Evidence map›Paper›PMID 27621693›Full record

ArticleKorean journal for food science of animal resources2016

Hydrolysis by Alcalase Improves Hypoallergenic Properties of Goat Milk Protein.

Tae-Hwan Jung, Sung-Seob Yun, Won-Jae Lee, Jin-Wook Kim, Ho-Kyung Ha, Michelle Yoo, Hyo-Jeong Hwang, Woo-Min Jeon, Kyoung-Sik Han

Open access · bronzeAbstract read
In one paragraph

Article in Korean journal for food science of animal resources, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

3 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Polymorphisms ofFoods (Basel, Switzerland) · 2024
    Article
  3. 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

9 authors at 3 institutions in 2 countries.

Tae-Hwan JungDepartment of Animal Biotechnology and Resource, Sahmyook University, Seoul 01795, Korea.
Sung-Seob YunR&D Center, Edam Co., Ltd., Chungbuk 38755, Korea.
Won-Jae LeeDepartment of Animal Bioscience and Institute of Agriculture and Life Science, Gyeongsang National University, Jinju 52828, Korea.
Jin-Wook KimDepartment of Animal Bioscience and Institute of Agriculture and Life Science, Gyeongsang National University, Jinju 52828, Korea.
Ho-Kyung HaDepartment of Animal Bioscience and Institute of Agriculture and Life Science, Gyeongsang National University, Jinju 52828, Korea.
Michelle YooCentre for Food Science, School of Sciences, Auckland University of Technology, New Zealand.
Hyo-Jeong HwangDepartment of Animal Biotechnology and Resource, Sahmyook University, Seoul 01795, Korea.
Woo-Min JeonDepartment of Animal Biotechnology and Resource, Sahmyook University, Seoul 01795, Korea.
Kyoung-Sik HanDepartment of Animal Biotechnology and Resource, Sahmyook University, Seoul 01795, Korea.
Sahmyook University · KRGyeongsang National University · KRAuckland University of Technology · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Goat milk is highly nutritious and is consumed in many countries, but the development of functional foods from goat milk has been slow compared to that for other types of milk. The aim of this study was to develop a goat milk protein hydrolysate (GMPH) with enhanced digestibility and better hypoallergenic properties in comparison with other protein sources such as ovalbumin and soy protein. Goat milk protein was digested with four commercial food-grade proteases (separately) under various conditions to achieve the best hydrolysis of αs -casein and β-lactoglobulin. It was shown that treatment with alcalase (0.4%, 60℃ for 30 min) effectively degraded these two proteins, as determined by SDS-PAGE, measurement of nonprotein nitrogen content, and reverse-phase high-performance liquid chromatography. Hydrolysis with alcalase resulted in a significant decrease in β-lactoglobulin concentration (almost to nil) and a ~40% reduction in the level of αs-casein. Quantification of histamine and TNF-α released from HMC-1 cells (human mast cell line) showed that the GMPH did not induce an allergic response when compared to the control. Hence, the GMPH may be useful for development of novel foods for infants, the elderly, and convalescent patients, to replace cow milk.

Indexed as

alcalasegoat milk protein hydrolysateαs-caseinβ-lactoglobulin

Identifiers

PMID27621693
PMCPMC5018512
OpenAlexW2513385628

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.