Leonid I. Kovalev, Marina A. Kovaleva, Ekaterina A. Ovseychik, Olga I. Klein, Diana A. Koshelkova, Natalia N. Gessler, Maria A. Danilova, Yulia I. Deryabina and Elena P. Isakova*,
{"title":"Changes in the Proteome of Japanese Quails’ Muscles Fed with the Supplements of Phytases of Fungal and Bacterial Origin","authors":"Leonid I. Kovalev, Marina A. Kovaleva, Ekaterina A. Ovseychik, Olga I. Klein, Diana A. Koshelkova, Natalia N. Gessler, Maria A. Danilova, Yulia I. Deryabina and Elena P. Isakova*, ","doi":"10.1021/acsagscitech.4c0055410.1021/acsagscitech.4c00554","DOIUrl":null,"url":null,"abstract":"<p >The changes in the proteomic profiles of pectoral and thigh muscles of Japanese quails (<i>Coturnix japonica</i>) were studied when a biological supplement based on the phytase from <i>Obesumbacterium proteus</i>, encapsulated in <i>Yarrowia lipolytica</i> yeast, was introduced into the diet compared to the commercial fungal phytase (Ladozym proxy) from <i>Aspergillus ficuum</i>. Both phytase preparations provided some changes in the histologic pattern of muscles and increased the protein amount. However, the encapsulated phytase from <i>O. proteus</i> acted more efficiently at normal levels of available phosphorus than the fungal phytase from <i>A. ficuum</i>. It provided a concomitant increase in troponin family proteins and a significant change in the contractility of skeletal muscles. Also, for all the groups using the phytases in the diet, we first demonstrated the acetylation of the N-terminal part of the molecule for four quails’ proteins, namely, parvalbumin alpha isoform X2 (<i>PVALB</i>), <span>l</span>-lactate dehydrogenase A chain (<i>LDHA</i>), a fragment of PDZ, and LIM domain protein 5 isoform X9 (<i>LOC107313615</i>) that could be related to the changes in forming the contractile apparatus of the muscles and the redistribution of the metabolites between aerobic and anaerobic metabolic pathways. It could impact the meat quality via acetylation/deacetylation of some enzymes related to glycogenolysis/glycolysis.</p>","PeriodicalId":93846,"journal":{"name":"ACS agricultural science & technology","volume":"5 6","pages":"962–980 962–980"},"PeriodicalIF":2.3000,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS agricultural science & technology","FirstCategoryId":"1085","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acsagscitech.4c00554","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
The changes in the proteomic profiles of pectoral and thigh muscles of Japanese quails (Coturnix japonica) were studied when a biological supplement based on the phytase from Obesumbacterium proteus, encapsulated in Yarrowia lipolytica yeast, was introduced into the diet compared to the commercial fungal phytase (Ladozym proxy) from Aspergillus ficuum. Both phytase preparations provided some changes in the histologic pattern of muscles and increased the protein amount. However, the encapsulated phytase from O. proteus acted more efficiently at normal levels of available phosphorus than the fungal phytase from A. ficuum. It provided a concomitant increase in troponin family proteins and a significant change in the contractility of skeletal muscles. Also, for all the groups using the phytases in the diet, we first demonstrated the acetylation of the N-terminal part of the molecule for four quails’ proteins, namely, parvalbumin alpha isoform X2 (PVALB), l-lactate dehydrogenase A chain (LDHA), a fragment of PDZ, and LIM domain protein 5 isoform X9 (LOC107313615) that could be related to the changes in forming the contractile apparatus of the muscles and the redistribution of the metabolites between aerobic and anaerobic metabolic pathways. It could impact the meat quality via acetylation/deacetylation of some enzymes related to glycogenolysis/glycolysis.