Degradation Kinetics of Myosin Heavy Chain of Pacific Whiting Surimi

Authors

  • JIRAWAT YONGSAWATDIGUL,

    1. The authors are with Oregon State Univ., Seafood Laboratory, 250 36th St., Astoria, OR 97103-2499. Address inquiries to Dr. Jae W. Park.
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  • JAE W. PARK,

    1. The authors are with Oregon State Univ., Seafood Laboratory, 250 36th St., Astoria, OR 97103-2499. Address inquiries to Dr. Jae W. Park.
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  • EDWARD KOLBE

    1. The authors are with Oregon State Univ., Seafood Laboratory, 250 36th St., Astoria, OR 97103-2499. Address inquiries to Dr. Jae W. Park.
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  • This work was supported by grant No. NA36RG0451 (project no. R-SF-2) from the National Oceanic and Atmospheric Administration to the Oregon State University Sea Grant College Program and by appropriation made by the Oregon state legislature. The views expressed herein are those of the authors and do not necessarily reflect the view of NOAA or any of its subagencies.

ABSTRACT

Pacific whiting surimi paste was ohmically heated to investigate degradation of myosin heavy chain (MHC) caused by endogenous proteinase over a range of 40–85°C and 0.5–35 min. Degradation was best described with an apparent reaction order of 1.4. Changes of degradation rate increased with temperature and reached a maximum at 57°C. Then, rate of MHC degradation decreased with higher temperature and reached a minimum at 75°C. Ea values of activation and inactivation zone were 142.3 and 83.1 kJ/mol, respectively. Generally, failure shear stress and shear strain increased linearly with MHC content. Proteolytic degradation of actin exhibited the same trend as that of MHC but at a slower rate. The synergistic effect of actin in the gelation of whiting surimi was predominant at ≥75°C.

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