Changes in physicochemical properties of proteins in Kayserian Pastirma made from the M. semimembranosus muscle of cows during traditional processing

Food Science and Human Wellness

Volumn 2, Issue 1, 2013, Pages 46-55

  Ahhmed, Abdulatef Mrghni ^a,b,c   Kaneko, Gen ^a   Ushio, Hideki ^a   Inomata, Tomo ^b   Yetim, Hasan ^c   Karaman, Safa ^c   Muguruma, Michio ^d   Sakata, Ryoichi ^b  

^a UNIVERSITY OF TOKYO   (Japan)

^b AZABU UNIVERSITY   (Japan)

^c ERCIYES UNIVERSITY   (Turkey)

^d UNIVERSITY OF MIYAZAKI   (Japan)

Author keywords

M. semimembranosus; Meat processing; Pastirma; Physicochemical properties; Protein digestion

Indexed keywords

EID: 85068977532     PISSN: None     EISSN: 22134530     Source Type: Journal    
DOI: 10.1016/j.fshw.2013.03.001     Document Type: Article

References (45)

1. Gok, V., Obuz, E., Akkaya, L., Effects of packaging method and storage time on the chemical, microbiological, and sensory properties of Turkish pastirma. A dry cured beef product. Meat Science 80 (2008), 335–344.
2. Aksu, I.M., Kaya, M., Ockerman, H., Effects of modified atmosphere packaging and temperature on the shelf life of sliced pastirma produced from frozen/thawed meat. Journal of Muscle Foods 16 (2005), 192–206.
3. Aksu, I.M., Kaya, M., Some microbiological, chemical, and physical characteristics of pastirma marketed in Erzurum. Turkish Journal of Veterinary Animal Sciences 25 (2001), 319–326.
4. Kaban, G., Changes in the composition of volatile compounds and in microbiological and physicochemical parameters during pastirma processing. Meat Science 82 (2009), 17–23.
5. Zhou, G., Zhao, G., Biochemical changes during processing of traditional Jinhua ham. Meat Science 77 (2007), 114–120.
6. Virgili, R., Schivazappa, C., Muscle traits for long matured dried meats. Meat Science 62 (2002), 331–343.
7. Flores, M., Spanier, A.M., Toldra, F., Flavour analysis of dry-cured ham. Shahidi de, F., (eds.) Flavor of Meat, Meat Products and Seafood, 1998, Blackie Academic and Professional, London, UK, 320–341.
8. Ahhmed, A.M., Muguruma, M., A review of meat protein hydrolysates and hypertension. Meat Science 86 (2010), 110–118.
9. Aktas, N., Gurses, A., Original Research Article: moisture adsorption properties and adsorption isosteric heat of dehydrated slices of pratirma (Turkish dry meat product). Meat Science 71 (2005), 571–576.
10. Isikli, N.D., Karababa, E.A., Rheological characterization of fenugreek paste (cemen). Journal of Food Engineering 69 (2005), 185–190.
11. Ahhmed, A.M., Kawahara, S., Ohta, K., et al. Differentiation in improvements of gel strength in chicken and beef sausages induced by transglutaminase. Meat Science 76 (2007), 455–462.
12. Gornall, G.A., Baradawill, J.C., David, M.M., Determination of serum protein by means of the biuret reaction. Journal of Biological Chemistry 177 (1949), 751–766.
13. Hayakawa, I., Kajihara, J., Morikawa, K., et al. Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals. Journal of Food Science 50 (1985), 486–491.
14. Tomita, S., Studies on the fluorometric analysis of polyelectrolytes (I) protein. Japan National Chemistry Laboratory of Industry 58 (1963), 99–107.
15. Ahhmed, A.M., Nasu, T., Huy, Q.D., et al. Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef. Meat Science 82 (2009), 170–178.
16. Chelh, L., Gatellier, P.M., Sante-Lhoutellier, V., Technical note: a simplified procedure for myofibril hydrophobicity determination. Meat Science 74 (2006), 681–683.
17. Ahhmed, M.A., Kuroda, R., Kawahara, S., et al. Dependence of microbial transglutaminase on meat type in myofibrillar protein cross-linking. Food Chemistry 112 (2009), 354–361.
18. Kawahara, S., Ahhmed, M.A., Ohta, K., et al. Inconsistency in the improvements of gel strength in chicken and pork sausages induced by microbial transglutaminase. Asian-Australian Journal of Animal Sciences 20 (2007), 1285–1291.
19. Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685.
20. Krzywicki, K., Assessment of relative content of myoglobin, oxymyoglobin and metmyoglobin at the surface of beef. Meat Science 3 (1979), 1–10.
21. Saito, K., Ahhmed, A., Takeda, H., et al. Effects of a humidity-stabilizing sheet on the color and K value of beef stored at cold temperatures. Meat Science 75 (2007), 275–282.
22. Ahhmed, M.A., Nasu, T., Muguruma, M., Impact of transglutaminase on the textural, physicochemical, and structural properties of chicken skeletal, smooth, and cardiac muscles. Meat Science 83 (2009), 759–767.
23. Luccia, D.A., Picariello, G., Cacae, G., et al. Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams. Meat Science 69 (2005), 479–491.
24. Yetim, H., Sagdic, O., Dogan, M., et al. Sensitivity of three pathogenic bacteria to Turkish cemen paste and its ingredients. Meat Science 74 (2006), 354–358.
25. Toldra, F., Etherington, D.J., Examination of cathepsins B, D, H and L activities in dry-cures hams. Meat Science 59 (1988), 531–538.
26. Zhao, G.M., Zhou, G.H., Wang, Y.L., et al. Time related changes in cathepsin B and L activities during processing of Jinhua ham as a function of pH, salt and temperature. Meat Science 70 (2005), 603–681.
27. Zhen, Z.Y., He, Z.F., Li, H.J., et al. Prospect of study on the Jinhua ham maturating and microorganism fermenting. Sichuan Food and Fermentation: Chinese 40 (2004), 1–3.
28. Sano, T., Ohno, T., Otsuka-Fuchino, H., et al. Carp natural actomyos, thermal denaturationmechanism. Journal of Food Science 59 (1994), 1002–1008.
29. Yongsawatdigul, J., Park, J.W., Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry 83 (2003), 409–416.
30. Mignino, L.A., Paredi, M.E., Physico-chemical and functional properties of myofibrillar proteins from different species of mollusks. LWT: Food Science and Technology 39 (2006), 35–42.
31. Muguruma, M., Tsuruoka, K., Katayama, K., et al. Soybean and milk protein modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Science 63 (2003), 191–197.
32. Prevolnik, M., krlep, M.S., Janes, J., et al. Accuracy of near infrared spectroscopy for prediction of chemical composition, salt content and free amino acids in dry-cured ham. Meat Science 88 (2011), 299–304.
33. Ruiz, J., Garcia, C., Carmen Diaz, M., et al. Dry cured Iberian ham non-volatile components as affected by the length of the curing process. Food Research International 32 (1999), 643–651.
34. Virgili, R., Saccani, G., Gabba, L., et al. Changes of free amino acids and biogenic amines during extended ageing of Italian dry cured ham. LWT: Food Science and Technology 40 (2007), 871–878.
35. Faustman, C., Phillips, L.A., Measurement of discoloration in fresh meat. Worlstad, R.E., (eds.) Current Protocols in Food Analytical Chemistry, 2001, Wiley & Sons, Inc., New York, F3.3.1–F3.3.13.
36. Clydesdale, F.M., Colorimetry-methodology and applications. Critical Reviews in Food Science and Nutrition 10 (1978), 243–301.
37. Bekhit, A.E., Faustman, C., Review: metmyoglobin reducing activity. Meat Science 71 (2005), 407–439.
38. Carpenter, C.E., Cornforth, D.P., Whittier, D., Consumer preferences for beef color and packaging did not affect eating satisfaction. Meat Science 57 (2001), 359–363.
39. Tekinsen, O.C., Dogruer, Y., Nizamloglu, M., et al. The possibility of using potassium sorbate in cemen and its effect on the microbial quality of pastrami. Turkish Journal of Veterinary and Animal Sciences 23 (1999), 227–235.
40. Swatland, H.J., The Conversion of Muscles to Meat. Structure and Development of Meat Animals and Poultry. 1994, Technomic Publishing Company, Pennsylvania.
41. Saito, K., Ahhmed, M.A., Kawahara, S., et al. Evaluation of the performance of osmotic dehydration sheets on freshness parameters in cold-stored beef biceps femoris muscle. Meat Science 82 (2009), 260–265.
42. Claeys, E., De Smet, S., Balcaen, A., et al. Quantification of fresh meat peptides by SDS-PAGE in relation to ageing time and taste intensity. Meat Science 67 (2004), 281–288.
43. Samaranayaka, A.G.P., Li-Chan, E.C.Y., Food-derived peptidic antioxi-dants: a review of their production, assessment, and potential applications. Journal of Functional Food 3 (2011), 229–254.
44. Damez, J., Clerjon, S., Meat quality assessment using biophysical methods related to meat structure. Meat Science 80 (2008), 132–149.
45. Huff-Lonergan, E., Lonergan, M., Mechanisms of water holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Science 71 (2005), 194–204.