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A novel thermostable chitinase (PJC) from pomegranate (Punica granatum) juice |
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| Authors: | Narasimha Kumar Kopparapu Zhuqing Liu Qiaojuan Yan Zhengqiang Jiang Shuping Zhang |
| Affiliation: | 1. Department of Biotechnology, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China;2. College of Water Conservancy and Civil Engineering, China Agricultural University, Beijing 100083, China;3. Bioresource Utilization Laboratory, College of Engineering, China Agricultural University, Beijing 100083, China |
| Abstract: | A novel chitinase was isolated and purified to its homogeneity from pomegranate juice by a combination of ammonium sulphate precipitation and ion-exchange chromatography. The pomegranate juice chitinase (PJC) was purified to specific activity of 14.5 U/mg and a recovery of 34%. The monomeric protein migrated on SDS–PAGE at 29 kDa. The enzyme was found to be glycosylated (7.2%). It exhibited optimal activity at pH 4.5 and 70 °C. The enzyme was stable in the pH range 3.0–9.0 and up to 65 °C. The internal peptide sequence results suggest that the purified PJC shared high homology with class III chitinases of other known plant chitinases. The purified enzyme could hydrolyse colloidal chitin to its oligomers. It did not exhibit any antifungal activity. |
| Keywords: | BSA bovine serum albumin CHES N-cyclohexyl-2-aminoethane sulphonic acid DTT dithiothreitol EDTA ethylenediaminetetracetic acid MES 2-(N-morpholino) ethane sulphonic acid MOPS 3-(N-morpholino) propane sulphonic acid PJC a 29 kDa chitinase from pomegranate juice PPL2 Parkia platycephala lectin 2 SDS&ndash PAGE sodium dodecyl sulphate polyacrylamide gel electrophoresis TLC thin-layer chromatography |
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