메뉴 건너뛰기




Volumn 214, Issue , 2017, Pages 423-431

Aggregation and conformational change of mushroom (Agaricus bisporus) polyphenoloxidase subjected to thermal treatment

Author keywords

Aggregation; Conformation; Inactivation; Microstructure; Polyphenoloxidase; Thermal treatment

Indexed keywords

AGGLOMERATION; DICHROISM; FLUORESCENCE; HEAT TREATMENT; MICROSTRUCTURE;

EID: 84978640093     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.07.041     Document Type: Article
Times cited : (51)

References (37)
  • 2
    • 84928493730 scopus 로고    scopus 로고
    • Effect of thermal treatment on secondary structure and conformational change of mushroom polyphenol oxidase (PPO) as food quality related enzyme: A FTIR study
    • Baltacioglu, H., Bayindirli, A., Severcan, M., Severcan, F., Effect of thermal treatment on secondary structure and conformational change of mushroom polyphenol oxidase (PPO) as food quality related enzyme: A FTIR study. Food Chemistry 187 (2015), 263–269.
    • (2015) Food Chemistry , vol.187 , pp. 263-269
    • Baltacioglu, H.1    Bayindirli, A.2    Severcan, M.3    Severcan, F.4
  • 3
    • 84870254687 scopus 로고    scopus 로고
    • The inactivation kinetics of polyphenol oxidase in mushroom (Agaricus bisporus) during thermal and thermosonic treatments
    • Cheng, X.F., Zhang, M., Adhikari, B., The inactivation kinetics of polyphenol oxidase in mushroom (Agaricus bisporus) during thermal and thermosonic treatments. Ultrasonics Sonochemistry 20 (2013), 649–674.
    • (2013) Ultrasonics Sonochemistry , vol.20 , pp. 649-674
    • Cheng, X.F.1    Zhang, M.2    Adhikari, B.3
  • 4
    • 84923359255 scopus 로고    scopus 로고
    • Pre-heating and polyphenol oxidase inhibition impact on extraction of purple sweet potato anthocyanins
    • de Aguiar Cipriano, P., Ekici, L., Barnes, R.C., Gomes, C., Talcott, S.T., Pre-heating and polyphenol oxidase inhibition impact on extraction of purple sweet potato anthocyanins. Food Chemistry 180 (2015), 227–234.
    • (2015) Food Chemistry , vol.180 , pp. 227-234
    • de Aguiar Cipriano, P.1    Ekici, L.2    Barnes, R.C.3    Gomes, C.4    Talcott, S.T.5
  • 7
    • 0034003094 scopus 로고    scopus 로고
    • Resolution of ligand positions by site-directed tryptophan fluorescence in tear lipocalin
    • Gasymov, O.K., Abduragimov, A.R., Yusifov, T.N., Glasgow, B.J., Resolution of ligand positions by site-directed tryptophan fluorescence in tear lipocalin. Protein Science 9 (2000), 325–331.
    • (2000) Protein Science , vol.9 , pp. 325-331
    • Gasymov, O.K.1    Abduragimov, A.R.2    Yusifov, T.N.3    Glasgow, B.J.4
  • 8
    • 84855814116 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of the thermal inactivation of polyphenol oxidase in an aqueous extract from Agaricus bisporus
    • Gouzi, H., Depagne, C., Coradin, T., Kinetics and thermodynamics of the thermal inactivation of polyphenol oxidase in an aqueous extract from Agaricus bisporus. Journal of Agricultural and Food Chemistry 60 (2012), 500–506.
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , pp. 500-506
    • Gouzi, H.1    Depagne, C.2    Coradin, T.3
  • 9
    • 84879779757 scopus 로고    scopus 로고
    • Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
    • Goyeneche, R., Di Scala, K., Roura, S., Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus). LWT – Food Science and Technology 54 (2013), 57–62.
    • (2013) LWT – Food Science and Technology , vol.54 , pp. 57-62
    • Goyeneche, R.1    Di Scala, K.2    Roura, S.3
  • 10
    • 0032939813 scopus 로고    scopus 로고
    • Applications of circular dichroism in protein and peptide analysis
    • Greenfield, N.J., Applications of circular dichroism in protein and peptide analysis. TrAC – Trends Analytical Chemistry 18 (1999), 236–244.
    • (1999) TrAC – Trends Analytical Chemistry , vol.18 , pp. 236-244
    • Greenfield, N.J.1
  • 11
    • 79952740870 scopus 로고    scopus 로고
    • Aggregation and homogenization, surface charge and structural change, and inactivation of mushroom tyrosinase in an aqueous system by subcritical/supercritical carbon dioxide
    • Hu, W.F., Zhang, Y., Wang, Y.Y., Zhou, L.Y., Leng, X.J., Liao, X.J., et al. Aggregation and homogenization, surface charge and structural change, and inactivation of mushroom tyrosinase in an aqueous system by subcritical/supercritical carbon dioxide. Langmuir 27 (2011), 909–916.
    • (2011) Langmuir , vol.27 , pp. 909-916
    • Hu, W.F.1    Zhang, Y.2    Wang, Y.Y.3    Zhou, L.Y.4    Leng, X.J.5    Liao, X.J.6
  • 12
    • 84896725734 scopus 로고    scopus 로고
    • Advances in structure-function relationships of tyrosinase from Agaricus bisporus – Investigation on heat-induced conformational changes
    • Ionita, E., Aprodu, I., Stanciuc, N., Rapeanu, G., Bahrim, G., Advances in structure-function relationships of tyrosinase from Agaricus bisporus – Investigation on heat-induced conformational changes. Food Chemistry 156 (2014), 129–136.
    • (2014) Food Chemistry , vol.156 , pp. 129-136
    • Ionita, E.1    Aprodu, I.2    Stanciuc, N.3    Rapeanu, G.4    Bahrim, G.5
  • 13
    • 79959257956 scopus 로고    scopus 로고
    • Crystal structure of Agaricus bisporus mushroom tyrosinase: Identity of the tetramer subunits and interaction with tropolone
    • Ismaya, W.T., Rozeboom, H.J., Weijn, A., Mes, J.J., Fusetti, F., Wichers, H.J., et al. Crystal structure of Agaricus bisporus mushroom tyrosinase: Identity of the tetramer subunits and interaction with tropolone. Biochemistry 50 (2011), 5477–5486.
    • (2011) Biochemistry , vol.50 , pp. 5477-5486
    • Ismaya, W.T.1    Rozeboom, H.J.2    Weijn, A.3    Mes, J.J.4    Fusetti, F.5    Wichers, H.J.6
  • 15
    • 0000260537 scopus 로고
    • Modification of biopolymer functions by high pressure
    • Kunugi, S., Modification of biopolymer functions by high pressure. Progress in Polymer Science 18 (1993), 805–838.
    • (1993) Progress in Polymer Science , vol.18 , pp. 805-838
    • Kunugi, S.1
  • 16
    • 84929458631 scopus 로고    scopus 로고
    • Influence of denaturation and aggregation of β-lactoglobulin on its tryptic hydrolysis and the release of functional peptides
    • Leeb, E., Gotz, A., Letzel, T., Cheison, S.C., Kulozik, U., Influence of denaturation and aggregation of β-lactoglobulin on its tryptic hydrolysis and the release of functional peptides. Food Chemistry 187 (2015), 545–554.
    • (2015) Food Chemistry , vol.187 , pp. 545-554
    • Leeb, E.1    Gotz, A.2    Letzel, T.3    Cheison, S.C.4    Kulozik, U.5
  • 17
    • 84905044452 scopus 로고    scopus 로고
    • Pectin plays an important role on the kinetics properties of polyphenol oxidase from honeydew peach
    • Liu, L., Cao, S.Q., Yang, H., Qi, X.Y., Pectin plays an important role on the kinetics properties of polyphenol oxidase from honeydew peach. Food Chemistry 168 (2015), 14–20.
    • (2015) Food Chemistry , vol.168 , pp. 14-20
    • Liu, L.1    Cao, S.Q.2    Yang, H.3    Qi, X.Y.4
  • 18
    • 84930225982 scopus 로고    scopus 로고
    • Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-shifting and mild heating processes
    • Liu, Q., Geng, R., Zhao, J.Y., Chen, Q., Kong, B.H., Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-shifting and mild heating processes. Journal of Agricultural and Food Chemistry 63 (2015), 4853–4861.
    • (2015) Journal of Agricultural and Food Chemistry , vol.63 , pp. 4853-4861
    • Liu, Q.1    Geng, R.2    Zhao, J.Y.3    Chen, Q.4    Kong, B.H.5
  • 19
    • 60149099551 scopus 로고    scopus 로고
    • Activation and conformational changes of mushroom polyphenoloxidase by high pressure microfluidization treatment
    • Liu, W., Liu, J.H., Liu, C.M., Zhong, Y.J., Liu, W.L., Wan, J., Activation and conformational changes of mushroom polyphenoloxidase by high pressure microfluidization treatment. Innovative Food Science and Emerging Technologies 10 (2009), 142–147.
    • (2009) Innovative Food Science and Emerging Technologies , vol.10 , pp. 142-147
    • Liu, W.1    Liu, J.H.2    Liu, C.M.3    Zhong, Y.J.4    Liu, W.L.5    Wan, J.6
  • 20
    • 67649210997 scopus 로고    scopus 로고
    • Characterization and high-pressure microfluidization-induced activation of polyphenoloxidase from Chinese pear (Pyrus pyrifolia Nakai)
    • Liu, W., Liu, J.H., Xie, M.Y., Liu, C.M., Liu, W.L., Wan, J., Characterization and high-pressure microfluidization-induced activation of polyphenoloxidase from Chinese pear (Pyrus pyrifolia Nakai). Journal of Agricultural and Food Chemistry 57 (2009), 5376–5380.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 5376-5380
    • Liu, W.1    Liu, J.H.2    Xie, M.Y.3    Liu, C.M.4    Liu, W.L.5    Wan, J.6
  • 21
    • 84875036426 scopus 로고    scopus 로고
    • The effect of citric acid on the activity, thermodynamics and conformation of mushroom polyphenoloxidase
    • Liu, W., Zou, L.Q., Liu, J.P., Zhang, Z.Q., Liu, C.M., Liang, R.H., The effect of citric acid on the activity, thermodynamics and conformation of mushroom polyphenoloxidase. Food Chemistry 140 (2013), 289–295.
    • (2013) Food Chemistry , vol.140 , pp. 289-295
    • Liu, W.1    Zou, L.Q.2    Liu, J.P.3    Zhang, Z.Q.4    Liu, C.M.5    Liang, R.H.6
  • 23
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • Mayer, A.M., Polyphenol oxidases in plants and fungi: Going places? A review. Phytochemistry 67 (2006), 2318–2331.
    • (2006) Phytochemistry , vol.67 , pp. 2318-2331
    • Mayer, A.M.1
  • 24
    • 0037559368 scopus 로고    scopus 로고
    • Effect of nonthermal treatment on the molecular properties of mushroom polyphenoloxidase
    • Sun, N., Song, K., Effect of nonthermal treatment on the molecular properties of mushroom polyphenoloxidase. Journal of Food Science 68 (2003), 1639–1643.
    • (2003) Journal of Food Science , vol.68 , pp. 1639-1643
    • Sun, N.1    Song, K.2
  • 25
    • 84928975581 scopus 로고    scopus 로고
    • Blueberry polyphenol oxidase: Characterization and the kinetics of thermal and high pressure activation and inactivation
    • Terefe, N.S., Delon, A., Buckow, R., Versteeg, C., Blueberry polyphenol oxidase: Characterization and the kinetics of thermal and high pressure activation and inactivation. Food Chemistry 188 (2015), 193–200.
    • (2015) Food Chemistry , vol.188 , pp. 193-200
    • Terefe, N.S.1    Delon, A.2    Buckow, R.3    Versteeg, C.4
  • 26
    • 0031073439 scopus 로고    scopus 로고
    • Biocatalysis by tyrosinase in organic solvent media; A model system using catechin and vanillin as substrates
    • Tse, M., Kermasha, S., Ismail, A., Biocatalysis by tyrosinase in organic solvent media; A model system using catechin and vanillin as substrates. Journal of Molecular Catalysis B: Enzymatic 2 (1997), 199–213.
    • (1997) Journal of Molecular Catalysis B: Enzymatic , vol.2 , pp. 199-213
    • Tse, M.1    Kermasha, S.2    Ismail, A.3
  • 29
    • 84901302578 scopus 로고    scopus 로고
    • Inhibitory effect of morin on tyrosinase: Insights from spectroscopic and molecular docking studies
    • Wang, Y.J., Zhang, G.W., Yan, J.K., Gong, D.M., Inhibitory effect of morin on tyrosinase: Insights from spectroscopic and molecular docking studies. Food Chemistry 163 (2014), 226–233.
    • (2014) Food Chemistry , vol.163 , pp. 226-233
    • Wang, Y.J.1    Zhang, G.W.2    Yan, J.K.3    Gong, D.M.4
  • 30
    • 84862950867 scopus 로고    scopus 로고
    • Effect of ultrahigh hydrostatic pressure on the activity and structure of mushroom (Agaricus bisporus) polyphenoloxidase
    • Yi, J.Y., Jiang, B., Zhang, Z., Liao, X.J., Zhang, Y., Hu, X.S., Effect of ultrahigh hydrostatic pressure on the activity and structure of mushroom (Agaricus bisporus) polyphenoloxidase. Journal of Agricultural and Food Chemistry 60 (2012), 593–599.
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , pp. 593-599
    • Yi, J.Y.1    Jiang, B.2    Zhang, Z.3    Liao, X.J.4    Zhang, Y.5    Hu, X.S.6
  • 31
    • 84922334659 scopus 로고    scopus 로고
    • Effect of high-hydrostatic-pressure on molecular microstructure of mushroom (Agaricusbisporus) polyphenoloxidase
    • Yi, J.J., Yi, J.Y., Dong, P., Liao, X.J., Hu, X.S., Zhang, Y., Effect of high-hydrostatic-pressure on molecular microstructure of mushroom (Agaricusbisporus) polyphenoloxidase. LWT – Food Science and Technology 60 (2015), 890–898.
    • (2015) LWT – Food Science and Technology , vol.60 , pp. 890-898
    • Yi, J.J.1    Yi, J.Y.2    Dong, P.3    Liao, X.J.4    Hu, X.S.5    Zhang, Y.6
  • 32
    • 84872609984 scopus 로고    scopus 로고
    • Influence of ultrasound to the activity of tyrosinase
    • Yu, Z.L., Zeng, W.C., Lu, X.L., Influence of ultrasound to the activity of tyrosinase. Ultrasonics Sonochemistry 20 (2013), 805–809.
    • (2013) Ultrasonics Sonochemistry , vol.20 , pp. 805-809
    • Yu, Z.L.1    Zeng, W.C.2    Lu, X.L.3
  • 33
    • 84864053225 scopus 로고    scopus 로고
    • Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity
    • Zhong, J.Z., Liu, W., Liu, C.M., Wang, Q.H., Li, T., Tu, Z.C., et al. Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity. Journal of Dairy Science 95 (2012), 4237–4245.
    • (2012) Journal of Dairy Science , vol.95 , pp. 4237-4245
    • Zhong, J.Z.1    Liu, W.2    Liu, C.M.3    Wang, Q.H.4    Li, T.5    Tu, Z.C.6
  • 34
    • 33745186912 scopus 로고    scopus 로고
    • Inactivation kinetics and secondary structural change of PEF-treated POD and PPO
    • Zhong, K., Wu, J.H., Wang, Z.F., Chen, F., Liao, X.J., Hu, X.S., et al. Inactivation kinetics and secondary structural change of PEF-treated POD and PPO. Food Chemistry 100 (2007), 115–123.
    • (2007) Food Chemistry , vol.100 , pp. 115-123
    • Zhong, K.1    Wu, J.H.2    Wang, Z.F.3    Chen, F.4    Liao, X.J.5    Hu, X.S.6
  • 35
    • 84988484374 scopus 로고    scopus 로고
    • Different modes of inhibition for organic acids on polyphenoloxidase
    • Zhou, L., Liu, W., Xiong, Z.Q., Zou, L.Q., Chen, J., Liu, J.P., et al. Different modes of inhibition for organic acids on polyphenoloxidase. Food Chemistry 199 (2016), 439–446.
    • (2016) Food Chemistry , vol.199 , pp. 439-446
    • Zhou, L.1    Liu, W.2    Xiong, Z.Q.3    Zou, L.Q.4    Chen, J.5    Liu, J.P.6
  • 36
    • 64549141148 scopus 로고    scopus 로고
    • Alterations in the activity and structure of pectin methylesterase treated by high pressure carbon dioxide
    • Zhou, L.Y., Wu, J.H., Hu, X.S., Zhi, X., Liao, X.J., Alterations in the activity and structure of pectin methylesterase treated by high pressure carbon dioxide. Journal of Agricultural and Food Chemistry 57 (2009), 1890–1895.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 1890-1895
    • Zhou, L.Y.1    Wu, J.H.2    Hu, X.S.3    Zhi, X.4    Liao, X.J.5
  • 37
    • 84893483332 scopus 로고    scopus 로고
    • Characterization and bioavailability of tea polyphenol nanoliposome prepared by combining an ethanol injection method with dynamic high-pressure microfluidization
    • Zou, L.Q., Liu, W., Liu, W.L., Liang, R.H., Li, T., Liu, C.M., et al. Characterization and bioavailability of tea polyphenol nanoliposome prepared by combining an ethanol injection method with dynamic high-pressure microfluidization. Journal of Agricultural and Food Chemistry 62 (2014), 934–941.
    • (2014) Journal of Agricultural and Food Chemistry , vol.62 , pp. 934-941
    • Zou, L.Q.1    Liu, W.2    Liu, W.L.3    Liang, R.H.4    Li, T.5    Liu, C.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.