Trypsin purification using magnetic particles of azocasein-iron composite.

Maria Helena Menezes Estevam Alves, Gabriela Ayres Nascimento, Mariana Paola Cabrera, Sara Isabel da Cruz Silvério, Clarisse Nobre, José António Teixeira, Luiz Bezerra de Carvalho

Food chemistry 2017 Jul 01

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This work presents an inexpensive, simple and fast procedure to purify trypsin based on affinity binding with ferromagnetic particles of azocasein composite (mAzo). Crude extract was obtained from intestines of fish Nile tilapia (Oreochromis niloticus) homogenized in buffer (01g tissue/ml). This extract was exposed to 100mg of mAzo and washed to remove unbound proteins by magnetic field. Trypsin was leached off under high ionic strength (3M NaCl). Preparation was achieved containing specific activity about 60 times higher than that of the crude extract. SDS-PAGE showed that the purified protein had molecular weight (24kDa) in concordance with the literature for the Nile tilapia trypsin. The mAzo composite can be reused and applied to purify trypsin from other sources. Copyright © 2016. Published by Elsevier Ltd.

Citation

Maria Helena Menezes Estevam Alves, Gabriela Ayres Nascimento, Mariana Paola Cabrera, Sara Isabel da Cruz Silvério, Clarisse Nobre, José António Teixeira, Luiz Bezerra de Carvalho. Trypsin purification using magnetic particles of azocasein-iron composite. Food chemistry. 2017 Jul 01;226:75-78