Secondary structure and conformational change of mushroom polyphenol oxidase during thermosonication treatment by using FTIR spectroscopy

Food Chemistry

Volumn 214, Issue , 2017, Pages 507-514

  Baltacıoğlu, Hande ^a,b   Bayındırlı, Alev ^b   Severcan, Feride ^b  

^a NIGDE UNIVERSITY   (Turkey)

^b MIDDLE EAST TECHNICAL UNIVERSITY   (Turkey)

Author keywords

Conformation change; FTIR; PPO; Protein secondary structure; Spectroscopy; Thermosonication

Indexed keywords

AGGREGATES; ENZYME ACTIVITY; ENZYMES; POLYPHENYLENE OXIDES; PROTEINS; SPECTROSCOPY; ULTRASONICS;

CONFORMATION CHANGE; CONFORMATIONAL CHANGE; FTIR; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SECONDARY STRUCTURES; THERMO SONICATIONS; ULTRASOUND TREATMENTS;

FOURIER TRANSFORM INFRARED SPECTROSCOPY;

CATECHOL OXIDASE; PLANT PROTEIN;

ALPHA HELIX; ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; CURVE FITTING; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME ISOLATION; INFRARED SPECTROSCOPY; MUSHROOM; NONHUMAN; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; TRANSITION TEMPERATURE; ULTRASOUND; AGARICALES; CHEMISTRY; ENZYMOLOGY; EVALUATION STUDY; HEAT; PROCEDURES; VEGETABLE;

AGARICALES; CATECHOL OXIDASE; HOT TEMPERATURE; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; ULTRASONICS; VEGETABLES;

EID: 84978654551     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.07.021     Document Type: Article

References (30)

1. Abid, M., Jabbar, S., Hu, B., Hashim, M.M., Wu, T., Lei, S.,.. Zeng, X., Thermosonication as a potential quality enhancement technique of apple juice. Ultrasonics Sonochemistry 21 (2014), 984–990.
2. Baltacıoğlu, H., Bayındırlı, 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: FTIR study. Food Chemistry 187 (2015), 263–269.
3. Bayındırlı, A., Alpas, H., Bozoglu, F., Hizal, M., Efficiency of high pressure treatment on inactivation of pathogenic microorganisms and enzymes in apple, orange, apricot and sour cherry juices. Food Control 17 (2006), 52–58.
4. Cakmak, G., Zorlu, F., Severcan, M., Severcan, F., Screening of protective effect of amifostine on radiation-induced structural and functional variations in rat liver microsomal membranes by FT-IR spectroscopy. Analytical Chemistry 83 (2011), 2438–2444.
5. Cheng, L.H., Soh, C.Y., Liew, S.C., Teh, F.F., Effects of sonication and carbonation on guava juice quality. Food Chemistry 104 (2007), 1396–1401.
6. 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), 674–679.
7. Cruz, R.M.S., Vieira, M.C., Silva, C.L.M., Effect of heat and thermosonication treatments on peroxidase inactivation kinetics in watercress (Nasturtium officinale). Journal of Food Engineering 72 (2006), 8–15.
8. De Gennaro, L., Cavella, S., Romano, R., Masi, P., The use of ultrasound in food technology I: Inactivation of peroxidase by thermosonication. Journal of Food Engineering 39 (1999), 401–407.
9. Garip, S., Yapici, E., Simsek Ozek, N., Severcan, M., Severcan, F., Evaluation and discrimination of simvastatin-induced structural alterations in proteins of different rat tissues by FTIR spectroscopy and neural network analysis. Analyst 135 (2010), 3233–3241.
10. Goormaghtigh, E., Gasper, R., Bénard, A., Goldsztein, A., Raussens, V., Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra. Biochimica et Biophysica Acta 1794 (2009), 1332–1343.
11. Haris, P.I., Severcan, F., FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. Journal of Molecular Catalysis B: Enzymatic 7 (1999), 207–221.
12. Kadkhodaee, R., Povey, M.J.W., Ultrasonic inactivation of Bacillus a-amylase. I. Effect of gas content and emitting face of probe. Ultrasonics Sonochemistry 15:2 (2008), 133–142.
13. Kucuk Baloglu, F., Garip, S., Heise, S., Brockmann, G., Severcan, F., FTIR imaging of structural changes in visceral and subcutaneous adiposity and brown to white adipocyte transdifferentiation. Analyst 140 (2015), 2205–2214.
14. Kuldiloke, J., Eshtiaghi, M., Zenker, M., Knorr, D., Inactivation of Lemon Pectinesterase by Thermosonication. International Journal of Food Engineering, 3(2), 2007 Art. 3.
15. Lopez, P., Sala, F.J., Delafuente, J.L., Condon, S., Raso, J., Burgos, J., Inactivation of peroxidase, lipoxygenase, and polyphenol oxidase by manothermosonication. Journal of Agricultural and Food Chemistry 42 (1994), 252–256.
16. Marchioni, C., Riccardi, E., Spinelli, S., Dell'Unto, F., Grimaldi, P., Bedini, A.,.. Congiu Castellano, A., Structural changes induced in proteins by therapeutic ultrasounds. Ultrasonics 49 (2009), 569–576.
17. Mawson, R., Gamage, M., Terefe, N.S., Knoerzer, K., Ultrasound in enzyme activation and inactivation. Feng, H., Barbosa-Canovas, G., Weiss, J., (eds.) Ultrasound technologies for food and bioprocessing, 2010, New York, Springer, 369–404.
18. O'Donnell, C.P., Tiwari, B.K., Bourke, P., Cullen, P.J., Effect of ultrasonic processing on food enzymes of industrial importance. Trends in Food Science & Technology 21 (2010), 358–367.
19. Pallua, J.D., Recheis, W., Pöder, R., Pfaller, K., Pezzei, C., Hahn, H.,.. Huck, C.W., Morphological and tissue characterization of the medicinal fungus Hericium coralloides by a structural and molecular imaging platform. Analyst 137:7 (2012), 1584–1595.
20. Severcan, F., Haris, P.I., Fourier transform infrared spectroscopy suggests unfolding of loop structures precedes complete unfolding of pig citrate synthase. Biopolymers 69 (2003), 440–447.
21. Severcan, M., Haris, P.I., Severcan, F., Using artificially generated spectral data to improve protein secondary structure prediction from Fourier transform infrared spectra of proteins. Analytical Biochemistry 332 (2004), 238–244.
22. Severcan, M., Severcan, F., Haris, P.I., Estimation of protein secondary structure from FTIR spectra using neural networks. Journal of Molecular Structure 565–566 (2001), 383–387.
23. Sun, N.K., Song, K.B., Effect of nonthermal treatment on the molecular properties of mushroom polyphenoloxidase. Journal of Food Science 68:5 (2003), 1639–1643.
24. Terefe, N.S., Buckow, R., Versteeg, C., Quality-related enzymes in plant-based products: effects of novel food-processing technologies Part 3: ultrasonic processing. Critical Reviews in Food Science and Nutrition 55 (2015), 147–158.
25. Toyran, N., Zorlu, F., Donmez, G., Öge, K., Severcan, F., Chronic hypoperfusion alters the content and structure of proteins and lipids of rat brain homogenates: a Fourier transform infrared spectroscopy study. European Biophysics Journal 33 (2004), 549–554.
26. Turker, S., Ilbay, G., Severcan, M., Severcan, F., Investigation of compositional, structural, and dynamical changes of pentylenetetrazol-induced seizures on a rat brain by FT-IR spectroscopy. Analytical Chemistry 86 (2014), 1365–1403.
27. Weemaes, C., Rubens, P., De Cordt, S., Ludikhuyze, L., Van Den Broeck, I., Hendrickx, M.,.. Tobback, P., Temperature sensitivity and pressure resistance of mushroom polyphenoloxidase. Journal of Food Science 62:2 (1997), 261–266.
28. Wu, J., Gamage, T.V., Vilkhu, K.S., Simons, L.K., Mawson, R., Effect of thermosonication on quality improvement of tomato juice. Innovative Food Science and Emerging Technologies 9 (2008), 186–195.
29. Yu, Z.-L., Zeng, W.-C., Lu, X.-L., Influence of ultrasound to the activity of tyrosinase. Ultrasonics Sonochemistry 20 (2013), 805–809.
30. Yu, Z.-L., Zeng, W.-C., Zhang, W.-H., Liao, X.-P., Shi, B., Effect of ultrasound on the activity and conformation of α-amylase, papain and pepsin. Ultrasonics Sonochemistry 21 (2014), 930–936.