Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

Food Engineering Reviews

Volumn 7, Issue 2, 2015, Pages 222-230

  Larrea Wachtendorff, Dominique ^a   Tabilo Munizaga, Gipsy ^a   Moreno Osorio, Luis ^a   Villalobos Carvajal, Ricardo ^a   Pérez Won, Mario ^b  

^a UNIVERSIDAD DEL BÍO BÍO   (Chile)

^b DEPARTAMENTO DE BIOLOGÍA   (Chile)

Author keywords

High hydrostatic pressure; Myofibrillar proteins; Protein secondary structure; Thermal stability

Indexed keywords

CALORIMETERS; CALORIMETRY; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; FISH; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDRAULICS; HYDROSTATIC PRESSURE; MUSCLE; THERMODYNAMIC STABILITY;

DENATURATION TEMPERATURES; ENDOTHERMIC TRANSITIONS; HIGH HYDROSTATIC PRESSURE; MYOFIBRILLAR PROTEINS; PRESSURE TREATMENTS; PROTEIN SECONDARY STRUCTURE; SECONDARY STRUCTURES; SERIOLELLA VIOLACEA;

PROTEINS;

EID: 84931562110     PISSN: 18667910     EISSN: 18667929     Source Type: Journal    
DOI: 10.1007/s12393-015-9107-1     Document Type: Article

References (47)

1. Abugoch L, Quitral V, Larraín MA, Vinagre J, Kriukov A, Chávez G (2006) Estudio de las modificaciones en proteínas de reineta (Brama australis), sometidas a congelación y almacenamiento a −18 °C y −30 °C. Arch Latinoam Nutr 56:1–11
2. Angsupanich K, Ledward DA (1998) High pressure treatment effects on cod (Gadus morhua) muscle. Food Chem 63:39–50
3. Aubourg SP, Torres JA, Saraiva JA, Guerra-Rodriguez E (2013) Effect of high-pressure treatments applied before freezing and frozen storage on the functional and sensory properties of Atlantic mackerel (Scomber scombrus). LWT Food Sci Technol 53:100–106
4. Balny C, Mozhaev VV, Lange R (1997) Hydrostatic pressure and proteins: basic concepts and new data. Comp Biochem Physiol 116A(4):299–304
5. Böcker U, Kohler A, Aursand IG, Ofstad R (2008) Effects of brine salting with regard to raw material variation of Atlantic salmon (Salmon salar) muscle investigated by FT-IR microspectroscopy. J Agr Food Chem 56:5129–5137
6. Brown WO (1986) Fish muscle as food. In: Bechtel PI (ed) Muscle as food, Chap 10, Academic Press, Orlando, pp 405–445
7. Buckow R, Sikes A, Tume RE (2013) Effect of high pressure on physicochemical properties of meat. Crit Rev Food Sci Nutr 53:770–786
8. Cao Y, Xia T, Zhou G, Xinglian X (2012) The mechanism of high pressure-induced gels of rabbit myosin. Innov Food Sci Emerg 16:41–46
9. Carton I, Böcker U, Ofstad R, Sørheim O, Kohler A (2009) Monitoring secondary structural changes in salted smoked salmon muscle myofiber proteins by FT-IR microspectroscopy. J Agr Food Chem 57:3563–3570
10. Celej MS, Dassie SA, González M, Bianconi ML, Fidelio GD (2006) Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins. Anal Biochem 350:277–284
11. Chapleau N, Mangavel C, Compoint JP, de Lamballerie-Anton M (2003) Effect of high-pressure processing on myofibrillar protein structure. J Sci Food Agric 84:66–74
12. Dissanayake M, Kasapis S, George P, Adhikari B, Palmer M, Meurer B (2013) Hydrostatic pressure effects on the structural properties of condensed whey protein/lactose systems. Food Hydrocoll 30:632–640
13. Dzwolak W, Kato M, Taniguchi Y (2002) Fourier transform infrared spectroscopy in high-pressure studies on proteins. Biochim Biophys Acta 1595:131–144
14. Dzwolak W, Smirnovas V (2005) A conformational α-helix to β-sheet transition accompanies racemic self-assembly of polylysine: an FT-IR spectroscopic study. Biophys Chem 115:49–54
15. Geirsdottir M (1998) Prædiktion of frysestabilitet ved DSC målinger. MSc thesis, Denmark’s Technical University, Lyngby, Denmark
16. Heremans K, Smeller L (1998) Protein structure and dynamics at high pressure. Biochim Biophys Acta 1386:353–370
17. Honikel KO, Hamid A, Fischer C, Hamm R (1981) Influence of postmortem changes in bovine muscle on the water-holding capacity of beef. Postmortem storage of muscle at various temperatures between 0 and 30 °C. J Food Sci 46:23–31
18. Ikkai T, Ooi T (1966) The effects of pressure on G-F transformation of actin. Biochemistry 5:1551–1560
19. Jasra SK, Pardeep K, Jasra PK, Talesara CL (2001) Myofibrillar protein degradation of carp (Labeo rohita (Hamilton)) muscle after post-mortem unfrozen and frozen storage. J Sci Food Agric 81:519–524
20. Lauritzsen K, Akse L, Johansen A, Joensen S, Sørensen NK, Olsen RL (2004) Physical and quality attributes of salted cod (Gadus morhua L.) as affected by the state of rigor and freezing prior to salting. Food Res Int 37:677–688
21. Law HY, Choi SM, Ma CY (2008) Study of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetry. Food Res Int 41:720–729
22. Lian X, Wang C, Zhang K, Li L (2014) The retrogradation properties of glutinous rice and buckwheat starches as observed with FT-IR, 13C NMR and DSC. Int J Biol Macromol 64:288–293
23. Lo YL, Rahman YE (1998) Effect of lipids on the thermal stability and conformational changes of proteins: ribonuclease A and cytochrome c. Int J Pharm 161:137–148
24. Ma CY, Harwalkar VR (1991) Thermal analysis of food proteins. Adv Food Nutr Res 35:317–366
25. Ma H, Ledward DA (2013) High pressure processing of fresh meat—Is it worth it? Meat Sci 95:897–903
26. Matos E, Silva ST, Tiago T, Aureliano M, Dinis MT, Dias J (2011) Effect of harvesting stress and storage conditions on protein degradation in fillets of farmed gilthead seabream (Sparus aurata): a differential scanning calorimetry study. Food Chem 126:270–276
27. Meersman F, Dobson CM, Heremans K (2006) Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions. Chem Soc Rev 35:908–917
28. Messens W, Van Camp J, Huyghebaert A (1997) The use of high pressure to modify the functionality of food proteins. Trends Food Sci Technol 8:107–112
29. Mobili P, Londero A, Maria TMR, Eusébio MES, De Antoni GL, Fausto R (2009) Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry. Vib Spectrosc 50:68–77
30. Nagai T, Kurata M, Nakamura T, Ito T, Fujiki K, Nakao M, Yano T (1999) Properties of myofibrillar protein from Japanese stingfish (Sebastes inermis) dorsal muscle. Food Res Int 32:401–405
31. Park JW, Korhonen RW, Lanier TC (1990) Effects of rigor mortis on gel-forming properties of surimi and unwashed mince prepared from tilapia. J Food Sci 55:353–355
32. Paredi ME, Tomas MC, Crupkin M (2003) Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC). Braz J Chem Eng 20:153–159
33. Qiu C, Xia W, Jiang Q (2013) Effect of high hydrostatic pressure (HHP) on myofibril-bound serine proteinases and myofibrillar protein in silver carp (Hypophthalmichthys molitrix). Food Res Int 52:199–205
34. Rivalain N, Roquain J, Demazeau G (2010) Development of high hydrostatic pressure in biosciences: pressure effect on biological structures and potential applications in Biotechnologies. Biotechnol Adv 28:659–672
35. Rora AMB, Furuhaug R, Fjaera SO, Skjervold PO (2004) Salt diffusion in pre-rigor filleted Atlantic salmon. Aquaculture 232:255–263
36. Rustad T (1992) Muscle chemistry and the quality of wild and farmed cod. In: Huss HH, Jacobsen M, Liston J (eds) Quality assurance in the fish industry. Elsevier, London, pp 19–27
37. Schubring R (2003) Differential scanning calorimetric (DSC) measurements on the roe of rainbow trout (Oncorhynchus mykiss): influence of maturation and technological treatment. Thermochim Acta 415:89–98
38. Schubring R (2005) Characterizing protein changes caused by application of high hydrostatic pressure on muscle food by means of DSC. J Therm Anal Calorim 82:229–237
39. Smeller L (2002) Pressure-temperature phase diagrams of biomolecules. Biochim Biophys Acta 1595:11–29
40. Somkuti J, Smeller L (2013) High pressure effects on allergen food proteins. Biophys Chem 183:19–29
41. Tabilo-Munizaga G, Gordon TA, Villalobos-Carvajal R, Moreno-Osorio L, Salazar FN, Pérez-Won M, Acuña S (2014) Effects of high hydrostatic pressure (HHP) on the protein structure and thermal stability of Sauvignon blanc wine. Food Chem 155:214–220
42. Thorarinsdottir KA, Arason S, Geirsdottir M, Bogason SG, Kristbergsson K (2002) Changes in myofibrillar proteins during processing of salted cod (Gadus morhua) as determined by electrophoresis and differential scanning calorimetry. Food Chem 77:377–385
43. Villamonte G, Simonin H, Duranton F, Chéret R, de Lamballerie M (2013) Functionality of pork meat proteins: impact of sodium chloride and phosphates under high-pressure processing. Innov Food Sci Emerg 18:15–23
44. Winter R, Dzwolak W (2005) Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins. Philos Trans R Soc A 363:537–563
45. Wright DJ, Leach IB, Wilding P (1977) Differential scanning calorimetric studies of muscles and its constituent proteins. J Sci Food Agric 28:557–564
46. Yu L, Christie G (2001) Measurement of starch thermal transitions using differential scanning calorimetry. Carbohydr Polym 46:179–184
47. Zhang J, Peng X, Jonas A, Jonas J (1995) NMR study of the cold, heat and pressure unfolding of RNA. Biochemistry 34:8631–8641