, Structure and functions of feruloylated polysaccharides. Plant Sci 127:111-127 (1997).
    • (1997) Plant Sci , vol.127 , pp. 111-127
    • Ishii, T.1
  • 109
    • 0033059228 scopus 로고    scopus 로고
    • Ferulic acid and diferulic acid as components of sugar-beet pectins and maize bran heteroxylans
    • Saulnier L and Thibault J-F, Ferulic acid and diferulic acid as components of sugar-beet pectins and maize bran heteroxylans. J Sci Food Agric 79:396-402 (1999).
    • (1999) J Sci Food Agric , vol.79 , pp. 396-402
    • Saulnier, L.1    Thibault, J.-F.2
  • 110
    • 0025068644 scopus 로고
    • Feruloylated xyloglucan and p-coumaroyl arabinoxylan oligosaccharides from bamboo shoot cell walls
    • Ishii T, Hiroi T and Thomas JR, Feruloylated xyloglucan and p-coumaroyl arabinoxylan oligosaccharides from bamboo shoot cell walls. Phytochemistry 29:1999-2003 (1990).
    • (1990) Phytochemistry , vol.29 , pp. 1999-2003
    • Ishii, T.1    Hiroi, T.2    Thomas, J.R.3
  • 111
    • 0000506710 scopus 로고
    • Cross-linking of matrix polymers in the growing cell walls of angiosperms
    • Fry SC, Cross-linking of matrix polymers in the growing cell walls of angiosperms. Annu Rev Plant Physiol 37:165-186 (1986).
    • (1986) Annu Rev Plant Physiol , vol.37 , pp. 165-186
    • Fry, S.C.1
  • 112
    • 0000206036 scopus 로고
    • Phenolic bridges between polysaccharides and lignin in wheat internodes
    • Iiyama K, Lam TBT and Stone BA, Phenolic bridges between polysaccharides and lignin in wheat internodes. Phytochemistry 29:733-737 (1990).
    • (1990) Phytochemistry , vol.29 , pp. 733-737
    • Iiyama, K.1    Lam, T.B.T.2    Stone, B.A.3
  • 113
    • 0001835303 scopus 로고
    • Lignin/hydroxycinnamic acid polysaccharide complexes: Synthetic models for regiochemical characterization
    • ed. by Jun HG, Buxton DR, Hatfield RD and Ralph J. American Society for Agronomy - Crop Science Society of America - Soil Science Society of America, Madison
    • Ralph J and Helm RF, Lignin/hydroxycinnamic acid polysaccharide complexes: synthetic models for regiochemical characterization, in Forage Cell Wall Structure and Digestibility, ed. by Jun HG, Buxton DR, Hatfield RD and Ralph J. American Society for Agronomy - Crop Science Society of America - Soil Science Society of America, Madison, pp. 119-127 (1992).
    • (1992) Forage Cell Wall Structure and Digestibility , pp. 119-127
    • Ralph, J.1    Helm, R.F.2
  • 114
    • 0035800179 scopus 로고    scopus 로고
    • Bonding of hydroxycinnamic acids to lignin: Ferulic and p-coumaric acids are predominantly linked at the benzyl position of lignin, not the β-position, in grass cell walls
    • Lam TBT, Kadoya K and Iiyama K, Bonding of hydroxycinnamic acids to lignin: ferulic and p-coumaric acids are predominantly linked at the benzyl position of lignin, not the β-position, in grass cell walls. Phytochemistry 57:987-992 (2001).
    • (2001) Phytochemistry , vol.57 , pp. 987-992
    • Lam, T.B.T.1    Kadoya, K.2    Iiyama, K.3
  • 115
    • 0001220718 scopus 로고
    • Induction of cellulolytic and xylanolytic enzyme systems in Streptomyces spp.
    • MacKenzie CR, Bilous D, Schneider H and Johnson KG, Induction of cellulolytic and xylanolytic enzyme systems in Streptomyces spp. Appl Environ Microbiol 53:2835-2839 (1987).
    • (1987) Appl Environ Microbiol , vol.53 , pp. 2835-2839
    • MacKenzie, C.R.1    Bilous, D.2    Schneider, H.3    Johnson, K.G.4
  • 117
    • 14544304535 scopus 로고    scopus 로고
    • Sporotrichum thermophile type C feruloyl esterase (StFaeC): Purification, characterization, and its use for phenolic acid (sugar) ester synthesis
    • Topakas E, Vafiadi C, Stamatis H and Christakopoulos P, Sporotrichum thermophile type C feruloyl esterase (StFaeC): purification, characterization, and its use for phenolic acid (sugar) ester synthesis. Enzyme Microb Technol 36:729-736 (2005).
    • (2005) Enzyme Microb Technol , vol.36 , pp. 729-736
    • Topakas, E.1    Vafiadi, C.2    Stamatis, H.3    Christakopoulos, P.4
  • 118
    • 33747106943 scopus 로고    scopus 로고
    • Microbial hemicellulolytic carbohydrate esterases
    • ed. by Hou CT. Taylor & Francis Group, Boca Raton, USA
    • Biely P and Côté GL, Microbial hemicellulolytic carbohydrate esterases, in Handbook of Industrial Biocatalysis, ed. by Hou CT. Taylor & Francis Group, Boca Raton, USA. pp. 21-1-21-24 (2005).
    • (2005) Handbook of Industrial Biocatalysis , pp. 211-2124
    • Biely, P.1    Côté, G.L.2
  • 119
    • 0033485928 scopus 로고    scopus 로고
    • A cinnamoyl esterase from Aspergillus niger can break plant cell wall cross-links without release of free diferulic acid
    • Garcia-Conesa M-T, Kroon PA, Ralph J, Mellon FA, Colquhoun IJ, Saulnier L, et al, A cinnamoyl esterase from Aspergillus niger can break plant cell wall cross-links without release of free diferulic acid. Eur J Biochem 266:644-652 (1999).
    • (1999) Eur J Biochem , vol.266 , pp. 644-652
    • Garcia-Conesa, M.-T.1    Kroon, P.A.2    Ralph, J.3    Mellon, F.A.4    Colquhoun, I.J.5    Saulnier, L.6
  • 121
    • 0028518891 scopus 로고
    • Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger
    • Ralet M-C, Faulds CB, Williamson G and Thibault J-F, Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger. Carbohydr Res 263:257-269 (1994).
    • (1994) Carbohydr Res , vol.263 , pp. 257-269
    • Ralet, M.-C.1    Faulds, C.B.2    Williamson, G.3    Thibault, J.-F.4
  • 122
    • 0025012288 scopus 로고
    • Assay for trans-coumaroyl esterase using a specific substrate from plant cell walls
    • Borneman WS, Hartley RD, Himmelsbach DS and Ljungdahl LG, Assay for trans-coumaroyl esterase using a specific substrate from plant cell walls. Anal Biochem 190:129-133 (1990).
    • (1990) Anal Biochem , vol.190 , pp. 129-133
    • Borneman, W.S.1    Hartley, R.D.2    Himmelsbach, D.S.3    Ljungdahl, L.G.4
  • 123
    • 0026448264 scopus 로고
    • Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2
    • Borneman WS, Ljungdahl LG, Hartley RD and Akin DE, Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2. Appl Environ Microbiol 58:3762-3766 (1992).
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3762-3766
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 124
    • 0028518976 scopus 로고
    • Isolation and purification of feruloylated oligosaccharides from cell walls of sugar-beet pulp
    • Ralet MC, Thibault J-F, Faulds CB and Williamson G, Isolation and purification of feruloylated oligosaccharides from cell walls of sugar-beet pulp. Carbohydr Res 263:227-241 (1994).
    • (1994) Carbohydr Res , vol.263 , pp. 227-241
    • Ralet, M.C.1    Thibault, J.-F.2    Faulds, C.B.3    Williamson, G.4
  • 125
    • 0031009608 scopus 로고    scopus 로고
    • Process for isolation of preparative quantities of [2-O-(trans-feruloyl)- α-L-arabinofuranosyl]-(1 → 5)-L-arabinofuranose from sugarbeet
    • Kroon PA, Garcia-Conesa M-T, Colquhoun IJ and Williamson G, Process for isolation of preparative quantities of [2-O-(trans-feruloyl)-α-L- arabinofuranosyl]-(1 → 5)-L-arabinofuranose from sugarbeet. Carbohydr Res 300:351-354 (1997).
    • (1997) Carbohydr Res , vol.300 , pp. 351-354
    • Kroon, P.A.1    Garcia-Conesa, M.-T.2    Colquhoun, I.J.3    Williamson, G.4
  • 126
    • 0026201162 scopus 로고
    • Spectrophotometric assay and electrophoretic detection of trans-feruloyl esterase activity
    • McCallum JA, Taylor IEP and Towers GHN, Spectrophotometric assay and electrophoretic detection of trans-feruloyl esterase activity. Anal Biochem 196:360-366 (1991).
    • (1991) Anal Biochem , vol.196 , pp. 360-366
    • McCallum, J.A.1    Taylor, I.E.P.2    Towers, G.H.N.3
  • 127
    • 0030909862 scopus 로고    scopus 로고
    • Structures of ferulic acid glycoside esters in corn hulls
    • Hosny M and Rosazza JPN, Structures of ferulic acid glycoside esters in corn hulls. J Nat Prod 60:219-222 (1997).
    • (1997) J Nat Prod , vol.60 , pp. 219-222
    • Hosny, M.1    Rosazza, J.P.N.2
  • 128
    • 0037222888 scopus 로고    scopus 로고
    • Enzymic production of a feruloylated oligosaccharide with antioxidant activity from wheat flour arabinoxylan
    • Katapodis P, Vardakou M, Kalogeris E, Kekos D, Macris BJ and Christakopoulos P, et al, Enzymic production of a feruloylated oligosaccharide with antioxidant activity from wheat flour arabinoxylan, Eur J Nutr 42:55-60 (2003).
    • (2003) Eur J Nutr , vol.42 , pp. 55-60
    • Katapodis, P.1    Vardakou, M.2    Kalogeris, E.3    Kekos, D.4    Macris, B.J.5    Christakopoulos, P.6
  • 129
    • 33746900062 scopus 로고    scopus 로고
    • Feruloyl esterases
    • ed. by Whitaker JR, Voragen AGJ and Wong DWS. Marcel Dekker Inc., New York, Basel
    • Faulds CB and Williamson G, Feruloyl esterases, in Handbook of Food Enzymology, ed. by Whitaker JR, Voragen AGJ and Wong DWS. Marcel Dekker Inc., New York, Basel, pp. 657-666 (2003).
    • (2003) Handbook of Food Enzymology , pp. 657-666
    • Faulds, C.B.1    Williamson, G.2
  • 132
    • 0037450492 scopus 로고    scopus 로고
    • Two efficient ways to 2- and 5-feruloylated 4-nitrophenyl α-L-arabinofuranosides as substrates for differentiation of feruloyl esterases
    • Mastihubová M, Szemesová J and Biely P, Two efficient ways to 2- and 5-feruloylated 4-nitrophenyl α-L-arabinofuranosides as substrates for differentiation of feruloyl esterases, Tetrahedron Lett 44:1671-1673 (2003).
    • (2003) Tetrahedron Lett , vol.44 , pp. 1671-1673
    • Mastihubová, M.1    Szemesová, J.2    Biely, P.3
  • 133
    • 0036901753 scopus 로고    scopus 로고
    • Differentiation of feruloyl esterases on synthetic substrates in α-arabinofuranosidase-coupled and ultraviolet-spectrophotometric assay
    • Biely P, Mastihubová M, van Zyl WH and Prior BA, Differentiation of feruloyl esterases on synthetic substrates in α-arabinofuranosidase- coupled and ultraviolet-spectrophotometric assay, Anal Biochem 311:68-75 (2002).
    • (2002) Anal Biochem , vol.311 , pp. 68-75
    • Biely, P.1    Mastihubová, M.2    Van Zyl, W.H.3    Prior, B.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.