CrossRef 19. Zhou ZM,

Xu J, Liu XQ, Li XM, Li SY, Yang K, Wang XF, Liu M, Zhang QQ: Non-spherical racemic polylactide microarchitectures this website formation via solvent evaporation method. Polymer 2009, 50:3841–3850.CrossRef 20. Speer DP, Chvapil M, Eskelson CD, Ulreich J: Biological effects of residual glutaraldehyde in glutaraldehyde-tanned collagen biomaterials. J Biomed Mater Res 1980, 14:753–764.CrossRef 21. Tamura T, Kita T, Nakagawa T, Endo T, Kim TS, Ishihara T, Mizushima Y, Higaki M, Ito J: Drug delivery to the cochlea using PLGA nanoparticles. BIBW2992 supplier Laryngoscope 2005, 115:2000–2005.CrossRef 22. Zhang Y, Zhang WK, Löbler M, Schmitz KP, Saulnier P, Perrier T, Pyykkö I, Zou J: Inner ear biocompatibility of lipid nanocapsules after round window membrane application. Int J Pharm 2011, 404:211–219.CrossRef 23. Zou J, Saulnier P, Perrier T, Zhang Y, Manninen T, Toppila E, Pyykkö I: Distribution of lipid nanocapsules in different cochlear cell populations after round window membrane permeation. J Biomed Mater Res Part B Appl Biomater 2008, 87B:10–18.CrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions

ZY, ZZ, GH, QX, and MY performed the experiments and analyzed the results. ZY and MY conceived and designed the experiments, analyzed the results, and participated in writing the manuscript. All authors read and approved the final manuscript.”
“Background l-Asparaginase II (ASNase II) is an enzyme that is widely used for the treatment of hematopoietic diseases such as BMS202 concentration acute lymphoblastic leukemia. The enzyme is able to destroy asparagine-dependent tumors by degrading circulating l-asparagine and destroying malignant cells [1, 2]. However, native ASNase II is associated with a high incidence of allergic reactions. Due to the formation of neutralizing antibodies, the half-life of circulating ASNase II (18 to 24 h) can be shortened to approximately Resminostat 2.5 h [3]. Moreover, it is susceptible to proteolytic degradation by the proteases of the host organism. Much effort has been devoted to develop methods to avoid such side effects as well as to increase its in vivo half-life.

For example, ASNase II has been chemically modified by polyethyleneglycol [4], poly-(d,l-alanine) [5], and dextran [6]. In the recent years, nanotechnology has shown a significant promise in the preparation of immobilized enzymes. Immobilization of enzymes onto biopolymer nanoparticles may result in some benefits, such as improving their stability to pH and temperature, as well as resistance to proteases and other denaturing compounds. Candidate carrier biopolymers should exhibit chemical and physical stability, biological compatibility, high purity, homogeneous molecular weight (MW) distribution, and adequate functional groups for binding to biomolecules with high loading capacity. They exhibit several drug loading mechanisms including electrostatic attractions, hydrophobic interactions, and covalent binding.