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Purification and biochemical characterization of a novel intestinal protease from Scorpaena notata.
- Source :
-
International Journal of Food Properties . 2017 Supplement, Vol. 20, pS2151-S2165. 15p. 6 Charts, 5 Graphs. - Publication Year :
- 2017
-
Abstract
- A new protease was isolated from the intestine of small red scorpionfish. After ammonium sulfate precipitation, the enzyme was purified to homogeneity by a two-step chromatography with 6.69% recovery and fivefold increase in specific activity. The molecular weight of the protease was about 24 kDa as estimated by size exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme optimum pH and temperature were pH 10.0 and 40°C, respectively. The protease was stable at temperatures below 40°C and over a broad pH range (8.0-11.0). The Km and Kcat values were 0.36 mmol L-1 and 1.61 s-1, respectively. Interestingly, the enzyme presented specificity for casein, egg albumin, bovine serum albumin, and gelatin with obtained degrees of hydrolysis ranging from 3.14% to 6.58%, after 2 h of hydrolysis. Moreover, gluten hydrolysate analysis confirmed protein hydrolysis and solubilization. These results suggested the potential use of the protease in the preparation of food protein hydrolysates with interesting properties. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10942912
- Volume :
- 20
- Database :
- Academic Search Index
- Journal :
- International Journal of Food Properties
- Publication Type :
- Academic Journal
- Accession number :
- 127526558
- Full Text :
- https://doi.org/10.1080/10942912.2017.1368550