Preparation and characterization of gellan gum microspheres containing a cold-adapted β-galactosidase from Rahnella sp. R3

Carbohydrate Polymers

Volumn 162, Issue , 2017, Pages 10-15

  Fan, Yuting ^a,c   Yi, Jiang ^b   Hua, Xiao ^a   Zhang, Yuzhu ^c   Yang, Ruijin ^a  

^a JIANGNAN UNIVERSITY   (China)

^b SHENZHEN UNIVERSITY   (China)

^c WESTERN REGIONAL RESEARCH CENTER   (United States)

Author keywords

Cold adapted R Gal; Encapsulation; Gellan gum; Hydrogel beads

Indexed keywords

CALCIUM; ENCAPSULATION; ENZYMES; GELS; PH EFFECTS; SOLUTIONS; SUGARS;

COLD-ADAPTED ENZYMES; DIFFERENT EFFECTS; ENCAPSULATION EFFICIENCY; ENZYME CHARACTERISTICS; GELLAN GUM; HYDROGEL BEADS; MODERATE TEMPERATURE; STABILIZING INTERACTIONS;

HYDROGELS;

BACTERIAL POLYSACCHARIDE; BETA GALACTOSIDASE; GELLAN; MICROSPHERE;

CHEMISTRY; COLD; ENZYMOLOGY; METABOLISM; RAHNELLA;

BETA-GALACTOSIDASE; COLD TEMPERATURE; MICROSPHERES; POLYSACCHARIDES, BACTERIAL; RAHNELLA;

EID: 85009180976     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2017.01.033     Document Type: Article

References (34)

1. Agnihotri, S.A., Jawalkar, S.S., Aminabhavi, T.M., Controlled release of cephalexin through gellan gum beads: Effect of formulation parameters on entrapment efficiency, size, and drug release. European Journal of Pharmaceutics and Biopharmaceutics 63 (2006), 249–261.
2. Asraf, S.S., Gunasekaran, P., Current trends of ß-galactosidase research and application. Current Research. Technology and Education Topics in Applied Microbiology and Microbial Biotechnology, 2010, 880–890.
3. Bayarri, S., Costell, E., Duran, L., Influence of low sucrose concentrations on the compression resistance of gellan gum gels. Food Hydrocolloids 16 (2002), 593–597.
4. Bayramoglu, G., Tunali, Y., Arica, M.Y., Immobilization of β-galactosidase onto magnetic poly (GMA–MMA) beads for hydrolysis of lactose in bed reactor. Catalysis Communications 8 (2007), 1094–1101.
5. Bhatia, R.B., Brinker, C.J., Gupta, A.K., Singh, A.K., Aqueous sol-gel process for protein encapsulation. Chemistry of Materials 12 (2000), 2434–2441.
6. Blandino, A., Macṍas, M., Cantero, D., Glucose oxidase release from calcium alginate gel capsules. Enzyme and Microbial Technology 27 (2000), 319–324.
7. Bryant, C.M., McClements, D.J., Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends in Food Science & Technology 9 (1998), 143–151.
8. Bultema, J.B., Kuipers, B.J., Dijkhuizen, L., Biochemical characterization of mutants in the active site residues of the β-galactosidase enzyme of Bacillus circulans ATCC 31382. FEBS Open Bio 4 (2014), 1015–1020.
9. Chakraborty, S., Jana, S., Gandhi, A., Sen, K.K., Zhiang, W., Kokare, C., Gellan gum microspheres containing a novel α-amylase from marine Nocardiopsis sp. strain B2 for immobilization. International Journal of Biological Macromolecules 70 (2014), 292–299.
10. Clark, A., Kavanagh, G., Ross-Murphy, S., Globular protein gelation—theory and experiment. Food Hydrocolloids 15 (2001), 383–400.
11. De Maio, A., El-Masry, M., Portaccio, M., Diano, N., Di Martino, S., Mattei, A., et al. Influence of the spacer length on the activity of enzymes immobilised on nylon/polyGMA membranes: Part 1. Isothermal conditions. Journal of Molecular Catalysis B: Enzymatic 21 (2003), 239–252.
12. Escobar, S., Bernal, C., Mesa, M., Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant. Biochemical Engineering Journal 75 (2013), 32–38.
13. Fan, Y., Hua, X., Zhang, Y., Feng, Y., Shen, Q., Dong, J., et al. Cloning: Expression and structural stability of a cold-adapted beta-galactosidase from Rahnella sp. R3. Protein Expression Purification 115 (2015), 158–164.
14. Fan, Y., Yi, J., Hua, X., Feng, Y., Yang, R., Zhang, Y., Structure analysis of a glycosides hydrolase family 42 cold-adapted β-galactosidase from Rahnella sp. R3. RSC Advances 6 (2016), 37362–37369.
15. Fischer, J., Guidini, C.Z., Santana, L.N.S., de Resende, M.M., Cardoso, V.L., Ribeiro, E.J., Optimization and modeling of lactose hydrolysis in a packed bed system using immobilized β-galactosidase from Aspergillus oryzae. Journal of Molecular Catalysis B: Enzymatic 85 (2013), 178–186.
16. Grosová, Z., Rosenberg, M., Rebroš, M., Šipocz, M., Sedláčková, B., Entrapment of á-galactosidase in polyvinylalcohol hydrogel. Biotechnology Letters 30 (2008), 763–767.
17. Harju, M., Kallioinen, H., Tossavainen, O., Lactose hydrolysis and other conversions in dairy products: Technological aspects. International Dairy Journal 22:2 (2012), 104–109.
18. Jansson, P.E., Lindberg, B., Sandford, P.A., Structural studies of gellan gum: An extracellular polysaccharide elaborated by Pseudomonas elodea. Carbohydrate Research 124 (1983), 135–139.
19. Karasová-Lipovová, P., Strnad, H., Spiwok, V., Malá Š, Králová, B., Russell, N.J., The cloning, purification and characterisation of a cold-active á-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2. Enzyme and Microbial Technology 33 (2003), 836–844.
20. Klein, M.P., Fallavena, L.P., Schöffer, J., da, N., Ayub, M.A., Rodrigues, R.C., et al. High stability of immobilized β-d-galactosidase for lactose hydrolysis and galactooligosaccharides synthesis. Carbohydrate Polymers 95 (2013), 465–470.
21. Klein, M.P., Hackenhaar, C.R., Lorenzoni, A.S., Rodrigues, R.C., Costa, T.M., Ninow, J.L., et al. Chitosan crosslinked with genipin as support matrix for application in food process: Support characterization and β-d-galactosidase immobilization. Carbohydrate Polymers 137 (2016), 184–190.
22. Li, L., Li, G., Cao, L., Ren, G., Kong, W., Wang, S., et al. Characterization of the cross-linked enzyme aggregates of a novel β-galactosidase, a potential catalyst for the synthesis of galacto-oligosaccharides. Journal of Agricultural and Food Chemistry 63 (2015), 894–901.
23. Makowski, K., Białkowska, A., Szczęsna-Antczak, M., Kalinowska, H., Kur, J., Cieśliński, H., et al. Immobilized preparation of cold-adapted and halotolerant Antarctic β-galactosidase as a highly stable catalyst in lactose hydrolysis. FEMS Microbiology Ecology 59 (2007), 535–542.
24. Manjon, A., Llorca, F., Bonete, M., Bastida, J., Iborra, J., Properties of β-galactosidase covalently immobilized to glycophase-coated porous glass. Process Biochemistry 20 (1985), 17–22.
25. Matalanis, A., Jones, O.G., McClements, D.J., Structured biopolymer-based delivery systems for encapsulation, protection: and release of lipophilic compounds. Food Hydrocolloids 25 (2011), 1865–1880.
26. Posadowska, U., Brzychczy-Wloch, M., Pamula, E., Injectable gellan gum-based nanoparticles-loaded system for the local delivery of vancomycin in osteomyelitis treatment. Journal of Materials Science: Materials in Medicine 27 (2016), 1–9.
27. Selvakumaran, S., Muhamad, I.I., Razak, S.I.A., Evaluation of kappa carrageenan as potential carrier for floating drug delivery system: effect of pore forming agents. Carbohydrate Polymers 135 (2016), 207–214.
28. Shen, Q., Yang, R., Hua, X., Ye, F., Zhang, W., Zhao, W., Gelatin-templated biomimetic calcification for β-galactosidase immobilization. Process Biochemistry 46 (2011), 1565–1571.
29. Sworn, G., Sanderson, G., Gibson, W., Gellan gum fluid gels. Food Hydrocolloids 9 (1995), 265–271.
30. Wang, X., Gai, Z., Yu, B., Feng, J., Xu, C., Yuan, Y., et al. Degradation of carbazole by microbial cells immobilized in magnetic gellan gum gel beads. Applied and Environmental Microbiology 73 (2007), 6421–6428.
31. Wang, M., Qi, W., Jia, C., Ren, Y., Su, R., He, Z., Enhancement of activity of cross-linked enzyme aggregates by a sugar-assisted precipitation strategy: Technical development and molecular mechanism. Journal of Biotechnology 156 (2011), 30–38.
32. Wu, Y., Yuan, S., Chen, S., Wu, D., Chen, J., Wu, J., Enhancing the production of galacto-oligosaccharides by mutagenesis of Sulfolobus solfataricus β-galactosidase. Food Chemistry 138 (2013), 1588–1595.
33. Yang, F., Xia, S., Tan, C., Zhang, X., Preparation and evaluation of chitosan-calcium-gellan gum beads for controlled release of protein. European Food Research and Technology 237 (2013), 467–479.
34. Zhang, Z., Zhang, R., Zou, L., McClements, D.J., Protein encapsulation in alginate hydrogel beads: effect of pH on microgel stability: Protein retention and protein release. Food Hydrocolloids 58 (2016), 308–315.