抄録
<jats:title>ABSTRACT</jats:title><jats:p>Turbidity of fish myosin subfragment solutions increased with temperature, except cod heavy meromyosin turbidity leveled above 45°C. Extent of aggregation and number of cross‐linking sites for cod heavy and light meromyosins were significantly higher than for herring (p<0.05), but only at temperatures above 35°C and 45°C, respectively. Thermal aggregation ability increased linearly with increased surface hydrophobicity (S<jats:sub>o</jats:sub>) for the myosin subfragments, except cod heavy meromyosin where the increase in S<jats:sub>o</jats:sub> between 45–55°C did not correspond to an increase in cross‐linking ability. The lessened aggregation ability of herring myosins may be due to the low cross‐linking of the HMM (S‐2) region.</jats:p>
収録刊行物
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- Journal of Food Science
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Journal of Food Science 58 (5), 1057-1061, 1993-09
Wiley
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詳細情報
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- CRID
- 1364233269385102848
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- NII論文ID
- 30022190890
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- ISSN
- 17503841
- 00221147
- http://id.crossref.org/issn/00221147
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- データソース種別
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- Crossref
- CiNii Articles