Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions

• Main Author: Kim, Young S.
• Other Authors: Park, Jae W.
• Language: en_US
• Published: 2012
• Subjects: Surimi; Fishery processing; Muscle proteins
• Online Access: http://hdl.handle.net/1957/27189

Protein solubility of Pacific whiting muscle with isoelectric point at pH 5.5 was significantly affected by pH. The highest breaking force was measured from fish proteins treated at pH 11, while high deformation values were obtained at pH 2 and 11. Texture of gels made using the conventional method were quite inferior to gels made using fish proteins treated at pH 2 or 11, while color of conventional gels was significantly better than the other treatments. SDS-PAGE revealed that fish proteins were highly denatured during acid or alkali treatment. High cathepsin B-like activity was detected from acid-aided fish proteins. Strong cathepsin L-like activity was found in fish proteins treated at pH 10.5, which corresponded with the lower breaking force and deformation obtained from those samples. Disulfide bonds contributed to high texture value in fish proteins treated at pH 11. Physicochemical characteristics of sarcoplasmic proteins (SP) from rockfish and their interaction with Alaska pollock surimi (myofibrillar proteins) were investigated. Solubility of SP was significantly suppressed at acidic pH (2-4) plus high salt concentration (0.5 M NaCl). This was also supported by SDS-PAGE results (extensively degraded SP). DSC results revealed SP gave three endothermic transitions. The least amount ofproteins was lost when treated at pH 2 or 3 followed by precipitation at pH 5.5. SP did not enhance the gelation properties of myofibrillar proteins, but positively contributed to gelation with myofibrillar proteins when compared to sucrose. Myofibrillar proteins were primary components contributing to heat-induced gelation. Salt effect on acid- or alkali-treated surimi gel was investigated. Good gels were obtained without salt using acid- and alkali-treated fish proteins. Their texture properties decreased as NaCl content increased, unlike conventional surimi gels. Consequently, NaCl did not solubilize myofibrillar proteins once the fish proteins were treated by acid or alkali. Solubility was apparently not a key factor for the texture properties of acid- or alkali-treated surimi. Transglutaminase-mediated setting reaction was partially inactivated during acid or alkaline treatment. Acid-treated surimi gel gave the best color properties. === Graduation date: 2003