JOURNAL BROWSE
Search
Advanced SearchSearch Tips
Tenderization of Bovine Longissimus Dorsi Muscle using Aqueous Extract from Sarcodon aspratus
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Tenderization of Bovine Longissimus Dorsi Muscle using Aqueous Extract from Sarcodon aspratus
Kim, Ho-Kyoung; Lee, Sang-Hoon; Ryu, Youn-Chul;
  PDF(new window)
 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 cm3) 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
Sarcodon aspratus;proteolytic enzymes;beef;tenderization;
 Language
English
 Cited by
 References
1.
Ahnstrom, M. L., Enfalt, A. C., Hansson, I., and Lundstrom, K. (2006) Pelvic suspension improves quality characteristics in m. semimembranosus from Swedish dual purpose young bulls. Meat Sci. 72, 555-559. crossref(new window)

2.
Cho, H. Y., Jeong, S. H., and Cho, N. S. (2004) Effect of Neungi (Sarcodon aspratus) mushroom and its protease addition on the meat tenderizing. Mokchae Konghak 32, 39-44.

3.
Douglas, N., Hodes, D. N., and Dransfield, E. (1973) Effect of pre-slaughter injections of papain on toughness in lamb muscle induced by rapid chillings. J. Sci. Food Agric. 24, 1583-1587. crossref(new window)

4.
Ezmart, M., Ialaki, E., and Hamza, M. A. (1979) Edible mushrooms as producers of amylases. Food Chem. 4, 203-211. crossref(new window)

5.
Gerelt, B., Ikeuchi, Y., and Suzuki, A. (2000) Meat tenderization by proteolytic enzymes after osmotic dehydration. Meat Sci. 56, 311-318. crossref(new window)

6.
Gil, M., Ramirez, J. A., Pla, M., Arino, B., Hernandez, P., Pascual, M., Blasco, A., Guerrero, L., Hajos, G., Szerdahelyi, E. N., and Oliver, M. A. (2006) Effect of selection for growth rate on the ageing of myofibrils, meat texture properties and the muscle proteolytic potential of m. longissimus in rabbits. Meat Sci. 72, 121-129. crossref(new window)

7.
Gornall, A. G., Bardawill, C. J., and David, M. M. (1949) Determination of serum-protein by means of the biuret reaction. J. Biol. Chem. 177, 751-766.

8.
Hamm, R. and Deatherage, F. E. (1960) Changes in hydration solubility and charges of muscle proteins during hearting of meat. Food Res. 25, 587-610. crossref(new window)

9.
Hiizu, E., Yuji, N., Shoichiro, I., and Takeshi, T. (1995) Myosin heavy chain-degrading proteinase from spear squid muscle. Food Res. Intern. 28, 31-36. crossref(new window)

10.
Huff-Lonergan, E., Bass, T. J., Malek, M., Dekkers, J. C. M., Pursa, K., and Rothschild, M. F. (2002) Correlations among selected pork quality traits. Meat Sci. 80, 617-627.

11.
Hwang, I. H., Devine, C. E., and Hopkins, D. L. (2003) The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness: A review. Meat Sci. 65, 677-691. crossref(new window)

12.
Joo, S. T., Kauffman, R. G., Kim, B. C., and Park, G. B. (1999) The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci. 52, 291-297. crossref(new window)

13.
Kang, C. K. and Rice, E. E. (1970) Degradation of various meat fraction by tenderizing enzyme. J. Food Sci. 35, 563-567. crossref(new window)

14.
Kang, H. C., Yun, B. D., Yu, S. H., and Yoo, I. C. (2000) Chemical structure of the compounds isolated from the mushroom Sarcodon asparatus. Can. J. Chem. 65, 2369-2372.

15.
Kim, H. I. and Taub, I. A. (1991) Specific degradation of myosin in meat by bromelain. Food Chem. 40, 337-342. crossref(new window)

16.
Kim, H. K. (2013) Effect of mixed tenderizer using Sarcodonaspratus and kiwi on beef. Ph.D. thesis, Sejong Univ., Seoul, Korea.

17.
Koohmaraie, M., Kent, M. P., Shackelford, S. D., Veiseth, E., and Wheeler, T. L. (2002) Meat tenderness and muscle growth: Is there any relationship? Meat Sci. 62, 345-352. crossref(new window)

18.
Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227, 680-685. crossref(new window)

19.
Lee, J. H. and Jang, H. R. (2005) Proteolytic properties of Sarcodon aspratus on beef loin. Korean J. Culinary Res. 11, 110-124.

20.
Mizuno, M., Shiomi, Y., Minato, K., Kawakami, S., Ashida, H., and Tsuchida, H. (2000) Fucogalactan isolated from Sarcodon aspratus elicits release of tumor necrosis factor and nitric oxide from murine macrophages. Immunopharmacology 46, 113-121. crossref(new window)

21.
Naveena, B. M., Mendiratta, S. K., and Anjaneyulu, A. S. R. (2004) Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Meat Sci. 68, 363-369. crossref(new window)

22.
Rivero, J. L. L., Talmadge, R. J., and Edgerton, V. R. (1997) A sensitive electrophoretic method for the quantification of myosin heavy chain isoforms in horse skeletal muscle: Histochemical and immunocytochemical verifications. Electrophoresis 18, 1967-1972. crossref(new window)

23.
Ryu, Y. C., Choi, Y. M., and Kim, B. C. (2005) Variation in metabolite contents and protein denaturation of the longissimus dorsi muscle in various porcine quality classifications and metabolic rates. Meat Sci. 71, 522-529. crossref(new window)

24.
SAS (2001) SAS user's guide, version 8.2. Cary, NC: SAS Institute Inc.

25.
Song, J. H., Lee, H. S., Hwang, J. K., Han, J. W., Ro, J. G., Keum, D. H., and Park, K. M. (2003) Physiological activity of Sarcodon aspratus extracts. Korean J. Food Sci. Anim. Resour. 23, 172-179.

26.
Talmadge, R. J. and Roy, R. R. (1993) Electrophoretic separation of rat skeletal muscle myosin heavy chain isoforms. J. Appl. Physiol. 75, 2337-2340.

27.
Wada, M., Suzuki, T., Yaguti, Y., and Hasegawa, T. (2002) The effects of pressure treatments with kiwi fruit protease on adult cattle semitendinosus muscle. Food Chem. 78, 167-171. crossref(new window)

28.
Warner, R. D., Kauffman, R. G., and Greaser, M. L. (1997). Muscle protein changes post mortem in relation to pork traits. Meat Sci. 45, 339-352. crossref(new window)

29.
Yamasaki, Y. and Suzuki, Y. (1978) Purification and properties of β-glucosidase and glucamylase from Lentinus deodes. Agri. Biol. Chem. 42, 971-980. crossref(new window)