Evidence map›Paper›PMID 30248998›Full record

ArticleMarine drugs2018

Characterization and Antioxidant and Angiotensin I-Converting Enzyme (ACE)-Inhibitory Activities of Gelatin Hydrolysates Prepared from Extrusion-Pretreated Milkfish (

Chun-Yung Huang, Yung-Hsiang Tsai, Yong-Han Hong, Shu-Ling Hsieh, Ren-Han Huang

Open access · goldAbstract read
In one paragraph

Article in Marine drugs, 2018. 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
1.7field-weighted citation impact, top 15% 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, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Degradation ofMarine drugs · 2020
    Article
  8. 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

5 authors at 3 institutions in 1 country.

Chun-Yung HuangDepartment of Seafood Science, National Kaohsiung University of Science and Technology, No. 142, Haijhuan Rd., Nanzih District, Kaohsiung City 81157, Taiwan. cyhuang@nkust.edu.tw.ORCID 0000-0001-9117-1013
Yung-Hsiang TsaiDepartment of Seafood Science, National Kaohsiung University of Science and Technology, No. 142, Haijhuan Rd., Nanzih District, Kaohsiung City 81157, Taiwan. yht@nkust.edu.tw.
Yong-Han HongDepartment of Nutrition, I-Shou University (Yanchao Campus), No. 8, Yida Rd., Jiaosu Village, Yanchao District, Kaohsiung City 82445, Taiwan. yonghan@isu.edu.tw.
Shu-Ling HsiehDepartment of Seafood Science, National Kaohsiung University of Science and Technology, No. 142, Haijhuan Rd., Nanzih District, Kaohsiung City 81157, Taiwan. slhsieh@nkust.edu.tw.
Ren-Han HuangDepartment of Nursing, Mackay Medical College, No.46, Sec. 3, Zhongzheng Rd., Sanzhi District, New Taipei City 25245, Taiwan. lisa68850@gmail.com.
National Kaohsiung Marine University · TWI-Shou University · TWMackay Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fish gelatin hydrolysates have been shown to possess various biological activities due to their unique Gly-Pro-Y and Gly-X-Hyp sequences. In the current study, fish gelatin was extracted from non-extruded milkfish scale (FSG1) or extrusion-pretreated milkfish scale (FSG2); extracted gelatins were hydrolyzed with different combinations of Flavourzyme and Alcalase to give four different hydrolysates, namely: FSGH1 (FSG1 hydrolyzed with Flavourzyme), FSGH2 (FSG1 hydrolyzed with Alcalase + Flavourzyme), FSGH3 (FSG2 hydrolyzed with Flavourzyme), and FSGH4 (FSG2 hydrolyzed with Alcalase + Flavourzyme). The extrusion-pretreatment process enhanced the extraction yield of gelatin from fish scale. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) analyses showed the extracts FSG1 and FSG2 possessed characteristics of gelatin. Moreover, the physicochemical characteristics of FSGH1⁻FSGH4 were examined by analyses of their degree of hydrolysis, amino acid composition, UV spectrum, FTIR spectrum, molecular weight, and RP-HPLC profile. Additional biological functional analyses showed that all of the studied gelatin hydrolysates FSGH1⁻FSGH4 possessed antioxidant activity dose-dependently as revealed by DPPH scavenging, ABTS scavenging, and reducing power analyses. In addition, FSGH2 and FSGH4 showed higher angiotensin-I-converting enzyme (ACE)-inhibitory activity as compared to FSGH1 and FSGH3. Taken together, FSGH2 and FSGH4 showed high antioxidant activity and potent anti-ACE activity. Due to the potential antioxidant and antihypertensive properties of FSGH2 and FSGH4, further research is needed to explore their possible use as natural supplementary raw materials in food and nutraceutical products.

Indexed as

FishesAngiotensin-Converting Enzyme InhibitorsAnimalsAnimal ScalesAntihypertensive AgentsAntioxidantsChromatography, High Pressure LiquidDietary SupplementsEndopeptidasesEnzyme AssaysGelatinHydrolysisOligopeptidesPeptidyl-Dipeptidase AProtein HydrolysatesSubtilisinsAngiotensin-Converting Enzyme InhibitorsAntihypertensive AgentsAntioxidantsEndopeptidasesflavourzymeGelatinhippuryl-histidyl-leucineOligopeptidesPeptidyl-Dipeptidase AProtein HydrolysatesSubtilisinsAlcalaseangiotensin-I-converting enzymeantioxidantChanos chanosenzyme digestionextrusionFlavourzymegelatingelatin hydrolysate

Identifiers

PMID30248998
PMCPMC6213483
OpenAlexW2891703369

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.