Lysyl oxidase from jumbo squid (Dosidicus gigas) muscle: purification and partial characterization |
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| Authors: | Wilfrido Torres‐Arreola Josafat Marina Ezquerra‐Brauer Ramón Pacheco‐Aguilar Elisa M Valenzuela‐Soto Ofelia Rouzaud‐Sandez Maria E Lugo‐Sanchez Gisela Carvallo‐Ruiz |
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| Affiliation: | 1. Centro de Investigación en Alimentación y Desarrollo, A.C. Carretera a la Victoria Km 0.6. Apdo. Postal 1735, C.P. 83000, Hermosillo, Sonora;2. Departamento de Investigación y Posgrado en Alimentos, Universidad de Sonora, Blvd. Luis Encinas y Rosales s/n. Apdo. Postal 1658, C.P. 83000 Col. Centro, Hermosillo, Sonora;3. Departamento de Investigación y Posgrado en Alimentos, Universidad de Sonora, Blvd. Luis Encinas y Rosales s/n. Apdo. Postal 1658, C.P. 83000 Col. Centro, Hermosillo, Sonora |
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| Abstract: | Lysyl oxidase (LOX; E.C.1.4.3.13) was purified from jumbo squid muscle (Dosidicus gigas) with 1900‐fold and yield 1.9%, and characterized for the first time. The purification procedure consisted of fractionation with urea and a combination of size‐exclusion and anion‐exchange chromatography. The enzyme had a molecular weight of 32 kDa, as estimated by SDS‐PAGE. Using a specific LOX substrate (1,5‐diaminopentane), its optimum activity was determined at pH 8.2 and 65 °C. Activation energy (Ea) of the enzyme was 69.94 kJ K?1 mol?1. The enzyme was strongly inhibited by β‐aminopropionitrile fumarate (BAPN), a specific LOX inhibitor. Moreover, purified LOX was able to work at different temperatures (20–90 °C) at pH 8.2. Although further research is needed, the results from this work suggest that based on LOX activity, this enzyme may be of practical use in preventing textural changes in jumbo squid during storage or processing. |
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| Keywords: | Characterization collagen jumbo squid lysyl oxidase purification |
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