Evidence map›Paper›PMID 33902170›Full record

ArticleAnimal bioscience2021

Meat quality, post-mortem proteolytic enzymes, and myosin heavy chain isoforms of different Thai native cattle muscles.

Chanporn Chaosap, Panneepa Sivapirunthep, Ronachai Sitthigripong, Piyada Tavitchasri, Sabaiporn Maduae, Tipyaporn Kusee, Jutarat Setakul, Kazeem Adeyemi

Open access · goldAbstract read
In one paragraph

Article in Animal bioscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 11 citations in OpenAlex.

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  6. Foods (Basel, Switzerland) · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Chanporn ChaosapDepartment of Agricultural Education, Faculty of Industrial Education and Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.
Panneepa SivapirunthepDepartment of Agricultural Education, Faculty of Industrial Education and Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.
Ronachai SitthigripongDepartment of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.
Piyada TavitchasriDepartment of Animal Science, King Mongkut's Institute of Technology Ladkrabang, Prince of Chumphon Campus, Chumphon 86160, Thailand.
Sabaiporn MaduaeDepartment of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.
Tipyaporn KuseeDepartment of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.
Jutarat SetakulDepartment of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.
Kazeem AdeyemiDepartment of Animal Production, Faculty of Agriculture, University of Ilorin, PMB 1515, Ilorin, Nigeria.
King Mongkut's Institute of Technology Ladkrabang · THUniversity of Ilorin · NG

Funding

Thailand Research Fund RDG5320048
6 · The paper itself

Abstract

objectiveThis study investigated the meat quality characteristics, endogenous proteolytic enzymes, collagen content, and myosin heavy chain (MyHC) isoforms of different muscles of Thai native cattle (TNC).

methodsInfraspinatus (IF), Longissimus thoracis (LT), and Supraspinatus (SS) muscles were obtained from two TNC breeds, Kho-Lan (KL, n = 7) and Kho-Isaan (KI, n = 7). The muscle and meat characteristics of TNC breeds and their relationship with MyHC expression were examined.

resultsThree MyHC isoforms namely MyHC I, MyHC IIa, and MyHC IIx were detected in the muscles. The KL had higher (p<0.05) MyHC IIx than the KI. The IF muscle had higher (p<0.05) MyHC I compared to other muscles. The LT muscle had the least MyHC I. The LT had higher (p<0.05) MyHC IIx than the IF and SS muscles. The IF presented the least MyHC IIx. The KL had higher (p<0.05) lightness and moisture content and lower crude protein, redness, cooking loss, shear force, and calpastatin than the KI. The glycogen, total collagen, soluble collagen, crude protein, ash contents, and troponin T degradation product of IF and SS were lower (p<0.05) than that of LT. Ether extract in LT was lower (p<0.05) than that of IF and SS. The percentage of MyHC I, MyHC IIa, and MyHC IIx were significantly correlated with muscle and meat characteristics of TNC.

conclusionThese results suggest that the differences in the MyHC isoforms may partly account for the variation in meat quality between breeds and among muscles of TNC.

Indexed as

CalpainCalpastatinCollagenGlycogenTroponin

Identifiers

PMID33902170
PMCPMC8495336
OpenAlexW3158343158

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.