Immobilizacja naringinazy z Penicillium decumbens na magnetycznych nośnikach polisacharydowych

• Autorzy: Joanna Bodakowska-Boczniewicz , Zbigniew Garncarek

Warianty tytułu

Immobilization of naringinase from Penicillium decumbens on polysaccharide-coated magnetic particles

• Języki publikacji: PL

Abstrakty

Naringinaza z Penicillium decumbens została unieruchomiona na aktywowanych nośnikach polisacharydowych o właściwościach magnetycznych. W badaniach wykorzystano gumę guar, karobową, tragakantową, ksantanową oraz karagenianin. Nośniki otrzymano poprzez pokrycie mikrocząsteczek magnetytu (Fe3O4) polisacharydem, a następnie aktywując je aldehydem glutarowym lub polietylenoiminą. Celem niniejszej pracy była immobilizacja naringinazy z P. decumbens na magnetycznych nośnikach polisacharydowych oraz charakterystyka otrzymanego biokatalizatora. Najwyższą aktywność enzymu uzyskano poprzez immobilizację naringinazy na nośniku otrzymanym na bazie gumy karobowej aktywowanej polietylenoiminą. Immobilizacja naringinazy na tak otrzymanym nośniku wpływała na zmniejszenie optymalnej wartości pH oraz optymalnej temperatury aktywności badanego enzymu. Immobilizacja powodowała zwiększenie wartości stałej Michaelisa oraz zmniejszenie maksymalnej szybkości reakcji w porównaniu z enzymem wolnym.(abstrakt oryginalny)

EN

Naringinase from Penicillium decumbens was immobilized on activated polysaccharide supported with magnetic properties. Magnetic microparticles were prepared by coating a magnetite (Fe3O4) with a polysaccharide followed by activating with glutaraldehyde or polyethyleneimine. Guar gums, locust bean, tragacanth, xanthan and carrageenan were used in the research. The main goals of this work were the immobilization of naringinase on magnetic polysaccharide carriers and the characterization of such immobilized enzyme. The naringinase immobilized on a carrier obtained on the basis of carob gum activated with polyethyleneimine had the highest activity. The immobilization of the naringinase on the carrier thus obtained influenced the reduction of the optimal pH value and the optimal temperature. Immobilization increased the Michaelis constant value and decreased the maximum reaction rate, as compared to the free enzyme.(original abstract)

Słowa kluczowe

PL

Badanie produktów spożywczych; Żywność; Badanie żywności

EN

Food products study; Food; Food research

• Czasopismo: Prace Naukowe Uniwersytetu Ekonomicznego we Wrocławiu
• Rocznik: 2018
• Numer: nr 542 Wybrane zagadnienia z bioekonomii
• Strony: 9--24

Twórcy

autor

Joanna Bodakowska-Boczniewicz

• Uniwersytet Ekonomiczny we Wrocławiu

autor

Zbigniew Garncarek

• Uniwersytet Ekonomiczny we Wrocławiu

Bibliografia

• Alvarenga A.E., Romero C.M., Castro G.R., 2013, A novel α-l-rhamnosidase with potential applications in citrus juice industry and in winemaking, European Food Research and Technology, vol. 237, no. 6, s. 977-985.
• Awad G E.A., Abd El Aty A.A., Shehata A.N., Hassan M.E., Elnashar M.M., 2016, Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin, 3 Biotech, vol. 6, no. 1, s. 6-14.
• Bakuła Z., Stachowiak R., Wiśniewski J., 2013, Immobilizacja komórek - znaczenie biomedyczne, Postępy Mikrobiologii, vol. 52, nr 3, s. 233-245.
• Bolibok P., Gembala J., Wujak M., Roszek K., Terzyk A., Wiśniewski M., 2016, Immobilizacja enzymów na nośnikach sposobem na ukierunkowaną modyfikację właściwości biokatalizatorów, Przemysł Chemiczny, vol. 95, nr 11, s. 2254-2258.
• Busto M.D., Meza V., Ortega N., Perez-Mateos M., 2007, Immobilization of naringinase from Aspergillus niger CECT 2088 in poly(vinyl alcohol) cryogels for the debittering of juices, Food Chemistry, vol. 104, no. 3, s. 1177-1182.
• Cao M., Li Z., Wang J., Ge W., Yue T., Li R., William W.Y., 2012, Food related applications of magnetic iron oxide nanoparticles: enzyme immobilization, protein purification, and food analysis, Trends in Food Science & Technology, vol. 27, no. 1, s. 47-56.
• Cavia-Saiz M., Muñiz P., Ortega N., Busto M.D., 2011, Effect of enzymatic debittering on antioxidant capacity and protective role against oxidative stress of grapefruit juice in comparison with adsorption on exchange resin, Food Chemistry, vol. 125, no. 1, s. 158-163.
• Davis W.B., 1947, Determination of flavanones in citrus fruits, Analytical Chemistry, vol. 19, no. 7, s. 476-478.
• Del Nobile M.A., Piergiovanni L., Buonocore G.G., Fava P., Puglisi M.L., Nicolais L., 2003, Naringinase immobilization in polymeric films intended for food packaging applications, Journal of Food Science, vol. 68, no. 6, s. 2046-2049.
• Dembczyński R., Jankowski T., 2004, Unieruchamianie komórek drobnoustrojów metodą kapsułkowania - stan obecny i możliwośći rozwoju, Nauka. Technologia. Jakość, vol. 4, nr 41, s. 5-17.
• Elujoba A.A., Hardman R., 1987, Diosgenin production by acid and enzymatic hydrolysis of fenugreek, Fitoterapia, no. 58, s. 299-304.
• Gallego M.V., Pinaga F., Ramon D., Valles S., 2001, Purification and characterization of an alpha-L-rhamnosidase from Aspergillus terreus of interest in winemaking, Journal of Food Science, vol. 66, no. 2, s. 204-209.
• González-Pombo P., Fariña L., Carrau F., Batista-Viera F., Brena B.M., 2014, Aroma enhancement in wines using co-immobilized Aspergillus niger glycosidases, Food Chemistry, vol. 143, s. 185-191.
• Jiang D.S., Long S.Y., Huang J., Xiao H.Y., Zhou J.Y., 2005, Immobilization of Pycnoporus sanguineus laccase on magnetic chitosan microspheres, Biochemical Engineering Journal, vol. 25, no. 1, s. 15-23.
• Krajewska B., 2004, Application of chitin- and chitosan-based materials for enzyme immobilizations: a review, Enzyme and Microbial Technology, vol. 35, no. 2-3, s. 126-139.
• Lei S., Xu Y., Fan G., Xiao M., Pan S., 2011, Immobilization of naringinase on mesoporous molecular sieve MCM-41 and its application to debittering of white grapefruit, Applied Surface Science, vol. 257, no. 9, s. 4096-4099.
• Leonowicz A., Sarkar J.M., Bollag J., 1988, Improvement instability of an immobilized fungal laccase, Applied Microbiology and Biotechnology, vol. 29, no. 7, s. 129-135.
• Lowry O.H., Rosebrough N.J., Farr L., Randall R.J., 1951, Protein measurment with the Folin phenol reagent, The Journal of Biological Chemistry, no. 193, s. 265-275.
• Manjón A., Bastida J., Romero C., Jimeno A., Iborra J.L., 1985, Immobilization of naringinase on glycophase-coater porous glass, Biotechnology Letters, vol. 7, no. 7, s. 477-482.
• Mishra P., Kar R., 2003, Treatment of grapefruit juice for bitterness removal by Amberlite IR 120 and Amberlite IR 400 and alginate entrapped naringinase enzyme, Journal of Food Science, vol. 68, no. 4, s. 1229-1233.
• Nunes M.P., Vila-Real H., Fernandes P.C.B., Ribeiro M.H.L., 2010, Immobilization of naringinase in PVA-alginate matrix using an innovative technique, Applied Biochemistry and Biotechnology, vol. 160, no. 7, s. 2129-2147.
• Olsen R.W., Alfred L., 1974, Debittering of concentrated grapefruit juice with naringinase, Florida Agricultural Experiment Stations Journal Series, vol. 77, s. 321-325.
• Pedro H., Alfaia A.J., Marques J., Vila-Real H.J., Calado A., Ribeiro M.H.L., 2007, Design of an immobilized enzyme system for naringin hydrolysis at high-pressure, Enzyme and Microbial Technology, vol. 40, no. 3, s. 442-446.
• Puri M., 2012, Updates on naringinase: Structural and biotechnological aspects, Applied Microbiology and Biotechnology, vol. 93, no. 1, s. 49-60.
• Puri M., Kaur H., Kennedy J.F., 2005, Covalent immobilization of naringinase for the transformation of a flavonoid, Journal of Chemical Technology and Biotechnology, vol. 80, no. 10, s. 1160-1165.
• Puri M., Marwaha S., Kothari R., 1996, Studies on the applicability of alginate-entrapped naringinase for the debittering of kinnow juice, Enzyme and Microbial Technology, vol. 18, no. 4, s. 281-285.
• Rajdeo K., Harini T., Lavanya K., Fadnavis N.W., 2016, Immobilization of pectinase on reusable polymer support for clarification of apple juice, Food and Bioproducts Processing, no. 99, s. 12-19.
• Ribeiro I.A.C, Ribeiro M.H.L., 2008a, Kinetic modelling of naringin hydrolysis using a bitter sweet alfa-rhamnopyranosidase immobilized in k-carrageenan, Journal of Molecular Catalysis B: Enzymatic, vol. 51, no. 1-2, s. 10-18.
• Ribeiro I.A.C, Ribeiro M.H.L., 2008b, Naringin and naringenin determination and control in grapefruit juice by a validated HPLC method, Food Control, vol. 19, no. 4, s. 432-438.
• Romero C., Jimeno A., 1985, Immobilization of naringinase on glycophase-coater porous glass, Biotechnology Letters, vol. 7, no. 7, s. 477-482.
• Sankyo C., 1988, Preparation of antibiotic chloropolysporin-C, Canadian Patent.
• Şekeroğlu G., Fadiloglu S., Fahrettin G., 2006, Immobilization and characterization of naringinase for the hydrolysis of naringin, European Food Research and Technology, vol. 224, no. 1, s. 55-60.
• Shanmugaprakash M., Vinothkumar V., Ragupathy J., Reddy D.A., 2015, Biochemical characterization of three phase partitioned naringinase from Aspergillus brasiliensis MTCC 1344, International Journal of Biological Macromolecules, no. 80, s. 418-423.
• Soares N.F.F., Hotchkiss J.H., 1998, Bitterness reduction in grapefruit juice through active packaging, Packaging Technology and Science, no. 18, s. 9-18.
• Soria F., Ellenrieder G., Oliveira G.B., Cabrera M., Carvalho L.B., 2012, α-L-Rhamnosidase of Aspergillus terreus immobilized on ferromagnetic supports, Applied Microbiology and Biotechnology, vol. 93, no. 3, s. 1127-1134.
• Synowiecki J., Wołosowska S., 2007, Otrzymywanie i niektóre zastosowania unieruchomionych enzymów, Biotechnologia, vol. 2, nr 77, s. 7-26.
• Tsen H.Y., Tsai S.Y., 1998, Comparison of the kinetics and factors affecting the stabilities of chitin-immobilized naringinases from two fungal sources, Journal of Fermentation Technology, vol. 66, no. 2, s. 193-198.
• Vila-Real H., Alfaia A.J., Rosa M.E., Calado A.R., Ribeiro M.H.L, 2010, An innovative sol-gel naringinase bioencapsulation process for glycosides hydrolysis, Process Biochemistry, vol. 45, no. 6, s. 841-850.
• Wang F., Guo C., Liu H., Liu C., 2008, Immobilization of Pycnoporus sanguineus laccase by metal affinity adsorption on magnetic chelator particles, Chemical Technology and Biotechnology, vol. 83, no. 1, s. 97-104.
• Xiao A., You H., Wu C., Cai H., 2015, Immobilization and characterization of naringinase from Aspergillus aculeatus onto magnetic Fe3O4 nanoparticles, Nanoscience and Nanotechnology Letters, vol. 7, no. 9, s. 770-778.
• Zhu Y., Jia H., Xi M., Yang L., Li X., 2017, Characterization of a naringinase from Aspergillus oryzae 11250 and its application in the debitterization of orange juice, Process Biochemistry, no. 62, s. 114-121.

Identyfikatory

DOI

10.15611/pn.2018.542.01