Evaluation of the gelling ability of actomyosin-paramyosin from giant squid mantle (Dosidicus gigas)

Santacruz-Ortega H., . and Santos-Sauceda I., . and Brown-Bojórquez F., . and Suárez-Jiménez G. M., . and Tolano-Villaverde I. J., . and Márquez-Ríos E., . and Ramírez-Wong B., . Evaluation of the gelling ability of actomyosin-paramyosin from giant squid mantle (Dosidicus gigas). pp. 712-719. ISSN 2231-7546

The process of thermal gelation involves protein denaturation leading to the exposure of functional groups to form new interactions; these conformational changes favour protein-water-protein interactions and help to stabilise the gel. It is known that in muscle proteins myofibrillar proteins such as myosin are responsible for the main functional properties; however in invertebrate species actin and paramyosin exert an influence on the rheological properties of the gels. Therefore in the present work the gelling property of the actomyosin-paramyosin complex was studied. There were significant differences (p 0.05) in hardness and water-retention capacity which was higher for actomyosin-paramyosin isolate (API) than for mantle proteins (MP). This may have been due to its structure being more porous than that of MP which is agglomerated. The API system favoured protein-protein and water-protein interactions; these formed stronger cross-links which in turn favoured gelling. Moreover the presence of sarcoplasmic proteins may be more of a physical-chemical impediment rather than hydrolysis caused by endogenous proteases.

Full text available from: Official URL: http://www.ifrj.upm.edu.my/27%20(04)%202020/DONE%2...

Abstract

The process of thermal gelation involves protein denaturation leading to the exposure of functional groups to form new interactions; these conformational changes favour protein-water-protein interactions and help to stabilise the gel. It is known that in muscle proteins myofibrillar proteins such as myosin are responsible for the main functional properties; however in invertebrate species actin and paramyosin exert an influence on the rheological properties of the gels. Therefore in the present work the gelling property of the actomyosin-paramyosin complex was studied. There were significant differences (p 0.05) in hardness and water-retention capacity which was higher for actomyosin-paramyosin isolate (API) than for mantle proteins (MP). This may have been due to its structure being more porous than that of MP which is agglomerated. The API system favoured protein-protein and water-protein interactions; these formed stronger cross-links which in turn favoured gelling. Moreover the presence of sarcoplasmic proteins may be more of a physical-chemical impediment rather than hydrolysis caused by endogenous proteases.

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Item Type:	Article
AGROVOC Term:	Dosidicus gigas
AGROVOC Term:	Squids
AGROVOC Term:	Aquatic organisms
AGROVOC Term:	Gelling
AGROVOC Term:	Gels
AGROVOC Term:	Proteins
AGROVOC Term:	Gelation
AGROVOC Term:	Denaturation
AGROVOC Term:	Gel electrophoresis
AGROVOC Term:	Scanning microscopy
Depositing User:	Mr. AFANDI ABDUL MALEK
Last Modified:	24 Apr 2025 00:54
URI:	http://webagris.upm.edu.my/id/eprint/9281

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