Characteristics of minerals extracted from the mid-gut gland of Japanese scallop Patinopecten yessoensis at various pH values

• Published in: Fisheries science Vol. 78; no. 3; pp. 675 - 682
• Main Authors: Santoso, Joko, Ishizuka, Yuka, Yoshie-Stark, Yumiko
• Format: Journal Article
• Language: English
• Published: Japan Springer Japan 01.05.2012; Springer Nature B.V
• Subjects: Acidity; Binding sites; Biomedical and Life Sciences; Cadmium; Caustic soda; Copper; Dry matter; Environmental policy; Experiments; Fish & Wildlife Biology & Management; Fisheries; Fishery sciences; Food Science; Freshwater & Marine Ecology; Hydrochloric acid; Life Sciences; Magnesium; Marine; Minerals; Molecular weight; Mollusks; Original Article; Patinopecten yessoensis; Potassium; Proteins; Sodium; Solubility; Studies; Japan; Japanese scallop; Mid-gut gland; Minerals; Cadmium-binding protein; Water-soluble protein; Solubility
• ISSN: 0919-9268; 1444-2906
• DOI: 10.1007/s12562-012-0489-1

This experiment was carried out to determine the proximate composition of the mid-gut gland (MGG) of the Japanese scallop Patinopecten yessoensis to evaluate the characteristics of divalent minerals and water-soluble protein at various pHs, and to examine Cd-binding protein at different molecular weights. MGG of scallop contained protein, fat and ash of 28.9 g/100 g dry matter, 44.6 g/100 g dry matter and 6.78 g/100 dry matter, respectively. MGG also contained the macrominerals sodium, potassium, magnesium and calcium, and the trace minerals iron, zinc, cadmium and copper. The solubility of divalent minerals and water-soluble protein was high in both acidic and alkaline conditions, except that magnesium was not affected by acidity. The solubility of copper and iron had a positive correlation with water-soluble protein at all pH values, whereas cadmium had a strong correlation at alkaline pH. Low-molecular-weight water-soluble protein (fraction III, 437.5 < MW < 1,355) bound cadmium strongly in acidic, neutral and alkaline conditions. However, in acidic conditions cadmium had the strongest binding to protein.