CHARACTERIZATION OF PROTEINASE RECOVERED FROM PACIFIC WHITING SURIMI WASH WATER |
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Authors: | S BENJAKUL T A SEYMOUR M T MORRISSEY H AN |
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Affiliation: | Oregon State University Seafood Laboratory 2001 Marine Drive, RM 253 Astoria, OR 97103-3427 |
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Abstract: | Pacific whiting surimi wash water (SWW) proteinase was recovered by ohmic heating, ultrafiltration, and freeze-drying. By these processes, 5.9-fold purification was achieved. The most efficient step was ohmic heating, which concentrated the proteinase by 4.8 fold. Specific activity of the recovered SWW proteinase on casein and Z-Phe-Arg-NMec was 28.2 and 0.17 U/mg protein, respectively. The SWW proteinase showed good hydrolytic activity towards casein, acid-denatured hemoglobin and myofibrils. Acidification increased specific activity on all substrates tested but reduced thermal stability. β-Mercaptoethanol, dithiothreitol and urea enhanced activity against Z-Phe-Arg-NMec. Proteinase activity on Z-Phe-Arg-NMec showed an optimum pH of 4.0. The recovered proteinase showed 18.5% residual activity after 7 week storage at 4C. |
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