DOI QR코드

DOI QR Code

Physico-Chemical Characteristics Evaluation of White Pork Rind and Black Pork Rind

백돈피와 흑돈피의 이화학적 품질특성 평가

  • Jeon, Ki-Hong (Food Processing Technology Research Center, Korea Food Research Institute) ;
  • Hwang, Yoon-Seon (Food Processing Technology Research Center, Korea Food Research Institute) ;
  • Kim, Young-Boong (Food Processing Technology Research Center, Korea Food Research Institute) ;
  • Choi, Yun-Sang (Food Processing Technology Research Center, Korea Food Research Institute) ;
  • Kim, Byoung-Mok (Food Processing Technology Research Center, Korea Food Research Institute) ;
  • Kim, Dong-Wook (College of Animal Life Sciences, Kangwon National University) ;
  • Jang, Aera (College of Animal Life Sciences, Kangwon National University)
  • Received : 2015.06.22
  • Accepted : 2015.08.03
  • Published : 2015.08.31

Abstract

In order to determine the material characteristics of pork rinds according to the breeds, the chemical composition, color, pH, collagen contents, shear force, fatty acid and amino acid contents of pork rinds were investigated. White pork rinds (WPR) and black pork rinds (BPR) were evaluated before and after heating to compare the differences between breeds and the effects of heating treatment. In the chemical composition test, the respective moisture contents for WPR and BPR before heating were 49.90% and 53.75% but increased to 60.75% and 61.09% after heating. The test for crude protein and crude fat contents showed lower values after heating but WPR was higher than BPR. In the color test, the L value decreased rapidly with heating, dropping from 68.75 to 45.11 in WPR and from 67.22 to 49.64 in BPR. WPR had a higher L value and a lower a value than BPR before heating but had a higher L value and a lower a value than WPR after heating. pH was significantly higher in WPR than BPR regardless of heating (p<0.05). The collagen content for WPR and BPR was 10.38 g/100 g and 11.54 g/100 g but increased to 12.00 g/100 g in WPR and decreased to 11.40 g/100 g in BPR after heating. The shear force of 26.14 kgf in WPR was significantly higher than 12.89 kgf in BPR before heating (p<0.05), but the values decreased significantly after heating in both WPR and BPR. Linoleic acid in WPR was 17.29%, which was higher than 15.13% in BPR. The USFA for BPR was also higher than WPR. In amino acid composition, the EAA contents in WPR was 7,190 mg%, which was higher than 5,520 mg% in BPR.

Keywords

References

  1. AOAC. 2005. The Association Official methods of analysis. 18th ed., pp.1-24
  2. Campos H, Wilson Peter WF, Jimenez D, Mcnamara JR, Ordovas J, Schaefer EJ. 1990. Differences in apolipoprotein subfractions in postmenopausal women on and off estrogen therapy: Results from the Framingham offspring study. Metabolism : Clinical and Experimental 39:1033-1038 https://doi.org/10.1016/0026-0495(90)90162-6
  3. Cho YJ, Seo JE, Kim YJ, Lee NH, Hong SP, Kim YH. 2006. Study on the degradation of pigskim collagen using irradiation technique. J Korean Soc Food Sci Nutr 35:588-593 https://doi.org/10.3746/jkfn.2006.35.5.588
  4. Folch J, Less M, Sloane GH. 1957. A simple method for the isolation and purification of total lipids from animal tissues. J Biology and Chemistry 226:497-509
  5. Han CJ, Kang SM. 2008. The effect of collagen supplementation from pork skin on serum collagen, serum sex steroid hormone, serum lipid, and skin crack in Korean middle-aged women. Korean J Community Nutr 13:912-921
  6. Jeon YS, Kang SM. 2009. Influence of collagen intake upon facial-skin wrinkles. Korean Sci Aesthetics Cosmetics 7:79-94
  7. Kim CJ, Lee BM. 1988. Studies on utilization of pork skin gelatin as a binder or extender in sausage emulsion. Korean J Ani Sci 30:678-684
  8. Korea Pork Producers Association. 2014. Available from http://www.koreapork.or.kr [cited 2012 January 18]
  9. Lee GM. 1987. Effective production and usage of pork rind. The Korea Swine Journal 9:148-153
  10. Lee YJ, Kim CJ, Park BY, Sung PN, Kim JH, Kang KH, Kim DH, Cho SH. 2009. Warner-bratzler shear force, sarcomere length, total collagen contents and sensory characteristics of hanwoo beef (Korean native cattle) quality grade. Korean J Food Sci An 29:726-735 https://doi.org/10.5851/kosfa.2009.29.6.726
  11. National Academy of Agricultural Science. 2012. Food Composition Table. pp 500-502. Kyomunsa
  12. Osburn WN. 1996. Improving the functionality of recovered tissue protein. PhD. Thesis, Nebraska-Lincoln Univ. NE
  13. Ross RK, Pagamm HA, Mark TM, Henderson BE. 1989. Cardiovascular benefits of estrogen replacement therapy. Am J Obset Gynecol 160:1301-1306 https://doi.org/10.1016/S0002-9378(89)80017-1
  14. Sa MS. 2003. Diet snack using pig skin. Korea Patent
  15. Seong PN, Cho SH, Kim JH, Hah KH, Park BY, Lee JM, Kim DH. 2009. Meat quality of pork muscles from low-fat cuts. Korean J Ani Sci 29:364-373
  16. Shin MH. 2002. Properties of collagen extracted from chicken foot skins. J Culinary Research 8:95-105
  17. Yang SJ, Hong JH. 2012. Extraction and physicochemical properties of collagen from squid skin and alaska pollack skin. Korean J Food Cookery Sci 28:711-719 https://doi.org/10.9724/kfcs.2012.28.6.711
  18. Yang YS, Kim YH, Kim CJ, Lee MH, Lee CH. 1990. Manufacture of pork rind snack by extrusion cooking process. Korean J Food Sci 22:451-455