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| Hsiao,Nai-Wan; Chen,Yeh; Kuan,Yi-Chia; Lee,Yen-Chung; Lee,Shuo-Kang; Chan,Hsin-Hua; Kao,Chao-Hung. |
| Background Aspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, especially in the food processing industry. Here we describe a novel aspartic protease that was purified from Peptidase R, a commercial protease preparation derived from Rhizopus oryzae. Results An aspartic protease sourced from Peptidase R was purified to homogeneity by anion exchange chromatography followed by polishing with a hydrophobic interaction chromatography column, resulting in a 3.4-fold increase in specific activity (57.5 × 10³ U/mg) and 58.8% recovery. The estimated molecular weight of the purified enzyme was 39 kDa. The N-terminal sequence of the purified protein exhibited 63-75% identity to rhizopuspepsins from various Rhizopus... |
| Tipo: Journal article |
Palavras-chave: Chromatography; Endopeptidase; Food processing industry; Homogeneity; Rhizopuspepsin. |
| Ano: 2014 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200006 |
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