Affiliation:
1. Section of Genetics, Department of Zoology, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, Uttar
Pradesh, 202001, India
Abstract
Background:
Several reports have indicated that ultrasonication can change the solubility
of muscle proteins and improves the functional properties of meat and isolated muscle proteins.
Moreover, available literature suggests that ultrasonication can significantly improve the gelling
properties of muscle proteins.
Objectives:
The present study was carried out to investigate the effect of low-frequency
ultrasonication on the secondary structure of myosin and the impact of these structural changes on
solubility and gelling ability.
Methods:
Myosin from breast muscles (Pectoralis major) of broiler chicken was extracted and
exposed to low-frequency ultrasonication for 30 min. Four aliquots collected at the interval of 5, 10,
20, and 30 min were analysed for change in ATPase activity, sulfhydryl content, surface
hydrophobicity, alpha-helicity. The possible impact of these changes on heat-induced gelation was
observed through electron micrographs.
Results:
Ultrasonication reduced the enzymatic activity of myosin and increased the reactive
sulfhydryl content. Decreased α-helicity and increased intrinsic fluorescence displayed significant
structural changes at the secondary and tertiary levels. Myosin aggregation, as indicated by electron
micrographs, showed a marked decrease. The microstructure of myosin gels displayed a distinct
correlation with ultrasonication-induced structural changes. Furthermore, improved microstructure led
to a significant increase in the water retention capacity of myosin gels.
Conclusion:
In conclusion, ultrasonication of myosin caused a marked change in structure at the
tertiary and secondary levels. Structural changes apparently confined within the globular head region
and rod portion of myosin were displayed by reduced enzymatic activity and improved
gelation/solubility. Results of our study convincingly showed that ultrasonication improved the
microstructure of myosin gels resulting in increased WHC.
Publisher
Bentham Science Publishers Ltd.
Subject
Biochemistry,General Medicine,Structural Biology