CHARACTERISTICS OF SARCOPLASMIC PROTEINS AND THEIR INTERACTION WITH MYOFIBRILLAR PROTEINS

By Y. S. Kim, J. Yongsawatdigul, J. W. Park, S. Thawornchinsombut. 2005

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ABSTRACT The protein solubility and molecular-weight distribution of freeze-driedsarcoplasmic proteins (SPs) from rockfish treated under low and high pH aswell as various NaCl concentrations were elucidated. The solubility of SPswas significantly suppressed at an acidic pH (2.0–4.0) and in the presence ofhigh salt concentration (0.5 M NaCl). The least amount of protein was lostwhen SPs were treated at pH 2.0 or 3.0 followed by precipitation at pH 5.5.The interaction of SPs with Alaska pollock surimi (myofibrillar proteins) wasalso investigated. The addition of SPs appeared to delay the thermal denatur-ation of myosin and actin. The SPs positively contributed to the gelation ofmyofibrillar proteins as judged by breaking force. INTRODUCTION A new method for preparing fish protein isolate using pH shift hassignificant advantages over conventional surimi processing. This revolutionaryapproach can reduce water usage and subsequently minimize wastewater prob-lems. The new method can also provide extremely high yields (35–40%)because it solubilizes nearly all myofibrillar and sarcoplasmic proteins (SPs)through homogenization and pH adjustment before centrifugal recovery. Incontrast, the conventional process removes SPs through washing and dewater-ing, which results in significant protein loss and excessive water usage, andcontributes to wastewater problems (Hultin and Kelleher 1999; Hultin

Subfields: Animal Science and Zoology, Insect Science

View Paper: https://www.semanticscholar.org/paper/1b7a79b83d0912e9c0453b56f6ef862f48377153

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In Animal Science and Zoology

  1. I. Undeland
  2. Helgi Nolsøe

In Insect Science

  1. I. Undeland
  2. Helgi Nolsøe

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