Evidence map›Paper›PMID 32617526›Full record

ArticleFood chemistry: X2020

"Rigid" structure is a key determinant for the low digestibility of myoglobin.

Qian Li, Di Zhao, Hui Liu, Miao Zhang, Shuai Jiang, Xinglian Xu, Guanghong Zhou, Chunbao Li

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Food chemistry: X, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Formation of the mutagenic DNA lesion 1,NGenes and environment : the official journal of the Japanese Environmental Mutagen Society · 2023
    Article
  9. Article
  10. Article
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.

Qian LiKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Di ZhaoKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Hui LiuKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Miao ZhangKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Shuai JiangKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Xinglian XuKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Guanghong ZhouKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Chunbao LiKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myoglobin, a critical protein responsible for meat color, has been shown insusceptible to digestion. The underlying mechanism is not clear. The present study aimed to evaluate whether the structural properties of myoglobin are associated with its insusceptibility to digestion using spectroscopic and computational techniques. Myoglobin was degraded by only 7.03% by pepsin and 33.00% by pancreatin. The structure of myoglobin still maintained α-helix after the two-step digestion, with the exposure of some aromatic residues. In addition, molecular dynamics modeling suggested that hydrophobic amino acid residues (Phe 111, Leu 10, Ala 115, Pro 116) in pepsin and polar amino acid residues (Tyr 146, Thr 95) in myoglobin were found in the proximity of binding sites, which could result in the low digestibility of myoglobin. Our findings provide a new insight into the underlying mechanisms on the difficulty in digestion of myoglobin.

Indexed as

DigestibilityLiquid chromatography-tandem mass spectrometryMolecular dockingMolecular dynamicsMyoglobin

Identifiers

PMID32617526
PMCPMC7322683

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.