Mikrodalgada Kızartmanın Tavuk Göğüs Eti Miyofibriler ve Sarkoplazmik Proteinleri Üzerine Etkileri

Year 2017, Volume: 27 Issue: 4, 496 - 506, 26.12.2017

İşıl Barutçu Mazı , Bekir Mazı

https://doi.org/10.29133/yyutbd.305427

Abstract

Bu
çalışmanın temel amacı mikrodalgada kızartma işleminin ve farklı kızartma
sürelerinin tavuk göğüs eti miyofibriler ve sarkoplazmik proteinleri üzerine
etkilerinin incelenmesidir. Kızartılmış ürünlerin renk ve tekstürü de
belirlenmiştir. Kızartma işlemi mikrodalga fırında 365W (%70) güç seviyesinde
0,5 ve 1,5 dakika sürelerde, yağın sıcaklığı 180°C’ye getirildikten sonra
gerçekleştirilmiştir. Örnekler ayrıca, karşılaştırma amaçlı olarak, fritöz
içerisinde 180°C’de 2,0 ve 5,0 dakika süreler ile
kızartılmıştır. Nem oranı, 0,5 ve 1,5 dakika süre ile mikrodalgada kızartılan örnekler
için sırasıyla %59,3 ve %32,7’ye düşmüştür. Mikrodalga kızartma işlemi, 5,0
dakika süresince konvansiyonel yöntem ile kızartmayla karşılaştırıldığında,
daha açık renk ile daha düşük sertlik değerlerine sahip örnekler sağlamıştır.
Kızartılmış tavuk göğüs eti proteinleri, sodyum dodesil sülfat-poliakrilamid
jel elektroforezi (SDS-PAGE) ile incelenmiştir. Her iki kızartma yönteminde de
myosin ağır zincirine ait bandın yoğunluğunun önemli derecede azaldığı
gözlenmiştir. Genel olarak bakıldığında, kızartma yönteminin ve kızartma
süresinin tavuk göğüs eti miyofibriler ve sarkoplazmik proteinleri üzerinde
farklı etkileşimlere yol açmadığı gözlemlenmiştir. Örneklerin mikroyapısal
analizi de yapılmıştır.

Keywords

Mikrodalga kızartma, Tavuk eti, Miyofibriler protein, SEM, Renk, Sarkoplazmik

The Effects of Microwave Frying on Myofibrillar and Sarcoplasmic Proteins of Chicken Breast Meat

Abstract

The
main objective of this study is to investigate the effects of microwave frying
and different frying times on myofibrillar and sarcoplasmic proteins of chicken
breast muscle. The color and texture of the fried samples were also determined.
Frying was performed in microwave oven at 365W (70%) power level for 0.5 and
1.5 minutes after bringing the oil temperature to 180°C. Samples were also
fried in a conventional fryer at 180°C for 2.0 and 5.0 minutes for comparison.
The moisture content was dropped to 59.3% and 32.7% for 0.5 and 1.5 min
microwave fried samples, respectively. Microwave frying provided lighter
colored samples with lower hardness values when compared to the conventional
frying for 5.0 min. Fried chicken breast muscle proteins were examined using sodium dodecyl
sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). In both frying methods, the intensity of the
myosin heavy chain band was observed to decrease significantly. In general, it
was observed that the frying method and frying time did not cause divergent
interactions on myofibrillar and sarcoplasmic proteins of chicken breast
muscle. Microstructural analysis of samples was also
performed.

Keywords

Microwave frying, Chicken meat, Myofibrillar protein, Sarcoplasmic protein, SEM, Color

References

• AOAC (1995). Official Methods of Analysis, 16th ed., Association of Official Analytical Chemists, Washington.
• Barutcu I, Sahin S, Sumnu G (2009). Acrylamide formation in different batter formulations during microwave frying. LWT--Food Sci. Technol. 42(1): 17-22.
• Barutcu I, McCarthy MJ, Seo YS, Sahin S (2009). Magnetic resonance temperature mapping of microwave-fried chicken fingers. J. Food Sci. 74(5): E234-E240.
• Buffler CR (1993). Microwave Cooking and Processing: Engineering Fundamentals for the Food Scientist, 1st ed., Springer, New York.
• Claeys E, Uytterhaegen L, Buts B, Demeyer D (1995). Quantification of beef myofibrillar proteins by SDS-PAGE. Meat Sci. 39(2): 177–193.
• Ebashi S, Wakabayashi T, Ebashi F (1971). Troponin and its components. J. Biochem. 69(2): 441-445.
• Foegeding EA (1987). Functional properties of turkey salt-soluble proteins. J. Food Sci. 52(6): 1495-1499.
• Hay JD, Currie RW, Wolfe FH (1973). Polyacrylamide disc gel electrophoresis of fresh and aged chicken muscle proteins in sodium dodecylsulfate. J. Food Sci. 38(6): 987-990.
• Ho CY, Stromer MH, Robson RM (1994). Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie. 76(5): 369–375.
• Huang M, Huang F, Xu X, Zhou G (2009). Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging. Food Chem 115(1): 181–186.
• Huang F, Huang M, Xu X, Zhou G (2011). Influence of heat on protein degradation, ultrastructure and eating quality indicators of pork. J. Sci. Food Agric. 91(3): 443- 448.
• Hubbard LJ, Farkas BE (2000). Influence of oil temperature on convective heat transfer during immersion frying. J. Food Process. Preserv. 24(5): 143-162.
• Innawong B, Mallikarjunan P, Marcy J, Cundiff J (2006). Pressure conditions and quality of chicken nuggets fried under gaseous nitrogen atmosphere. J. Food Process. Preserv. 30(2): 231-245.
• Kurozawa LE, Park KJ, Hubinger MD (2008). Optimization of the enzymatic hydrolysis of chicken meat using response surface methodology. J. Food Sci. 73(5): C405-C412.
• Llorca E, Hernando I, Perez-Munuera I, Quiles A, Larrea, V, Lluch M (2007). Protein breakdown during the preparation of frozen batter-coated squid rings. Eur. Food Res. Technol. 225(5-6): 807-813.
• Lowey S, Risby D (1971). Light chains from fast and slow muscle myosins. Nature 234: 81–85.
• Maruyama K (1971). A study of β-actinin myofibrillar protein from rabbit skeletal muscle. J. Biochem. 69: 369.
• Masaki T, Takaiti O (1972). Purification of M-protein. J. Biochem. 71(2): 335-7.
• Morimoto K, Harrington WF (1972). Isolation and physical chemical properties of an M-line protein from skeletal muscle. J. Biol. Chem. 247(10): 3052-3061.
• Murphy RY, Johnson ER, Duncan LK, Clausen EC, Davis MD, March JA (2001). Heat transfer properties, moisture loss, product yield, and soluble proteins in chicken breast patties during air convection cooking. Poult. Sci. 80(4): 508-514.
• Murphy RY, Marks BP (2000). Effect of meat temperature on proteins, texture, and cook loss for ground chicken breast patties. Poult. Sci. 79(1): 99-104.
• Murphy RY, Marks BP, Marcy JA (1998). Apparent specific heat of chicken breast patties and their constituent proteins by differential scanning calorimetry. J. Food Sci. 63(2): 88-91.
• Ngadi M, Li Y, Oluka S (2007). Quality changes in chicken nuggets fried in oils with different degrees of hydrogenation. Lebensm. Wiss. Technol. 40: 1784-91.
• Oztop MH, Sahin S, Sumnu G (2007). Optimization of microwave frying of potato slices by using Taguchi Technique. J. Food Eng. 79(1): 83-91.
• Öztan A (1999). Et Bilimi ve Teknolojisi, 19. ed., Hacettepe Üniversitesi Mühendislik Bilimi Yayınları, Ankara.
• Sahin S, Sumnu G, Oztop MH (2007). Effect of osmotic pretreatment and microwave frying on acrylamide formation in potato strips. J. Sci. Food Agric. 87(15): 2830-2836.
• Schreurs FJG (2000). Post-mortem changes in chicken muscle. World's Poult. Sci. J. 56(4): 319-346.
• Tornberg E (2005). Effects of heat on meat proteins – Implications on structure and quality of meat products, a review. Meat Sci. 70(3): 493-508.
• Wattanachant S, Benjakul S, Ledward DA (2005). Effect of heat treatment on changes in texture, structure and properties of Thai indigenous chicken muscle. Food Chem. 93(2): 337-348.
• Wilkinson JM (1978). The components of troponin from chicken fast skeletal muscle. A comparison of troponin T and troponin I from breast and leg muscle. Biochem. J. 169(1): 229-238.
• Zapata I, Reddish JM, Miller MA, Lilburn MS, Wick M (2012). Comparative proteomic characterization of the sarcoplasmic proteins in the pectoralis major and supracoracoideus breast muscles in 2 chicken genotypes. Poult. Sci. 91(7): 1654–1659.