Nowa wersja platformy, zawierająca wyłącznie zasoby pełnotekstowe, jest już dostępna.
Przejdź na https://bibliotekanauki.pl

PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2008 | 58 | 1 |
Tytuł artykułu

Properties and application of egg white lysozyme and its modified preparations - a review

Treść / Zawartość
Warianty tytułu
PL
Wlasciwosci i zastosowanie lizozymu z bialka jaja i jego modyfikowanych preparatow - artykul przegladowy
Języki publikacji
EN
Abstrakty
EN
Lysozyme monomer exhibits strong antibacterial activity against Gram-positive organisms. This phenomenon has found a practical application in the food processing industry, in medicine and pharmaceutical industry. The use of lysozyme in the food processing industry is connected primarily with its application as a natural preservative. The enzyme is widely used as a preservative for meat, fish and their products, for milk and dairy products, as well as for fruit and vegetables. The pharmaceutical industry uses this enzyme in the manufacture of adjuvant drugs for antibiotics and analgesics in viral and bacterial infections, in the treatment of leukemia and neoplastic diseases. Lysozyme is also used as a diagnostic agent, being an indicator of the occurrence and the progression of pathological changes in humans and animals. The range of the practical applications of lysozyme may be considerably extended as a result of its modification. The enzyme after modification exhibits a new specific activity in relation to Gram-negative bacteria, being a result of dimerization, with no loss of activity against Gram-positive bacteria, characteristic for the monomer, as it was indicated in studies by Ibrahim et al. [1991;1996], Lesnierowski et al. [2004] and Kijowski et al. [2006]. The dimeric form of lysozyme has been used in the treatment of bacterial and viral animal diseases. A drug produced on the basis of lysozyme dimer shows immunostimulating and immunocorrective activity.
PL
Monomer lizozymu wykazuje silne działanie przeciwbakteryjne w stosunku do bakterii Gram-dodatnich. To zjawisko znalazło praktyczne zastosowanie w przemyśle spożywczym, w medycynie i przemyśle farmaceutycznym. Wykorzystanie lizozymu w przemyśle spożywczym jest związane głównie z jego zastosowaniem jako naturalnego środka konserwującego. Ten enzym jest szeroko stosowany jako środek utrwalający mięso, ryby, ich przetwory, mleko i produkty mleczne, jak również owoce i warzywa. Przemysł farmaceutyczny wykorzystuje lizozym w produkcji adiuwantów dla antybiotyków i środków przeciwbólowych w infekcjach wirusowych i bakteryjnych, w leczeniu białaczki i chorób nowotworowych. Lizozym jest także wykorzystywany jako środek diagnostyczny, będący wskaźnikiem występowania i zaawansowania zmian patologicznych u ludzi i zwierząt. Zakres praktycznych zastosowań lizozymu może się znacznie zwiększyć w wyniku jego modyfikacji. Enzym wykazuje wtedy nową specyficzną aktywność w stosunku do bakterii Gram–, będącą rezultatem dimeryzacji; właściwości w stosunku do bakterii Gram+, właściwe dla monomeru, są zachowane – o czym świadczą wyniki badań: Ibrahim et al. [1991, 1996]; Lesnierowski et al. [2004] oraz Kijowski et al. [2006]. Lizozym w formie dimeru wykorzystuje się w leczeniu chorób bakteryjnych i wirusowych zwierząt. Lek wyprodukowany na bazie dimeru lizozymu wykazuje działanie immunostymulujące i immunokorekcyjne.
Wydawca
-
Rocznik
Tom
58
Numer
1
Opis fizyczny
p.5-10,ref.
Twórcy
  • A.Cieszkowski Agricultural University, Wojska Polskiego 31, 60-624 Poznan, Poland
autor
Bibliografia
  • 1. Ahvenainen R., Heikonen M., Kreula M., Linko M., Linko P., Separation of lysozyme from egg white. J. Process Eng., 1979, 2, 301-310.
  • 2. Alderton G., Fevold H.L., Direct crystallization of lysozyme from egg white and some crystalline salts of lysozyme. J. Biol. Chem., 1946, 1, 1-5.
  • 3. Atrih A., Bacher G., Allmaier G., Williamson M.P., Foster S.J., Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J. Bacteriol., 1999, 181, 3956-3966.
  • 4. Banka L., Petrovic S, Becarevic, A., Lysozyme isolation from hen egg white on Fractogel TSK CM-650. Lebensm. Wissen. Unters Technol., 1993, 26, 76-79.
  • 5. Baron F., Réhault S., Compounds with antibacterial activity. 2007, in: Bioactive Egg Compounds (eds. R. Huophalathi, R. Lopez-Fandiño, M. Anton, R. Schade). Springer-Verlag, Berlin Heidelberg, pp. 191-198.
  • 6. Bera A., Herbert S., Jacob A., Vollmer W., Götz F., Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferaze OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol. Microbiol., 2005, 55, 778-787.
  • 7. Boland J.S., Davidson P.M., Weiss, J., Enhanced inhibition of Escherichia coli O 157:H7 by lysozyme and chelators. J. Food Prot., 2003, 66, 1783-1789.
  • 8. Carniero de Melo A.M.S., Cassar C.A., Miles R.J., Trisodium phosphate increases sensitivity of gram-negative bacteria to lysozyme and nisin. J. Food Prot., 1988, 61, 839-844.
  • 9. Cegielska-Radziejewska R., Lesnierowski G., Kijowski J., Antibacterial activity of lysozyme modified by the membrane technique. Electronic Journal of Polish Agricultural Universities, 2003, 6, (2), [www.ejpau.media.pl].
  • 10. Chander H., Lata K., Batish K.L., Bhatia, K.L., Antibacterial ac tivity of lysozyme against some common food poisoning organisms. Arch. Lebensmittelhyg., 1984, 35, 87-92.
  • 11. Chang C.T., Chen L.H., Sung H.Y., Kao M.D., Studies on the purification of lysozyme from egg white by ultrafiltration. J. Chin. Agr. Chem. Soc., 1986, 24, 86-93.
  • 12. Chiang B.H., Su C.K., Tsai G.J., Tsao G.T., Egg white lysozyme purification by ultrafiltration and affinity chromatography. J. Food Sci., 1993, 58, 303-306.
  • 13. Chiu H.C., Lin C.W., Suen S.Y., Isolation of lysozyme from hen egg albumen using glass fiber-based cation exchange membranes. J. Membrane Sci., 2007, 290, 259-266.
  • 14. Danyluk B., Kijowski J., The effect of lysozyme monomer on the growth of Clostridium tyrobutyricum. Przem. Spoż., 2001, 12, 16‑19 (in Polish).
  • 15. Durance T.D., Separation, purification, and thermal stability of lysozyme and avidin from chicken egg white. 1994, in: Egg Uses and Processing Technologies, New Developments (eds. J.S. Sim, S. Nakai). International CAB, Wallingford, UK, pp. 77-93.
  • 16. Düring K., Porsch P., Mahn A., Brinkmann O., Gieffers W., The non-enzymatic microbicidal activity of lysozyme. FEBS Lett., 1999, 449, 93-100.
  • 17. Gill A.O., Holley R.A., Inhibition of bacterial growth on ham and bologna by lysozyme, nisin and EDTA. Food Res. Int., 2000, 33, 83-90.
  • 18. Hughey V.L., Johnson E.A., Antimicrobial activity of lysozyme against bacteria involved in food spoilage and food-borne disease. Appl. Environ. Microbiol., 1987, 53, 2165-2170.
  • 19. Ibrahim H.R., On the novel catalytically-independent antimicrobial function of hen egg-white lysozyme: A conformation-dependent activity. Nahrung, 1998, 42, 187-193.
  • 20. Ibrahim H.R., Hen egg white lysozyme and ovotransferrin: mystery, structural role and antimicrobial function. 2003, in: Proceedings of the Xth European Symposium on the Quality of Eggs and Egg Products (ed. Y. Nys). Saint-Brieuc, France, pp. 350-365.
  • 21. Ibrahim H.R., Higashiguchi S., Juneja L.R., Kim M., Yamamoto T., A structural phase of heat-denatured lysozyme with novel antimicrobial action. J. Agric. Food Chem., 1996, 44, 1416-1423.
  • 22. Ibrahim H.R., Higashiguchi S., Sugimoto Y., Aoki, T., Role of divalent cations in the novel bactericidal activity of the partially unfolded lysozyme. J. Agric. Food Chem., 1997, 45, 89-94.
  • 23. Ibrahim H.R., Kato A., Kobayashi K., Antimicrobial effects of lysozyme against Gram-negative bacteria due to covalent binding of palmitic acid. J. Agric. Food Chem., 1991, 39, 2077-2082.
  • 24. Ibrahim, H.R., Kobayashi, K., Kato A., Length of hydrocarbon chain and antimicrobial action to Gram-negative bacteria of fatty acylated lysosome. J. Agric. Food Chem., 1993, 41, 1164-1168.
  • 25. Ibrahim H.R., Yamada M., Matsushita K., Kobayashi K., Kato A., Enhanced bactericidal action of lysozyme to Escherichia coli by inserting a hydrophobic pentapeptide into C Terminus. J. Biol. Chem., 1994, 269, 5059-5063.
  • 26. Ibrahim H. R., Matsuzaki T., Aoki T., Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Lett., 2001, 506, 27-32.
  • 27. Johnson, E.A., Egg-white lysozyme as a preservative for use in foods. 1994, in: Egg Uses and Processing Technologies, New Developments (eds. J.S. Sim, S. Nakai). International CAB, Wallingford, UK, pp. 177-191.
  • 28. Jolles P., Jolles J. What’s new in lysozyme research? Mol. Cell. Biochem., 1984, 63, 165-189.
  • 29. Kato A., Nakamura S., Ibrahim H., Matsumi T., Tsumiyama C., Kato M., Production of genetically modified lysozymes having extreme heat stability and antimicrobial activity against Gram negative bacteria in yeast and in plant. Nahrung, 1998, 42, 128‑130.
  • 30. Kiczka W., From monomer to dimmer of lysozyme. Życie Wet., 1994, 4A, 131-136 (in Polish; English abstract).
  • 31. Kijowski J., Cegielska-Radziejewska R., Leśnierowski G., Antibacterial action of chemical and chemical-thermally modified hen egg lysozyme. 2006, in: Proceedings of the XIIth European Poultry Conference. Verona, Italy, 10-14 September 2006.
  • 32. Kijowski, J., Lesnierowski, G., Fabisz-Kijowska, A., Methods of lysozyme separation, enzyme molecular form and functional quality of the residual egg white. 1998, in: Proceedings of the 2nd International Symposium on Egg Nutrition and Newly Emerging Ovo-Technologies. Banff, Alberta, p. 54 (Abstract).
  • 33. Kijowski J., Lesnierowski G., Fabisz-Kijowska A., Lysozyme polymer formation and functionality of residuals after lysozyme extraction. 2000, in: Egg Nutrition and Biotechnology (eds. J.S. Sim, S. Nakai, W. Guenter). International CAB, Wallingford, UK, pp. 269-285.
  • 34. Kijowski J., Marciszewska C., Cegielska-Radziejewska R., Quality and microbiological stability of chilled chicken breast muscles treated with a lysozyme solution. Pol. J. Food Nutr. Sci., 2002, 11/52, 47-54.
  • 35. Kopeć W., Trziszka T., Lysozyme and its characteristics. Part II. Isolation and practical applications. Przem. Spoż., 1997, 51, 36‑37 (in Polish).
  • 36. Kopeć W., Skiba T., Korzeniowska M., Bobak Ł., Trziszka T., Activity of protease inhibitors and lysozyme of hen’s egg depending on feed modification and egg storage. Pol. J. Food Nutr. Sci., 2005, 14/55, 79-83.
  • 37. Lesnierowski G., Cegielska-Radziejewska R., Kijowski J., Thermally and chemical-thermally modified lysozyme and its bacteriostatic activity. World’s Poultry Sci. J., 2004, 60, 303-310.
  • 38. Lesnierowski G., Kijowski J., Enzymatic activity of lysozyme and its application for food preservation. Przem. Spoż., 1995, 49, 116–119 (in Polish).
  • 39. Lesnierowski G., Kijowski, J., Lysozyme sorption techniques on ion exchange matrix. 1997, in: Proceedings of the 7th European Symposium on the Quality of Eggs and Egg Products (eds. J. Kijowski, J. Pikul). WPSA Polish Branch, Poznan, Poland, pp. 307-313.
  • 40. Lesnierowski G., Kijowski J., Isolation of lysozyme from hen egg white by ion-exchange techniques and its spray drying dehydratation. Pol. J. Food Nutr. Sci., 2001, 51/2, 43-47.
  • 41. Lesnierowski G., Kijowski J., Separation of lysozyme from chicken egg white by direct ultrafiltration method. Żywność, 2002, 31, 2, 59-69 (in Polish; English abstract).
  • 42. Lesnierowski G., Kijowski J., Lysozyme. 2007, in: Bioactive Egg Compounds (eds. R. Huophalathi, R. Lopez-Fandiño, M. Anton, R. Schade). Springer-Verlag, Berlin Heidelberg, pp. 33-42.
  • 43. Lesnierowski G., Kijowski J., Magnuski, T., The use of ultrafiltration in desalination of egg white after the process of lysozyme isolation. Przem. Spoż., 1993, 47, 476-479 (in Polish; English abstract).
  • 44. Leśnierowski G., Kijowski J., Kopeć W., Karkoszka K., Method of lysozyme enrichment. Poland, patent No. 377130, 19.09.2005 (in Polish).
  • 45. Li-Chan E., Nakai S., Sim J., Bragg D.G., Lo K.V., Lysozyme separation from egg white by cation exchange column chromatography. J. Food Sci., 1986, 51, 1032-1036.
  • 46. Liu S.T., Sugimoto T., Azakami H., Kato A., Lipophilization of lysozyme by short and middle chain fatty acids. J. Agric. Food Chem., 2000, 48, 265-269.
  • 47. Marciszewska C., Application of lysozyme on the growth of bacteria characteristic for chilled poultry meat. 2000, Dissertation, Department of Food Quality Management, Agricultural University of Poznań, pp. 1-105 (in Polish).
  • 48. Masschalck B., Deckers D., Michiels C.W., Lytic and nonlytic mechanism of inactivation of Gram-positive bacteria by lysozyme under atmospheric and high hydrostatic pressure. J. Food Prot., 2002, 65, 12, 1916-1923.
  • 49. Masschalck B., Van Houdt R., Van Haver E.G.R., Michiels C.W., Inactivation of Gram-negative bacteria by lysozyme, denatured lysozyme, and lysozyme-derived peptides under high hydrostatic pressure. App. Environ. Microbiol., 2001, 67, 339-344.
  • 50. Muzzarelli R.A.A., Barontini G., Rochetti R., Isolation of lysozyme on chitosan. Biotechnol. Bioeng. 1978, 20, 87-94.
  • 51. Nakimbugwe D., Masschalck B., Atanassova M., Zewdie‑Bosüner A., Michiels C.W., Comparison of bactericidal activity of six lysozymes at atmospheric pressure and under high hydrostatic pressure. Int. J. Food Microb., 2006, 108, 355-363.
  • 52. Odabasi M., Say R., Denizli A., Molecular imprinted particles for lysozyme purification. Material Sci. Eng. C – Biomimetic & Supramolec. Syst., 2007, 27, 90-99.
  • 53. Okanojo M., Shiraki K., Kudou M., Nishikori S., Takagi M., Diamines prevent thermal aggregation and inactivation of lysozyme. J. Biosci. Bioeng., 2005, 100, 556-561.
  • 54. Pellegrini A., Thomas U., Von Fellenberg R., Wild P., Bactericidal activities of lysozyme and aprotinin against Gram-negative and Gram-positive bacteria related to their basic character. J. Appl. Bacteriol., 1992, 72, 180-187.
  • 55. Proctor V.A., Cunnigham F.E., The chemistry of lysozyme and its use as a food preservative and a pharmaceutical. CRC Crit. Rev. Food Sci. Nutr., 1988, 26, 359-395.
  • 56. Ratajczak P., Białas W., Dembczyński R., Grajek W., Jankowski T., An aqueous two-phase extraction of lysozyme from egg white. Żywność, 2004, 40, 3, 40-52 (in Polish; English abstract).
  • 57. Rosiak E., Kołożyn-Krajewska D., Application of prognostic microbiology methods for evaluation of growth of saprophytic bacteria in meat products preservated with lysozyme in monomer form. Żywność, 2003, 36, 3, 5-20 (in Polish; English abstract).
  • 58. Shen L.L., Cao X.J., Synthesis of thermo-sensitive polyacrylamide derivates for affinity precipitation and its application in purification of lysozyme. Biochem. Eng. J., 2007, 33, 66-71.
  • 59. Smith J.L., Mccolgan C., Marmer B.S., Growth temperature and action of lysozyme on Listeria monocytogenes. J. Food Sci., 1991, 54, 1388-1394.
  • 60. Sophianopoulos A.J., Association sites of lysozyme in solution. I. The active side. J. Biol. Chem., 1969, 244, 3188-3193.
  • 61. Świerczewska E., Niemiec J., Noworyta–Głowacka J., A note on the effect of immunostimulation of laying hens on the lysozyme activity in egg white. Animal Sci. Papers Reports, 2003a, 21, 1, 63-68.
  • 62. Świerczewska E., Kopeć W., Noworyta-Głowacka J., Riedel R., Activity of egg albumen proteins in relation to the hen housing systems. Medycyna Wet., 2003b, 59, 157-160 (in Polish; English abstract).
  • 63. Tomizawa H., Yamada H., Imoto, T., The mechanism of irreversible inactivation of lysozyme at pH 4 and 100°C. Biochemistry, 1994a, 33, 130–132.
  • 64. Tomizawa H., Yamada H., Ueda T., Imoto T., Isolation and characterization of 101-succinimide lysozyme that possesses the cyclic imide at Asp 101 – Gly 102. Biochemistry, 1994b, 33, 8770-8774.
  • 65. Weaver G.L., Carta, G., Protein adsorption on cation exchangers: comparison of macroporous and gel-composite media. Biotechnol. Progress, 1996, 12, 342-345.
  • 66. Weaver G.L., Kroge M., Katz F., Deaminated chitin affinity chromatography: a method for isolation, purification and concentration of lysozyme. J. Food Sci., 1977, 42, 1084-1087.
  • 67. Yamada H., Fukumura T., Ito Y., Imoto T., Chitin-coated celite as an affinity adsorbent for high-performance liquid chromatography of lysozyme. Anal. Biochem., 1985, 146, 71-75.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-3c51a543-e36a-41a8-9b8c-ad3dc815a94a
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.