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Volumn 6, Issue JUN, 2018, Pages

Aggregation and conformational changes in native and thermally treated polyphenol oxidase from apple juice (Malus domestica)

Author keywords

Activity center; Aggregation; Catechol; Conformation; Pyrogallol; Thermal processing (TP); max

Indexed keywords


EID: 85050358866     PISSN: None     EISSN: 22962646     Source Type: Journal    
DOI: 10.3389/fchem.2018.00203     Document Type: Article
Times cited : (42)

References (41)
  • 1
    • 84867478435 scopus 로고    scopus 로고
    • Biochemical and structural changes of taro (Colocasia esculenta) tubers during simple thermal treatments (low temperature) or in combination with chemicals
    • Aboubakar, B. C., Râpeanu, G., Njintang, N. Y., Mbofung, C. M., and Bahrim, G. (2012). Biochemical and structural changes of taro (Colocasia esculenta) tubers during simple thermal treatments (low temperature) or in combination with chemicals. Food Bioprocess Technol. 5, 2739-2747. doi: 10.1007/s11947-011-0622-7
    • (2012) Food Bioprocess Technol , vol.5 , pp. 2739-2747
    • Aboubakar, B.C.1    Râpeanu, G.2    Njintang, N.Y.3    Mbofung, C.M.4    Bahrim, G.5
  • 3
    • 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., and Severcan, F. (2015). Effect of thermal treatment on secondary structure and conformational change of mushroom polyphenol oxidase (PPO) as food quality related enzyme: a FTIR study. Food Chem. 187, 263-269. doi: 10.1016/j.foodchem.2015.04.097
    • (2015) Food Chem , vol.187 , pp. 263-269
    • Baltacioglu, H.1    Bayindirli, A.2    Severcan, M.3    Severcan, F.4
  • 4
    • 0037447846 scopus 로고    scopus 로고
    • Detection and prevention of protein aggregation before, during, and after purification
    • Bondos, S. E., and Bicknell, A. (2003). Detection and prevention of protein aggregation before, during, and after purification. Anal. Biochem. 316, 223-231. doi: 10.1016/S0003-2697(03)00059-9
    • (2003) Anal. Biochem , vol.316 , pp. 223-231
    • Bondos, S.E.1    Bicknell, A.2
  • 5
    • 68949170818 scopus 로고    scopus 로고
    • Inactivation kinetics of apple polyphenol oxidase in different pressure-temperature domains
    • Buckow, R., Weiss, U., and Knorr, D. (2009). Inactivation kinetics of apple polyphenol oxidase in different pressure-temperature domains. Innov. Food Sci. Emerg. Technol. 10, 441-448. doi: 10.1016/j.ifset.2009.05.005
    • (2009) Innov. Food Sci. Emerg. Technol , vol.10 , pp. 441-448
    • Buckow, R.1    Weiss, U.2    Knorr, D.3
  • 6
    • 79956344900 scopus 로고    scopus 로고
    • Ultrasonics sonochemistry effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate
    • Chandrapala, J., Zisu, B., Palmer, M., Kentish, S., and Ashokkumar, M. (2011). Ultrasonics sonochemistry effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrason 18, 951-957. doi: 10.1016/j.ultsonch.2010.12.016
    • (2011) Ultrason , vol.18 , pp. 951-957
    • Chandrapala, J.1    Zisu, B.2    Palmer, M.3    Kentish, S.4    Ashokkumar, M.5
  • 7
    • 0035824433 scopus 로고    scopus 로고
    • Hysteresis and positive cooperativity of iceberg lettuce polyphenol oxidase
    • Chazarra, S., García-Carmona, F., and Cabanes, J. (2001). Hysteresis and positive cooperativity of iceberg lettuce polyphenol oxidase. Biochem. Biophys. Res. Commun. 289, 769-775. doi: 10.1006/bbrc.2001.6014
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 769-775
    • Chazarra, S.1    García-Carmona, F.2    Cabanes, J.3
  • 8
    • 84902194771 scopus 로고    scopus 로고
    • Characterization of germin-like protein with polyphenol oxidase activity from Satsuma mandarine
    • Cheng, X., Huang, X., Liu, S., Tang, M., Hu, W., and Pan, S. (2014). Characterization of germin-like protein with polyphenol oxidase activity from Satsuma mandarine. Biochem. Biophys. Res. Commun. 449, 313-318. doi: 10.1016/j.bbrc.2014.05.027
    • (2014) Biochem. Biophys. Res. Commun , vol.449 , pp. 313-318
    • Cheng, X.1    Huang, X.2    Liu, S.3    Tang, M.4    Hu, W.5    Pan, S.6
  • 9
    • 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., and Talcott, S. T. (2015). Pre-heating and polyphenol oxidase inhibition impact on extraction of purple sweet potato anthocyanins. Food Chem. 180, 227-234. doi: 10.1016/j.foodchem.2015.02.020
    • (2015) Food Chem , vol.180 , pp. 227-234
    • De Aguiar Cipriano, P.1    Ekici, L.2    Barnes, R.C.3    Gomes, C.4    Talcott, S.T.5
  • 10
    • 33746291588 scopus 로고    scopus 로고
    • The first crystal structure of tyrosinase: all questions answered?
    • Decker, H., Schweikardt, T., and Tuczek, F. (2006). The first crystal structure of tyrosinase: all questions answered? Angew. Chemie Int. Ed. 45, 4546-4550. doi: 10.1002/anie.200601255
    • (2006) Angew. Chemie Int. Ed , vol.45 , pp. 4546-4550
    • Decker, H.1    Schweikardt, T.2    Tuczek, F.3
  • 11
  • 12
    • 26844559400 scopus 로고    scopus 로고
    • Evidence for a common regulation in the activation of a polyphenol oxidase by trypsin and sodium dodecyl sulfate
    • Gandía-Herrero, F., Jiménez-Atiénzar, M., Cabanes, J., García-Carmona, F., and Escribano, J. (2005). Evidence for a common regulation in the activation of a polyphenol oxidase by trypsin and sodium dodecyl sulfate. Biol. Chem. 386, 601-607. doi: 10.1515/BC.2005.070
    • (2005) Biol. Chem , vol.386 , pp. 601-607
    • Gandía-Herrero, F.1    Jiménez-Atiénzar, M.2    Cabanes, J.3    García-Carmona, F.4    Escribano, J.5
  • 13
    • 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., and Coradin, T. (2012). Kinetics and thermodynamics of the thermal inactivation of polyphenol oxidase in an aqueous extract from Agaricus bisporus. J. Agric. Food Chem. 60, 500-506. doi: 10.1021/jf204104g
    • (2012) J. Agric. Food Chem , vol.60 , pp. 500-506
    • Gouzi, H.1    Depagne, C.2    Coradin, T.3
  • 14
    • 84879779757 scopus 로고    scopus 로고
    • Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus)
    • Goyeneche, R., Di Scala, K., and Roura, S. (2013). Biochemical characterization and thermal inactivation of polyphenol oxidase from radish (Raphanus sativus var. sativus). LWT Food Sci. Technol. 54, 57-62. doi: 10.1016/j.lwt.2013.04.014
    • (2013) LWT Food Sci. Technol , vol.54 , pp. 57-62
    • Goyeneche, R.1    Di Scala, K.2    Roura, S.3
  • 15
    • 84918500919 scopus 로고    scopus 로고
    • Inactivation, aggregation, secondary and tertiary structural changes of germin-like protein in Satsuma mandarine with high polyphenol oxidase activity induced by ultrasonic processing
    • Huang, N., Cheng, X., Hu, W., and Pan, S. (2015). Inactivation, aggregation, secondary and tertiary structural changes of germin-like protein in Satsuma mandarine with high polyphenol oxidase activity induced by ultrasonic processing. Biophys. Chem. 197, 18-24. doi: 10.1016/j.bpc.2014.12.001
    • (2015) Biophys. Chem , vol.197 , pp. 18-24
    • Huang, N.1    Cheng, X.2    Hu, W.3    Pan, S.4
  • 16
    • 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., Râpeanu, G., and Bahrim, G. (2014). Advances in structure-function relationships of tyrosinase from Agaricus bisporus-Investigation on heat-induced conformational changes. Food Chem. 156, 129-136. doi: 10.1016/j.foodchem.2014.01.089
    • (2014) Food Chem , vol.156 , pp. 129-136
    • Ionita, E.1    Aprodu, I.2    Stanciuc, N.3    Râpeanu, G.4    Bahrim, G.5
  • 17
    • 77955772490 scopus 로고    scopus 로고
    • Inhibition of polyphenol oxidase and peroxidase activities on fresh-cut apple by simultaneous treatment of ultrasound and ascorbic acid
    • Jang, J. H., and Moon, K. D. (2011). Inhibition of polyphenol oxidase and peroxidase activities on fresh-cut apple by simultaneous treatment of ultrasound and ascorbic acid. Food Chem. 124, 444-449. doi: 10.1016/j.foodchem.2010.06.052
    • (2011) Food Chem , vol.124 , pp. 444-449
    • Jang, J.H.1    Moon, K.D.2
  • 18
    • 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., Götz, A., Letzel, T., Cheison, S. C., and Kulozik, U. (2015). Influence of denaturation and aggregation of β-lactoglobulin on its tryptic hydrolysis and the release of functional peptides. Food Chem. 187, 545-554. doi: 10.1016/j.foodchem.2015.04.034
    • (2015) Food Chem , vol.187 , pp. 545-554
    • Leeb, E.1    Götz, A.2    Letzel, T.3    Cheison, S.C.4    Kulozik, U.5
  • 20
    • 34247211578 scopus 로고    scopus 로고
    • Effects of pulsed electric fields on physicochemical properties of soybean protein isolates
    • Li, Y., Chen, Z., and Mo, H. (2007). Effects of pulsed electric fields on physicochemical properties of soybean protein isolates. LWT Food Sci. Technol. 40, 1167-1175. doi: 10.1016/j.lwt.2006.08.015
    • (2007) LWT Food Sci. Technol , vol.40 , pp. 1167-1175
    • Li, Y.1    Chen, Z.2    Mo, H.3
  • 21
    • 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., Chen, Q., and Kong, B. (2015). Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-shifting and mild heating processes. J. Agric. Food Chem. 63, 4853-4861. doi: 10.1021/acs.jafc.5b01331
    • (2015) J. Agric. Food Chem , vol.63 , pp. 4853-4861
    • Liu, Q.1    Geng, R.2    Zhao, J.3    Chen, Q.4    Kong, B.5
  • 22
    • 84992151844 scopus 로고    scopus 로고
    • Effect of ultrasonic processing on the changes in activity, aggregation and the secondary and tertiary structure of polyphenol oxidase in oriental sweet melon (Cucumis melo var. makuwa Makino)
    • Liu, S., Liu, Y., Huang, X., Yang, W., Hu, W., and Pan, S. (2017). Effect of ultrasonic processing on the changes in activity, aggregation and the secondary and tertiary structure of polyphenol oxidase in oriental sweet melon (Cucumis melo var. makuwa Makino). J. Sci. Food Agric. 97, 1326-1334. doi: 10.1002/jsfa.7869
    • (2017) J. Sci. Food Agric , vol.97 , pp. 1326-1334
    • Liu, S.1    Liu, Y.2    Huang, X.3    Yang, W.4    Hu, W.5    Pan, S.6
  • 23
    • 60149099551 scopus 로고    scopus 로고
    • Activation and conformational changes of mushroom polyphenoloxidase by high pressure microfluidization treatment
    • Liu, W., Liu, J., Liu, C., Zhong, Y., Liu, W., and Wan, J. (2009). Activation and conformational changes of mushroom polyphenoloxidase by high pressure microfluidization treatment. Innov. Food Sci. Emerg. Technol. 10, 142-147. doi: 10.1016/j.ifset.2008.11.009
    • (2009) Innov. Food Sci. Emerg. Technol , vol.10 , pp. 142-147
    • Liu, W.1    Liu, J.2    Liu, C.3    Zhong, Y.4    Liu, W.5    Wan, J.6
  • 24
    • 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., and Liang, R. H. (2013). The effect of citric acid on the activity, thermodynamics and conformation of mushroom polyphenoloxidase. Food Chem. 140, 289-295. doi: 10.1016/j.foodchem.2013.02.028
    • (2013) Food Chem , 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
  • 25
    • 84914166663 scopus 로고    scopus 로고
    • Stability and structural changes of horseradish peroxidase: microwave versus conventional heating treatment
    • Lopes, L. C., Barreto, M. T. M., Gonçalves, K. M., Alvarez, H. M., Heredia, M. F., de Souza, R. O. M. A., et al. (2015). Stability and structural changes of horseradish peroxidase: microwave versus conventional heating treatment. Enzyme Microb. Technol. 69, 10-18. doi: 10.1016/j.enzmictec.2014.11.002
    • (2015) Enzyme Microb. Technol , vol.69 , pp. 10-18
    • Lopes, L.C.1    Barreto, M.T.M.2    Gonçalves, K.M.3    Alvarez, H.M.4    Heredia, M.F.5    de Souza, R.O.M.A.6
  • 28
    • 84987916596 scopus 로고    scopus 로고
    • Characterization of polyphenol oxidase from blueberry (Vaccinium corymbosum L.)
    • Siddiq, M., and Dolan, K. D. (2017). Characterization of polyphenol oxidase from blueberry (Vaccinium corymbosum L.). Food Chem. 218, 216-220. doi: 10.1016/j.foodchem.2016.09.061
    • (2017) Food Chem , vol.218 , pp. 216-220
    • Siddiq, M.1    Dolan, K.D.2
  • 29
    • 57049160430 scopus 로고    scopus 로고
    • Kinetics and thermal activation/inactivation of starking apple polyphenol oxidase
    • Soysal, ç. (2008). Kinetics and thermal activation/inactivation of starking apple polyphenol oxidase. J. Food Process. Preserv. 32, 1034-1046. doi: 10.1111/j.1745-4549.2008.00298.x
    • (2008) J. Food Process. Preserv , vol.32 , pp. 1034-1046
    • Soysal, Ç.1
  • 30
    • 39049165190 scopus 로고    scopus 로고
    • A comparative analysis of property of lychee polyphenoloxidase using endogenous and exogenous substrates
    • Sun, J., Shi, J., Zhao, M., Xue, S. J., Ren, J., and Jiang, Y. (2008). A comparative analysis of property of lychee polyphenoloxidase using endogenous and exogenous substrates. Food Chem. 108, 818-823. doi: 10.1016/j.foodchem.2007.11.036
    • (2008) Food Chem , vol.108 , pp. 818-823
    • Sun, J.1    Shi, J.2    Zhao, M.3    Xue, S.J.4    Ren, J.5    Jiang, Y.6
  • 31
    • 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., and Versteeg, C. (2015). Blueberry polyphenol oxidase: characterization and the kinetics of thermal and high pressure activation and inactivation. Food Chem. 188, 193-200. doi: 10.1016/j.foodchem.2015.04.040
    • (2015) Food Chem , vol.188 , pp. 193-200
    • Terefe, N.S.1    Delon, A.2    Buckow, R.3    Versteeg, C.4
  • 32
    • 84951944359 scopus 로고    scopus 로고
    • High pressure thermal processing of pears: effect on endogenous enzyme activity and related quality attributes
    • Terefe, N. S., Tepper, P., Ullman, A., Knoerzer, K., and Juliano, P. (2016). High pressure thermal processing of pears: effect on endogenous enzyme activity and related quality attributes. Innov. Food Sci. Emerg. Technol. 33, 56-66. doi: 10.1016/j.ifset2015.12.001
    • (2016) Innov. Food Sci. Emerg. Technol , vol.33 , pp. 56-66
    • Terefe, N.S.1    Tepper, P.2    Ullman, A.3    Knoerzer, K.4    Juliano, P.5
  • 33
    • 0019741905 scopus 로고
    • Polyphenol oxidases and peroxidases in fruits and vegetables
    • Vámos-Vigyázó, L., and Haard, N. F. (1981). Polyphenol oxidases and peroxidases in fruits and vegetables. CRC Crit. Rev. Food Sci. Nutr. 15, 49-127. doi: 10.1080/10408398109527312
    • (1981) CRC Crit. Rev. Food Sci. Nutr , vol.15 , pp. 49-127
    • Vámos-Vigyázó, L.1    Haard, N.F.2
  • 34
    • 1342293174 scopus 로고    scopus 로고
    • Conformational Transitions in b-lactoglobulin induced by cationic amphiphiles: equilibrium Studies
    • Viseu, M. I., and Carvalho, T. I. (2004). Conformational Transitions in b-lactoglobulin induced by cationic amphiphiles: equilibrium Studies. Biochim. Biophys. Acta 86, 2392-2402. doi: 10.1016/S0006-3495(04)74296-4
    • (2004) Biochim. Biophys. Acta , vol.86 , pp. 2392-2402
    • Viseu, M.I.1    Carvalho, T.I.2
  • 35
    • 67349161371 scopus 로고    scopus 로고
    • Quantification and characterisation of polyphenol oxidase from vanilla bean
    • Waliszewski, K. N., Márquez, O., and Pardio, V. T. (2009). Quantification and characterisation of polyphenol oxidase from vanilla bean. Food Chem. 117, 196-203. doi: 10.1016/j.foodchem.2009.03.118
    • (2009) Food Chem , vol.117 , pp. 196-203
    • Waliszewski, K.N.1    Márquez, O.2    Pardio, V.T.3
  • 36
    • 43649102026 scopus 로고    scopus 로고
    • Latent and active polyphenol oxidase (PPO) in red clover (Trifolium pratense) and use of a low PPO mutant to study the role of PPO in proteolysis reduction
    • Winters, A. L., Minchin, F. R., Michaelson-Yeates, T. P. T., Lee, M. R. F., and Morris, P. (2008). Latent and active polyphenol oxidase (PPO) in red clover (Trifolium pratense) and use of a low PPO mutant to study the role of PPO in proteolysis reduction. J. Agric. Food Chem. 56, 2817-2824. doi: 10.1021/jf0726177
    • (2008) J. Agric. Food Chem , vol.56 , pp. 2817-2824
    • Winters, A.L.1    Minchin, F.R.2    Michaelson-Yeates, T.P.T.3    Lee, M.R.F.4    Morris, P.5
  • 37
    • 84862950867 scopus 로고    scopus 로고
    • Effect of ultrahigh hydrostatic pressure on the activity and structure of mushroom (Agaricus bisporus) polyphenoloxidase
    • Yi, J., Jiang, B., Zhang, Z., Liao, X., Zhang, Y., and Hu, X. (2012). Effect of ultrahigh hydrostatic pressure on the activity and structure of mushroom (Agaricus bisporus) polyphenoloxidase. J. Agric. Food Chem. 60, 593-598. doi: 10.1021/jf203405u
    • (2012) J. Agric. Food Chem , vol.60 , pp. 593-598
    • Yi, J.1    Jiang, B.2    Zhang, Z.3    Liao, X.4    Zhang, Y.5    Hu, X.6
  • 38
    • 84955562218 scopus 로고    scopus 로고
    • Effects of relative air humidity on the phenolic compounds contents and coloration in the 'Fuji' apple (Malus domestica Borkh.) peel
    • Zhang, M., Zhang, G., You, Y., Yang, C., Li, P., and Ma, F. (2016). Effects of relative air humidity on the phenolic compounds contents and coloration in the 'Fuji' apple (Malus domestica Borkh.) peel. Sci. Hortic. 201, 18-23. doi: 10.1016/j.scienta.2016.01.017
    • (2016) Sci. Hortic , vol.201 , pp. 18-23
    • Zhang, M.1    Zhang, G.2    You, Y.3    Yang, C.4    Li, P.5    Ma, F.6
  • 39
    • 84988484374 scopus 로고    scopus 로고
    • Different modes of inhibition for organic acids on polyphenoloxidase
    • Zhou, L., Liu, W., Xiong, Z., Zou, L., Chen, J., Liu, J., et al. (2016). Different modes of inhibition for organic acids on polyphenoloxidase. Food Chem. 199, 439-446. doi: 10.1016/j.foodchem.2015.12.034
    • (2016) Food Chem , vol.199 , pp. 439-446
    • Zhou, L.1    Liu, W.2    Xiong, Z.3    Zou, L.4    Chen, J.5    Liu, J.6
  • 40
    • 84978640093 scopus 로고    scopus 로고
    • Aggregation and conformational change of mushroom (Agaricus bisporus) polyphenoloxidase subjected to thermal treatment
    • Zhou, L., Liu, W., Zou, L., Xiong, Z., Hu, X., and Chen, J. (2017). Aggregation and conformational change of mushroom (Agaricus bisporus) polyphenoloxidase subjected to thermal treatment. Food Chem. 214, 423-431. doi: 10.1016/j.foodchem.2016.07.041
    • (2017) Food Chem , vol.214 , pp. 423-431
    • Zhou, L.1    Liu, W.2    Zou, L.3    Xiong, Z.4    Hu, X.5    Chen, J.6
  • 41
    • 61349137551 scopus 로고    scopus 로고
    • Comparison of the inactivation kinetics of pectin methylesterases from carrot and peach by high-pressure carbon dioxide
    • Zhou, L., Zhang, Y., Hu, X., Liao, X., and He, J. (2009). Comparison of the inactivation kinetics of pectin methylesterases from carrot and peach by high-pressure carbon dioxide. Food Chem. 115, 449-455. doi: 10.1016/j.foodchem.2008.12.028
    • (2009) Food Chem , vol.115 , pp. 449-455
    • Zhou, L.1    Zhang, Y.2    Hu, X.3    Liao, X.4    He, J.5


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