Tenderization of Bovine Longissimus Dorsi Muscle using Aqueous Extract from Sarcodon aspratus.

Ho-Kyoung Kim, Sang-Hoon Lee, Youn-Chul Ryu
Author Information
  1. Ho-Kyoung Kim: Department of Culinary & Food Service Management, Sejong University, Seoul 143-747, Korea.
  2. Sang-Hoon Lee: Department of Nutritional Science and Food Management, College of Health Science, Ewha Womans University, Seoul 120-750, Korea.
  3. Youn-Chul Ryu: Division of Biotechnology, College of Applied Life Sciences, Jeju National University, Jeju 690-756, Korea.

Abstract

The aim of this study was to investigate the effects of aqueous extract from Sarcodon aspratus on tenderization of the bovine longissimus dorsi muscles in comparison with commercial proteolytic enzymes. Furthermore, meat quality and muscle protein degradation were examined. We marinated meat with 2% Sarcodon aspratus extract, 2% kiwi extract, and 0.2% papain. Beef chunks (3×3×3 cm(3)) were marinated with distilled water (control), Sarcodon aspratus extract (T1), kiwi extract (T2) or papain (T3) for 48 h at 4℃. There were no significant differences in muscle pH and lightness between control and treated samples. T1 had the lowest redness (p<0.01), and higher cooking loss and water holding capacity than control and T2 (p<0.05). T1 and T3 exhibited lower shear force values than control (p<0.05). Total protein solubility did not differ significantly between T1 and control, but T1 had less myofibrillar protein solubility than control and T2 (p<0.001). The degradation of myosin heavy chain in T1 and T3 was observed. This degradation of myofibrillar protein suggests that Sarcodon aspratus extract could influence tenderization. These results show that aqueous extract of Sarcodon aspratus extract actively affect the tenderness of the bovine longissimus dorsi muscle.

Keywords

References

  1. Nature. 1970 Aug 15;227(5259):680-5 [PMID: 5432063]
  2. J Anim Sci. 2002 Mar;80(3):617-27 [PMID: 11892678]
  3. Meat Sci. 2005 Nov;71(3):522-9 [PMID: 22060928]
  4. Immunopharmacology. 2000 Feb;46(2):113-21 [PMID: 10647870]
  5. J Appl Physiol (1985). 1993 Nov;75(5):2337-40 [PMID: 8307894]
  6. J Sci Food Agric. 1973 Dec;24(12):1583-8 [PMID: 4771842]
  7. J Biol Chem. 1949 Feb;177(2):751-66 [PMID: 18110453]
  8. Meat Sci. 2006 Jan;72(1):121-9 [PMID: 22061382]
  9. Electrophoresis. 1997 Oct;18(11):1967-72 [PMID: 9420154]
  10. Meat Sci. 2002 Nov;62(3):345-52 [PMID: 22061610]
  11. Meat Sci. 2006 Mar;72(3):555-9 [PMID: 22061740]
  12. Meat Sci. 2000 Nov;56(3):311-8 [PMID: 22062083]
  13. Meat Sci. 1997 Mar;45(3):339-52 [PMID: 22061472]
  14. Meat Sci. 1999 Jul;52(3):291-7 [PMID: 22062578]
  15. Meat Sci. 2004 Nov;68(3):363-9 [PMID: 22062404]
  16. Meat Sci. 2003 Oct;65(2):677-91 [PMID: 22063428]

Word Cloud

Created with Highcharts 10.0.0extractSarcodonaspratuscontrolT1proteinp<0tenderizationmuscledegradation2%T2T3aqueousbovinelongissimusdorsiproteolyticenzymesmeatmarinatedkiwipapainwater05solubilitymyofibrillaraimstudyinvestigateeffectsmusclescomparisoncommercialFurthermorequalityexamined0Beefchunks3×3×3cm3distilled48h4℃significantdifferencespHlightnesstreatedsampleslowestredness01highercookinglossholdingcapacityexhibitedlowershearforcevaluesTotaldiffersignificantlyless001myosinheavychainobservedsuggestsinfluenceresultsshowactivelyaffecttendernessTenderizationBovineLongissimusDorsiMuscleusingAqueousExtractbeef

Similar Articles

Cited By