Effect of rosemary transglutaminase on yoghurt fortified with whey protein isolate

• Autorzy: Ibrahim O. , Glibowski P. , Nour M. , El-Hofi M. , El-Tanboly E.-S. , Abd-Rabou N.
• Języki publikacji: EN

Abstrakty

EN

Rosemary (Rosmarinus officinalis L.) transglutaminase (RTGase) was used to cross-link whey protein isolate (WPI) and its ability to induce gelation was investigated. The rheological and textural properties of WPI were improved with RTGase treatment. Set-type yoghurts fortifi ed with 1% WPI powder treated with RTGase at the level of 2.5 and 10 unit/g protein were studied. Chemical, rheological, textural and organoleptic properties of the yoghurt treated with RTGase were better than these of the control yoghurt.

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2017
• Tom: 67
• Numer: 4
• Opis fizyczny: p.265-274,fig.,ref.

Twórcy

autor

Ibrahim O.

• Dairy Sciences Department, National Research Centre in Dokki, Cairo, Egypt

autor

Glibowski P.

• Department of Biotechnology, Human Nutrition and Food Raw Material Science, University of Life Sciences in Lublin, Skromna 8, 20–704 Lublin, Poland

autor

Nour M.

• Dairy Department, Faculty of Agriculture, Al-Azhar University, Cairo, Egypt

autor

El-Hofi M.

• Dairy Sciences Department, National Research Centre in Dokki, Cairo, Egypt

autor

El-Tanboly E.-S.

• Dairy Sciences Department, National Research Centre in Dokki, Cairo, Egypt

autor

Abd-Rabou N.

• Dairy Sciences Department, National Research Centre in Dokki, Cairo, Egypt

Bibliografia

• 1. Ando H., Adachi M., Umeda K., Matsuura A., Nonaka M., Uchio R, Purifi cation and characterization of a novel transglutaminase derived from micro-organisms. Agric. Biol. Chem., 1989, 53, 2613–2617.
• 2. AOAC, Offi cial Methods of Analysis. (16thed). 1995, Arlington, VA, USA: Association of Official Analytical Chemists.
• 3. Bönisch M.P., Huss M., Lauber S., Kulozik U., Yoghurt gel formation by means of enzymatic protein cross-linking during microbial fermentation. Food Hydrocoll., 2007a, 21, 585–595.
• 4. Bönisch M.P., Huss M., Weld K., Kulozik U., Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties. Int. Dairy J., 2007b, 17, SI, 1360–1371.
• 5. Del Duca S., Serafini-Fracassini D., Transglutaminases of higher, lower plants and fungi. 2005, in: Transglutaminases Family of Enzymes with Diverse Functions (eds. K. Mehta, R. Eckert). Karger, Basel, Switzerland. Prog. Tumor Res., 2005, 38, 223–247.
• 6. Del Duca S., Serafini-Fracassini D., Bonner P., Cresti M., Cai G., Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin fi laments. Biochem. J., 2009, 418, 651–664.
• 7. Di Sandro A., Del Duca S., Verderio E., Hargreaves A., Scarpellini A., Cai G., Cresti M., Faleri C., Iorio R., Hirose S., Furutani Y., Coutts L., Griffi n M., Bonner P., Serafini-Fracassini D., An extracellular transglutaminase is required for apple pollen tube growth. Biochem. J., 2010, 429, 261–271.
• 8. Domagała J., Wszołek M., Tamime A.Y., Kupiec-Teahan B., The effect of transglutaminase concentration on the texture, syneresis and microstructure of set-type goat’s milk yoghurt during the storage period. Small Rum. Res., 2013, 112, 154–161.
• 9. Eissa A.S., Khan S.A., Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme. Food Hydrocoll., 2006, 20, 543–547.
• 10. El-Hofi M., Ismail A., Nour M., Ibrahim O., Isolation, purifi - cation and characterization of transglutaminase from rosemary (Rosmarinus offi cinalis L.) leaves. Acta Sci. Pol. Technol. Alim., 2014, 13, 267–278.
• 11. Færgemand M., Qvist K.B., On the importance of using Ca+2-independent transglutaminase for cross-linking of β-lactoglobulin. Food Hydrocoll., 1999, 13, 199–201.
• 12. Færgemand M., Otte J., Qvist K.B., Enzymatic cross-linking of whey proteins by a Ca+2-indpendent microbial transglutaminase from Streptomyceslydicus. Food Hydrocoll., 1997, 11, 19–25.
• 13. Farnsworth J.P., Li J., Hendricks G.M., Guo M.R., Effects of transglutaminase treatment on functional properties and probiotic culture survivability of goat milk yogurt. Small Rum. Res., 2006, 65, 113–121.
• 14. Folk J.E., Cole P.W., Identification of a functional cysteine essential for the activity of guinea pig liver transglutaminase. J. Biol. Chem., 1966, 241, 3238–3240.
• 15. Gauche C., Barreto P.L.M., Bordignon-Luiz M.T., Effect of thermal treatment on whey protein polymerization by transglutaminase: Implications for functionality in processed dairy foods. LWT-Food Sci. Technol., 2010, 43, 214–219.
• 16. Gauche C., Tomazi T., Barreto P.L.M., Ogliari P.J., Bordignon- Luiz M.T., Physical properties of yoghurt manufactured with milk whey and Transglutaminase. LWT-Food Sci. Technol., 2009, 42, 239–243.
• 17. Genena A.K., Hense H., Smânia Junior A., Machado de Souza S., Rosemary (Rosmarinus offi cinalis) – a study of the composition, antioxidant and antimicrobial activities of extracts obtained with supercritical carbon dioxide. Ciência Tecnol. Alime., 2008, 28, 463–469.
• 18. Griffin M., Casadio R., Bergamini C.M., Transglutaminases: Nature’s biological glues. Biochem. J., 2002, 368, 377–396.
• 19. Guyot C., Kulozik U., Effectof transglutaminase-treated milk powders on thepropertiesofskim milk yoghurt. Int. Dairy J., 2011, 21, 628–635.
• 20. Ha G., Iuchi I., Transglutaminase. 2003, in: Handbook of Food Enzymology (eds. J.R. Whitaker, A.G. Voragen, D.W.S. Wong). Marcel Dekker, Inc., Basel, New York, p. 51.
• 21. Hernàndez-Balada E., Taylor M.M., Phillips J.G., Marmer W.N., Properties of biopolymers produced by transglutaminase treatment of whey protein isolate and gelatin. Biores. Technol., 2009, 100, 3638–3643.
• 22. Iličić M.D., Carć M.D., Milanović S.D., Dokić L.P.L.J., Ðurić M., Bošnjak G., Duraković K., Viscosity changes of probiotic yoghurt with transglutaminase during storage. APTEFF, 2008, 39, 11–19.
• 23. Iličić M.D., Milanović S.D., Carć M.D., Dokić L.P., Kanurić K.G., Effect of transglutaminase on texture and flow properties of stirred probiotic yoghurt during storage. J. Texture Stud., 2014, 45, 13–19.
• 24. Jaros D., Partschefeld C., Henle T., Rohm H., Transglutaminase in dairy products: chemistry, physics, applications. J. Texture Stud., 2006, 37, 113–155.
• 25. Kang H., Cho Y.D., Purifi cation and properties of transglutaminase from soybean (Glycine max) leaves. Biochem. Biophys. Res. Commun., 1996, 223, 288–292.
• 26. Kücükcetin A., Effect of heat treatment and casein to whey protein ratio of skim milk on graininess and roughness of stirred yoghurt. Food Res. Int., 2008, 41, 165–171.
• 27. Lauber S., Henle T., Klostermeyer H., Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt. Eur. Food Res. Technol., 2000, 210, 305–309.
• 28. Li-Chan E.C.Y., Properties of proteins in food systems: an introduction. 2004, in: Proteins in Food Processing (ed. R.Y. Yada). CRC Press, Boca Raton, FL, pp. 2–26.
• 29. Lilley G.R., Skill J., Griffi n M., Philip L.R., Detection of Ca+2 -dependent transglutaminase activity in root and leaftissue of monocotyledonous and dicotyledonous plants. Plant Physiol., 1998, 117, 1115–1123.
• 30. Lin S., Hsieh Y., Wang P., Chu W., Efficient purification of transglutaminase from recombinant Streptomyces platensis at various scales. Biotechnol. Lett., 2007, 29, 111–115.
• 31. Lorenzen P.C., Schlimme E., Properties and potential fields of application of transglutaminase preparations in dairying. Bull. Int. Dairy Fed., 1998, 332, 47–53.
• 32. Lorenzen P.C., Neve H., Mautner A., Schlimme E., Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yogurt. Int. J. Dairy Technol., 2002, 55, 152–157.
• 33. Loveday S.M., Sarkar A., Singh H., Innovative yoghurts: Novel processing technologies for improving acid milk gel texture. Trends Food Sci. Technol., 2013, 33, 5–20.
• 34. Maifreni M., Marino M., Pittia P., Rondinini G., Textural and sensorial characterization of Montasio cheese produced using proteolytic starters. Milchwissenchaft – Milk Sci. Int., 2002, 57, 23–26.
• 35. Motoki M., Kumazawa Y., Recent research trends in transglutaminase technology for food processing. Food Sci. Technol. Res., 2000, 6, 151–160.
• 36. Ozer B., Kirmaci H.A., Oztekin S., Hayaloglu A., Atamer M., Incorporation of microbial transglutaminase into non-fat yogurt production. Int. Dairy J., 2007, 17, 199–207.
• 37. Şanli T., Sezgin E., Deveci O., Şenel E., Benli M., Effect of using transglutaminase on physical, chemical and sensory properties of set-type yoghurt. Food Hydrocoll., 2011, 25, 1477–1481.
• 38. SAS Institute, SAS User’s Guid / STAT. 1990, Ver. 6.04, 4th ed., SAS Inst. Inc. Cary, NC.
• 39. Serafini-Fracassini D., Del Duca S., Transglutaminases: widespread cross-linking enzymes in plants. Ann. Bot., 2008, 102, 145–152.
• 40. Serafini-Fracassini D., Del Duca S., Monti F., Poli F., Sacchetti G., Bregoli A., Biondi S., Della Mea M., Transglutaminase activity during senescence and programmed cell death in the corolla of tobacco (Nicotiana tabacum) flowers. Cell Death Differ., 2002, 9, 309–321.
• 41. Signorini M., Beninati S., Bergamini D., Identifi cation of transglutaminase activity in the leaves of Silver Beet (Beta vulgaris L.). J. Plant Physiol., 1991, 137, 547–552.
• 42. Truong V.D., Clare D.A., Catignani G.L., Swaisgood H.E., Cross-linking and rheological changes of whey proteins treated with microbial transglutaminase. J. Agr. Food Chem., 2004, 52, 1170–1175.
• 43. Tsevdou M.S., Eleftheriou E.G., Taoukis P.S., Transglutaminase treatment of thermally and high pressure processed milk: Effects on the properties and storage stability of set yoghurt. Food Sci. Emerg. Technol., 2013, 17 144–152.
• 44. Wilcox C.P., Swaisgood H.E., Modifi cation of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase. J. Agric. Food Chem., 2002, 50, 5546–5551.
• 45. Wróblewska B., Kaliszewska A., Kołakowski P., Pawlikowska K., Troszyńska A., Impact of transglutaminase reaction on the immunoreactive and sensory quality of yoghurt starter. World J. Microbiol. Biotechnol., 2011, 27, 215–227.

Identyfikatory

DOI

10.1515/pjfns-2016-0020