Funkcjonalne wlasciwosci preparatu bialek miesniowych z kregoslupow dorsza baltyckiego

• Autorzy: Skierka E , Sadowska M. , Rzezuchowska E.

Warianty tytułu

EN

Functional properties of a muscle protein preparation from Baltic cod spine

• Języki publikacji: PL

Abstrakty

EN

The aim of the investigation was to establish the functional properties of muscle protein isolates from Baltic cod (Gadus morhua) spine which were also compared with a commercially available pork protein preparation. The muscle proteins were extracted in mild condition with 0.1M NaOH solution at 4°C and subsequently were precipitated at pH 4.5. The amino acid composition of protein isolates is similar to fresh muscle protein. At the basic pH values, the obtained preparation is almost three times more soluble than the commercially available pork protein. Cod proteins were in 25 and 90% solubilized at pH 8 and 12, respectively. At these pH values, after an increase of the ionic strength of the solution to 0.35, the protein solubility decreased about 10 and 15%, respectively. Spinal proteins at a pH range of 6-12 have a 16-time higher foaming capacity than that for pork proteins. The obtained proteins also have a two-times lower oil holding capacity and almost 5.5-times lower water holding capacity in comparison with the commercial preparation. The preparation of muscle proteins from Baltic cod had an ability to hold 0.26 g oil or 0.94 g water per g of protein. Its quite good functional properties encourage continuing research on the deodorization method. After deodorization this protein preparation could find an application in the food industry.

Słowa kluczowe

PL

ryby; dorsz baltycki; kregoslup; bialka miesniowe; preparat bialkowy z dorsza baltyckiego; wlasciwosci funkcjonalne

• Wydawca: -
• Czasopismo: Medycyna Weterynaryjna
• Rocznik: 2009
• Tom: 65
• Numer: 06
• Opis fizyczny: s.422-426,rys.,tab.,bibliogr.

Twórcy

autor

Skierka E

• Politechnika Gdanska, ul.Narutowicza 11/12, 80-952 Gdansk

autor

Sadowska M.

autor

Rzezuchowska E.

Bibliografia

• 1.Aluko R. E., Yada R. Y.: Structure - function relationships of cowpea (Vigna unguiculate) globulin isolate: influence of pH and NaCl physicochemical and functional properties. Food Chem. 1995, 53, 259-265.
• 2.Anon.: Meat and meat products - determination of L-hydroxyproline content. Reference method. International Standard, ISO 3496-1978 (E).
• 3.Aruna V., Prakash V.: Functional properties of the total proteins of sunflower (Helianthus annuus L.) seed. Effect of physical and chemical treatments. J. Agricul. Food Chem. 1993, 41, 18-23.
• 4.Barbut S.: Determining water and fat holding, [w:] Hall G. M. (red.): Methods of Testing Protein Functionality. Blackie Academic and Professional, New York 1999, 186-225.
• 5.Chavan U. D., McKenze D. B., Shahidi F.: Functional properties of protein isolates from beach pea (Lathyrus maritimus L.). Food Chem. 2001, 74, 177-187.
• 6.Diniz F. M., Martin A. M.: Effects of the extent of enzymatic hydrolysis on functional properties of shark protein hydrolysate. Lebensm.-Wiss.-Technol. 1997, 30, 266-272.
• 7.Fonkwe L. G., Singh R. K.: Protein recovery from mechanically deboned turkey residue by enzymic hydrolysis. Proc. Biochem. 1996, 31, 605-616.
• 8.Guan X., Yao H., Chen Z., Shan L., Zhang M.: Some functional properties of oat bran protein concentrate modified by trypsin. Food Chem. 2007, 101, 163-170.
• 9.Kaur M., Singh N.: Characterization of protein isolates from different Indian chickpea (Cicer arietinum L.) cultivars. Food Chem. 2007, 102, 366-374.
• 10.Khalid E. K., Babiker E. E., El Tinay A. H.: Solubility and functional properties of sesame seed proteins as influenced by pH and/or salt concentration. Food Chem. 2003, 82, 361-366.
• 11.Kijowski J., Stangierski J., Leśnierowski G.: Enzymatyczny hydrolizat białkowy z frakcji kostnej po mechanicznym odkostnieniu kurcząt. Przem. Spoż. 1992, 46, 149-152.
• 12.Lawal O. S., Adebowale K. O., Ogunsanwo B. M., Sosanowo O. A., Bankole S. A.: On the functional properties of globulin and albumin protein fractions and flours of African locust bean (Parkina biglobossa). Food Chem. 2005, 92, 681-691.
• 13.Lin C. S., Zayas J. F.: Functionality of defatted corn germ proteins in a model system: fat binding and water retention. J. Food Sci. 1987, 52, 1308-1311.
• 14.Lowry O. H., Rosebrough H. I., Farr A. L., Randall R. I.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193, 265-275.
• 15.Mwasaru M. A., Muhammad K., Bakar J., Che M., Yaakob B.: Effects of isolation technique and conditions on the extractability, physicochemical and functional properties of pigeonpea (Cajanus cajan) and cowpea (Vigna unguiculata) protein isolates. II. Functional properties. Food Chem. 1999, 67, 445-452.
• 16.Mwasaru M. A., Muhammad K., Bakar J., Che M., Yaakob B.: Influence of altered solvent environment on the functionality of pigeonpea (Cajanus cajan) and cowpea (Vigna unguiculata) protein isolates. Food Chem. 2000, 71, 157-165.
• 17.Oshodi A. A., Ojokan E.-O.: Effect of salts on some of the functional properties of bovine plasma protein concentrate. Food Chem. 1997, 59, 333-338.
• 18.Palka K., Sikorski Z. E., Rakowska M.: The recovery and nutritional evaluation of alkali extracted protein coagulates from crushed bone residues. Food Chem. 1985, 18, 291-299.
• 19.Pedroche J., Yust M. M., Lqari H., Girón-Calle J., Alaiz M., Vioque J., Millán F.: Brassica carinata protein isolates: chemical composition, protein characterization and improvement of functional properties by protein hydrolysis. Food Chem. 2004, 88, 337-346.
• 20.PN-75/A-04018. Oznaczenie azotu metodą Kjeldahla i przeliczanie na białko.
• 21.Ragab D. D. M., Babiker E. E., Eltinay A. H.: Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration. Food Chem. 2004, 84, 207-212.
• 22.Rutkowski A., Kozłowska H.: Preparaty żywnościowe z białka roślinnego. WNT, Warszawa 1981.
• 23.Sathe S. K., Deshpande S. S., Salunkhe D. K.: Functional properties of lupin seed (Lupinus mutabilis) proteins and protein concentrates. J. Food Sci. 1982, 47, 491-497.
• 24.Sathe S. K., Salunkhe D. K.: Functional properties of the Great Northern bean (Phaseolus vulgaris L.). Protein: emulsion, foaming, viscosity, and gelation properties. J. Food Sci. 1981, 46, 71-74.
• 25.Shahidi F., Han X.-Q., Synowiecki J.: Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem. 1995, 53, 285-293.
• 26.Sikorski Z. E.: Białka - budowa i właściwości, [w:] Sikorski Z. E. (red.): Chemia Żywności. WNT, Warszawa 2002, 243-277.
• 27.Sikorski Z. E.: Ryby i bezkęgowce morskie - pozyskiwanie, właściwości i przetwarzanie. WNT, Warszawa 2004, 64-73.
• 28.Sze-Tao K. W. C., Sathe S. K.: Functional properties and in vitro digestibility of almond (Prunus dulcis L.) protein isolate. Food Chem. 2000, 69, 153-160.
• 29.Tsumura K., Saito T., Tsuge K., Ashida H., Kugimiya W., Inouye K.: Functional properties of soy protein hydrolysates obtained by selective proteolysis. Lebensm.-Wiss.-Technol. 2005, 38, 255-261.
• 30.Yoshie-Stark Y., Wada Y., Wäsche A.: Chemical composition, functional properties, and bioactivities of rapeseed protein isolates. Food Chem. 2008, 107, 32-39.
• 31.Yu J., Ahmedna M., Goktepe I.: Peanut protein concentrate: Production and functional properties as affected by processing. Food Chem. 2007, 103, 121-129.