PXD023290

PXD023290 is an original dataset announced via ProteomeXchange.

Title	In gel trypsin digested 1 D resolved bands of freeze-dried camel milk
Description	Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190°C - 250°C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. This study provides useful insights for optimization of CM powder production.
HostingRepository	PRIDE
AnnounceDate	2021-02-25
AnnouncementXML	Submission_2021-02-24_22:07:51.354.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD023290
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Katarina Smiljanic
SpeciesList	scientific name: Camelus dromedarius; NCBI TaxID: 9838;
ModificationList	No PTMs are included in the dataset
Instrument	LTQ Orbitrap XL

Revision	Datetime	Status	ChangeLog Entry
0	2020-12-23 03:53:53	ID requested
⏵ 1	2021-02-24 22:07:51	announced

Dataset with its publication pending

submitter keyword: soluble camel milk protein fraction of lyophilized camel milk, 1 D gel bands in reducing condition of camel milk powder

Tanja D. Cirkovic Velickovic
contact affiliation	Tanja Ćirković Velicković, PhD Professor of Biochemistry & Corresponding member of Serbian Academy of Sciences and Arts University of Belgrade-Faculty of Chemistry, Center of Excellence for Molecular Food Sciences and Department of Biochemistry, Studentski trg 12-16, 11 000 Belgrade, Serbia. Professor of Food Chemistry Department of Environmental Technology, Food Technology and Molecular Biotechnology, Ghent University Global Campus, Yeonsu-Gu, 21985 Incheon, Republic of Korea
contact email	tcirkov@chem.bg.ac.rs
lab head
Katarina Smiljanic
contact affiliation	Senior Research Associate at University of Belgrade-Faculty of Chemistry, Center of Excellence for Molecular Food Sciences
contact email	katarinas@chem.bg.ac.rs
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD023290
     1. Label: PRIDE project
     2. Name: In gel trypsin digested 1 D resolved bands of freeze-dried camel milk