DIGESTIBILITY AND ENZYMATIC ACTIVITY IN VITRO OF HEN EGG WHITE LYSOZYME
Objective: The aim of this study was to evaluate the protein digestibility and analyze the residual enzymatic activity of lysozyme.
Methods: Protein digestibility was evaluated hydrolyzing the protein with pepsin at pH 1.2, 2.0, and 3.2 during 60, 90, and 120 minutes of incubation.
These hydrolysates were analyzed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reversed-phase high-performance liquid
chromatography. Residual enzymatic activity was evaluated with the spectrophotometric method at 450 nm.
Results: Lysozyme was totally hydrolyzed with pepsin at pH 1.2. At pH 2.0, lysozyme was partially hydrolyzed and at pH 3.2 hydrolysis was absent at
all times of the assay.
Conclusions: Lysozyme was hydrolyzed with pepsin at low pH. Residual enzymatic method can be used to determine the grade of hydrolysis in
Keywords: Lysozyme, Enzymatic hydrolysis, Muramidase activity, Antimicrobial activity.
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