Influence of pyrophosphate (PPi) and adenosine 5`-triphosphate (ATP) on the conformational stability and ultrastructure of silver carp myofibrillar proteins at low salinity

Zhuolin Wang; Yuanyong Tian; Yumeng Lin; Yuki Ogasawara; Tetsuro Yamashita; Youling Xiong; Chunhong Yuan

doi:10.1016/j.foohum.2023.09.020

Influence of pyrophosphate (PPi) and adenosine 5`-triphosphate (ATP) on the conformational stability and ultrastructure of silver carp myofibrillar proteins at low salinity

Zhuolin Wang, Yuanyong Tian, Yumeng Lin, Yuki Ogasawara, Tetsuro Yamashita, Youling Xiong, Chunhong Yuan

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

The effect of pyrophosphate (PPi) in comparison with adenosine 5`-triphosphate (ATP) on the thermal and ultrastructural properties of silver carp myofibrillar protein (SMf) was studied. The temperatures for 50 % denaturation (T_1/2) of PPi-treated myosin and actin were 38 °C and 41 °C, respectively, lower than those for control SMf (43 °C and 48 °C, respectively). In comparison, T_1/2 of myosin in ATP-treated SMf was 42 °C, while T_1/2 of actin cannot be detected because no changes in actin digestion pattern. The ultrastructural change of PPi-treated and control SMf differed considerably from that of ATP-treated SMf in which the typical striated structural pattern disappeared, replaced by an aggregated form. In contrast, PPi-treated SMf retained the striated structure with lengthened sarcomere. Therefore, while both PPi and ATP can dissociate actomyosin, the presence of ATP hinders the chymotryptic digestion of actin.

Original language	English
Pages (from-to)	1229-1237
Number of pages	9
Journal	Food and Humanity
Volume	1
DOIs	https://doi.org/10.1016/j.foohum.2023.09.020
State	Published - Dec 2023

Bibliographical note

Publisher Copyright:
© 2023 Elsevier B.V.

Funding

The authors are grateful to Honorary Prof. Kunihiko Konno, Graduate school of Fisheries Science, Hokkaido University, for his comments on the manuscript. The authors also thank Professor Emeritus of the University of Tokyo, Shugo Watabe, for his help in sampling silver carp and for comments on the manuscript. This work was supported by Japan Society for the Promotion of Science (19H05611).

Funders	Funder number
Japan Society for the Promotion of Science Fund for the Promotion of Joint International Research	19H05611
Japan Society for the Promotion of Science Fund for the Promotion of Joint International Research

Keywords

ATP
Low salinity
Myofibrillar protein
Pyrophosphate
Silver carp
Thermostability
Ultrastructure

ASJC Scopus subject areas

Food Science

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10.1016/j.foohum.2023.09.020

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title = "Influence of pyrophosphate (PPi) and adenosine 5`-triphosphate (ATP) on the conformational stability and ultrastructure of silver carp myofibrillar proteins at low salinity",

abstract = "The effect of pyrophosphate (PPi) in comparison with adenosine 5`-triphosphate (ATP) on the thermal and ultrastructural properties of silver carp myofibrillar protein (SMf) was studied. The temperatures for 50 \% denaturation (T1/2) of PPi-treated myosin and actin were 38 °C and 41 °C, respectively, lower than those for control SMf (43 °C and 48 °C, respectively). In comparison, T1/2 of myosin in ATP-treated SMf was 42 °C, while T1/2 of actin cannot be detected because no changes in actin digestion pattern. The ultrastructural change of PPi-treated and control SMf differed considerably from that of ATP-treated SMf in which the typical striated structural pattern disappeared, replaced by an aggregated form. In contrast, PPi-treated SMf retained the striated structure with lengthened sarcomere. Therefore, while both PPi and ATP can dissociate actomyosin, the presence of ATP hinders the chymotryptic digestion of actin.",

keywords = "ATP, Low salinity, Myofibrillar protein, Pyrophosphate, Silver carp, Thermostability, Ultrastructure",

author = "Zhuolin Wang and Yuanyong Tian and Yumeng Lin and Yuki Ogasawara and Tetsuro Yamashita and Youling Xiong and Chunhong Yuan",

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year = "2023",

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doi = "10.1016/j.foohum.2023.09.020",

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AU - Wang, Zhuolin

AU - Tian, Yuanyong

AU - Lin, Yumeng

AU - Ogasawara, Yuki

AU - Yamashita, Tetsuro

AU - Xiong, Youling

AU - Yuan, Chunhong

PY - 2023/12

Y1 - 2023/12

N2 - The effect of pyrophosphate (PPi) in comparison with adenosine 5`-triphosphate (ATP) on the thermal and ultrastructural properties of silver carp myofibrillar protein (SMf) was studied. The temperatures for 50 % denaturation (T1/2) of PPi-treated myosin and actin were 38 °C and 41 °C, respectively, lower than those for control SMf (43 °C and 48 °C, respectively). In comparison, T1/2 of myosin in ATP-treated SMf was 42 °C, while T1/2 of actin cannot be detected because no changes in actin digestion pattern. The ultrastructural change of PPi-treated and control SMf differed considerably from that of ATP-treated SMf in which the typical striated structural pattern disappeared, replaced by an aggregated form. In contrast, PPi-treated SMf retained the striated structure with lengthened sarcomere. Therefore, while both PPi and ATP can dissociate actomyosin, the presence of ATP hinders the chymotryptic digestion of actin.

AB - The effect of pyrophosphate (PPi) in comparison with adenosine 5`-triphosphate (ATP) on the thermal and ultrastructural properties of silver carp myofibrillar protein (SMf) was studied. The temperatures for 50 % denaturation (T1/2) of PPi-treated myosin and actin were 38 °C and 41 °C, respectively, lower than those for control SMf (43 °C and 48 °C, respectively). In comparison, T1/2 of myosin in ATP-treated SMf was 42 °C, while T1/2 of actin cannot be detected because no changes in actin digestion pattern. The ultrastructural change of PPi-treated and control SMf differed considerably from that of ATP-treated SMf in which the typical striated structural pattern disappeared, replaced by an aggregated form. In contrast, PPi-treated SMf retained the striated structure with lengthened sarcomere. Therefore, while both PPi and ATP can dissociate actomyosin, the presence of ATP hinders the chymotryptic digestion of actin.

KW - ATP

KW - Low salinity

KW - Myofibrillar protein

KW - Pyrophosphate

KW - Silver carp

KW - Thermostability

KW - Ultrastructure

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Influence of pyrophosphate (PPi) and adenosine 5`-triphosphate (ATP) on the conformational stability and ultrastructure of silver carp myofibrillar proteins at low salinity

Abstract

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