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Lysyl oxidase from jumbo squid ( Dosidicus gigas ) muscle: purification and partial characterization
Author(s) -
TorresArreola Wilfrido,
EzquerraBrauer Josafat Marina,
PachecoAguilar Ramón,
ValenzuelaSoto Elisa M.,
RouzaudSandez Ofelia,
LugoSanchez Maria E.,
CarvalloRuiz Gisela
Publication year - 2012
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2011.02926.x
Subject(s) - enzyme , lysyl oxidase , fractionation , squid , chemistry , substrate (aquarium) , biochemistry , size exclusion chromatography , urea , chromatography , ion chromatography , yield (engineering) , biology , fishery , materials science , ecology , metallurgy
Summary 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 ( E a ) 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.