journal article·2010-05

Elaboration, characterization and study of a novel affinity membrane made from electrospun hybrid chitosan/nylon-6 nanofibers for papain purification

Haitao Zhang, Chengyao Wu, Yunlong Zhang, Christopher J. Branford White, Yong Xue, Huali Nie, Limin Zhu

Journal of Materials Science· Volume 45· Issue 9
Publisher page

Abstract

Electrospun hybrid chitosan/nylon-6 nanofibrous mats with fiber diameters in the range of 80–310 nm were successfully fabricated using an electrospinning method. Nanofibrous membranes were prepared by nucleophilic reaction of the chitosan’s hydroxyl and amidocyanogen with the triazinyl chloride of Cibacron Blue F3GA (CB) ligand. This system was used to study the purification of papain. Physical and chemical properties of the affinity membrane were characterized by scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (ATR-FTIR), differential scanning calorimetry (DSC), contact angle (CA) and element analysis (EA). The equilibrium adsorption capacity (from Langmuir isotherm data) for papain was 93.46 mg/g affinity membrane. Fifteen layers of the composite affinity membrane were packed into a spin column to separate papain from raw material. Significant amount of the adsorbed papain (about 90.4%) was eluted by 1.0 M NaSCN at pH 9.0, and 4.8-fold purification was achieved in a single step. Experiments on regeneration and dynamic adsorption were also performed. It is shown that this system has the potential to be developed for the industrial purification of the papain.
Source: openaire · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Electrospun Nanofibers in Biomedical Applications · Nanocomposite Films for Food Packaging · Advanced Sensor and Energy Harvesting Materials

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

References (39)

Show source-provided references
1. Huang R, Kostanski LK, Filipe CDM, Ghosh R (2009) J Membr Sci 336:4210.1016/j.memsci.2009.03.002 ↗
2. Svang-Ariyaskui A, Koros WJ, Rousseau RW (2009) Chem Eng Sci 64:198010.1016/j.ces.2008.12.024 ↗
3. Ma ZW, Ramakrishna S (2008) J Membr Sci 319:2310.1016/j.memsci.2008.03.045 ↗
4. Xue H, Ming D, Ma YF, Day DE (2008) J Mater Sci 43:5618. doi: 10.1007/s10853-008-2756-110.1007/s10853-008-2756-1 ↗
5. Yasemin AU, Yavuz E, Yücel S, Kadir P, Attila Y (2009) J Mater Sci 44:3148. doi: 10.1007/s10853-009-3419-610.1007/s10853-009-3419-6 ↗
6. Ma ZW, Kotaki M, Ramakrishna S (2006) J Membr Sci 272:17910.1016/j.memsci.2005.07.038 ↗
7. Redjala T, Sterckeman T, Morel JL (2009) Environ Exp Bot 67:23510.1016/j.envexpbot.2009.05.012 ↗
8. Madaeni SS, Salehi E (2009) J Membr Sci 333:10010.1016/j.memsci.2009.02.006 ↗
9. Lee DS, Kim BM, Seol DW (2009) Biochem Biophys Res Commun 378:64010.1016/j.bbrc.2008.11.096 ↗
10. Cristiana B, Valentina B, Matteo S, Carlo C, Giulio CS (2009) J Chromatogr A 1216:868710.1016/j.chroma.2009.05.045 ↗
11. Ma ZW, Lan ZW, Matsuura T, Ramakrishna S (2009) J Chromatogr B 877:368610.1016/j.jchromb.2009.09.019 ↗
12. Elias K (2000) J Membr Sci 179:110.1016/S0376-7388(00)00514-7 ↗
13. Lu P, Hsieh YL (2009) J Membr Sci 330:28810.1016/j.memsci.2008.12.064 ↗
14. Cristina GD, Jorge C (2008) Chem Eng J 143:33710.1016/j.cej.2008.06.022 ↗
15. Jia GD, Dong SY, Sun Y (2008) Sep Purif Technol 59:27710.1016/j.seppur.2007.06.019 ↗
16. Çetinus ŞA, Öztop HN, Saraydın D (2007) Enzyme Microb Technol 41:44710.1016/j.enzmictec.2007.03.014 ↗
17. Zhang J, Zhang ZP, Song Y, Cai React H (2006) Funct Polym 66:91610.1016/j.reactfunctpolym.2005.12.003 ↗
18. Nie HL, Zhu LM (2007) Int J Biol Macromol 40:26110.1016/j.ijbiomac.2006.08.005 ↗
19. Hao WQ, Wang JD, Zhang XM (2006) J Chromatogr A 1114:12310.1016/j.chroma.2006.02.047 ↗
20. Sang YM, Gu QB, Sun TC, Li FS, Liang CZ (2008) J Hazard Mater 153:86010.1016/j.jhazmat.2007.09.035 ↗
21. Sang YM, Li FS, Gu QB, Liang CZ, Chen JQ (2008) Desalination 223:34910.1016/j.desal.2007.01.208 ↗
22. Yun KM, Hogan CJH Jr, Matsubayashi Y, Kawabe M, Iskandar F, Okuyama K (2007) Chem Eng Sci 62:475110.1016/j.ces.2007.06.007 ↗
23. Nova CJM, Paolucci-Jeanjean D, Ballaville MP, Barboiu M, Rivallin M, Rios G (2008) J Membr Sci 321:8110.1016/j.memsci.2007.12.002 ↗
24. Kumbar SG, Nukavarapu SP, James R, Nair LS, Laurencin CT (2008) Biomaterials 29:410010.1016/j.biomaterials.2008.06.028 ↗
25. Park SH, Kim TG, Kim HC, Yang DY, Park TG (2008) Acta Biomater 4:119810.1016/j.actbio.2008.03.019 ↗
26. Zhang YZ, Venugopal JR, El-Turki A, Ramakrishna S, Su B, Lim CT (2008) Biomaterials 29:431410.1016/j.biomaterials.2008.07.038 ↗
27. Chang CP, Yuan CL (2009) J Mater Sci 44:5485. doi: 10.1007/s10853-009-3766-310.1007/s10853-009-3766-3 ↗
28. Hota G, Kumar BR, Ng WJ, Ramakrishna S (2009) J Mater Sci 43:212. doi: 10.1007/s10853-007-2142-410.1007/s10853-007-2142-4 ↗
29. Zhang HT, Nie HL, Li SB, White CJB, Zhu LM (2009) Mater Lett 63:119910.1016/j.matlet.2009.02.035 ↗
30. Cai YB, Li Q, Wu YB, Song L, Hu Y (2008) J Mater Sci 43:6132. doi: 10.1007/s10853-008-2921-610.1007/s10853-008-2921-6 ↗
31. Aussawasathien D, Teerawattananon C, Vongachariya A (2008) J Membr Sci 315:1110.1016/j.memsci.2008.01.049 ↗
32. Kim C, Park SH, Lee WJ, Yang KS (2004) Electrochim Acta 50:87710.1016/j.electacta.2004.02.071 ↗
33. Zhang HT, Li SB, White CJB, Ning X, Nie HL, Zhu LM (2009) Electrochim Acta 54:573910.1016/j.electacta.2009.05.021 ↗
34. Ruckenstein E, Zeng XF (1998) J Membr Sci 142:1310.1016/S0376-7388(98)00025-8 ↗
35. Clontech Laboratories (2005) HAT protein expression and purification system—user manual cat. no. 631205, PT 3250-1 (PR 53603)
36. Bradford MM (1976) Anal Biochem 72:24810.1016/0003-2697(76)90527-3 ↗
37. Yoon K, Kim K, Wang XF, Fang DF, Hsiao BS, Chu B (2006) Polymer 47:243410.1016/j.polymer.2006.01.042 ↗
38. Li XR, Zhang H, Li H, Tang GW, Zhao YH, Yuan XY (2008) Polym Degrad Stab 93:61810.1016/j.polymdegradstab.2008.01.003 ↗
39. Ma ZW, Kotaki M, Ramakrishna S (2005) J Membr Sci 265:11510.1016/j.memsci.2005.04.044 ↗