Study on nucleotide, myofibrillar protein biochemical properties and microstructure of freeze-dried scallop striated muscle during storage and rehydration

Huamao Wei; Md Golam Rasul; Zhongqi Sun; Wenge Yang; Tao Huang; Tetsuro Yamashita; Koichi Takaki; Chunhong Yuan

doi:10.1016/j.foodres.2022.111461

Study on nucleotide, myofibrillar protein biochemical properties and microstructure of freeze-dried scallop striated muscle during storage and rehydration

Food Res Int. 2022 Aug:158:111461. doi: 10.1016/j.foodres.2022.111461. Epub 2022 Jun 13.

Authors

Huamao Wei¹, Md Golam Rasul², Zhongqi Sun¹, Wenge Yang¹, Tao Huang¹, Tetsuro Yamashita³, Koichi Takaki⁴, Chunhong Yuan⁵

Affiliations

¹ College of Food and Pharmaceutical Sciences, Ningbo University, 315211, China; Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China.
² Department of Fisheries Technology, Bangabandhu Sheikh Mujibur Rahman Agricultural University, Gazipur 1706, Bangladesh.
³ Faculty of Agriculture, Iwate University, Ueda 3-18-8, Morioka, Iwate 020-8550, Japan.
⁴ Faculty of Science and Engineering, Iwate University, Ueda 4-3-5, Morioka, Iwate 020-8551, Japan.
⁵ Faculty of Agriculture, Iwate University, Ueda 3-18-8, Morioka, Iwate 020-8550, Japan. Electronic address: chyuan@iwate-u.ac.jp.

PMID: 35840193
DOI: 10.1016/j.foodres.2022.111461

Abstract

The biochemical properties and microstructural changes of freeze-dried Japanese scallop (Patinopecten yessoensis) striated muscle during room temperature storage and rehydration were investigated. The results showed that the content of ATP in freeze-dried scallop muscle remained stable with no significant difference (p > 0.05). However, ATP was rapidly decomposed and AMP accumulated within 1.5 min of rehydration, and HxR and Hx were gradually produced from AMP decomposition with the extension of rehydration time. Besides, the results of chymotryptic digestion patterns demonstrated that the rod of myosin was unstable after dehydration, reflecting lower salt solubility than that of frozen-thawed scallop. In contrast, the myosin subfragment-1 (S-1) was stable, as indicated by the constant of Ca²⁺-ATPase activity of freeze-dried scallops throughout the storage and rehydration (p > 0.05). Furthermore, the microstructural analysis revealed that the Z line of the freeze-dried scallop was broken after dehydration process. This study might be useful for developing high-quality dehydrated scallops in the future.

Keywords: Ca(2+)-ATPase activity; Chymotryptic digestion patterns; Microstructure; SDS-PAGE; Salt solubility.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Monophosphate / analysis
Adenosine Monophosphate / metabolism
Adenosine Triphosphate / analysis
Adenosine Triphosphate / metabolism
Animals
Dehydration / metabolism
Fluid Therapy
Muscle, Skeletal / chemistry
Muscle, Striated*
Nucleotides / analysis
Pectinidae* / chemistry
Proteins / analysis

Substances

Nucleotides
Proteins
Adenosine Monophosphate
Adenosine Triphosphate

Supplementary concepts

Mizuhopecten yessoensis