Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment
Authors
Peruško, MarijaSimović, Ana
Stevanović, Nikola
Smiljanić, Katarina
Radomirović, Mirjana Ž.
Stanić-Vučinić, Dragana
Ghnimi, Sami
Ćirković-Veličković, Tanja
Conference object (Published version)
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Show full item recordAbstract
Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand
for camel milk has increased worldwide.Production of camel milk powders facilitate its transport,
prolonge shelf-life, and also offer an attractive additive for various food products. In this study we
characterized proteins of soluble fraction of freeze/spray dried camel milk powders.
Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six
different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon
the treatments were analysed by combination of electrophoretic techniques and circular dichroism.
Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.
Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native
electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of
spray drying. That indicated occurence of the... Maillard reaction. Far-UV circular dichroism spectra
showed no differences in secondary structures between freeze and spray dried samples. Mass
spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1
(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum
albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne
(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on
immunoglobulin heavy chain.
Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray
drying treatment which further may affect techno-functional properties of camel milk powders,
their shelf-life and nutritional value.
Acknowledgments: This work was supported by the Ministry of Education, Science and
Technological Development of the Republic of Serbia, grant number 172024. The project leading to
this application has received funding from the European Union's Horizon 2020 research and
innovation programme under grant agreement No 810752.
Keywords:
camel milk powder / spray drying / Maillard reactionSource:
The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia, 2019, 7-7Publisher:
- The Faculty of Sciences, University of Novi Sad, Serbian proteomic association
Funding / projects:
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-MESTD-Basic Research (BR or ON)-172024)
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-H2020-810752)
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Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - CONF AU - Peruško, Marija AU - Simović, Ana AU - Stevanović, Nikola AU - Smiljanić, Katarina AU - Radomirović, Mirjana Ž. AU - Stanić-Vučinić, Dragana AU - Ghnimi, Sami AU - Ćirković-Veličković, Tanja PY - 2019 UR - http://cherry.chem.bg.ac.rs/handle/123456789/5129 AB - Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand for camel milk has increased worldwide.Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we characterized proteins of soluble fraction of freeze/spray dried camel milk powders. Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic techniques and circular dichroism. Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry. Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Mass spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1 (GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne (CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on immunoglobulin heavy chain. Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray drying treatment which further may affect techno-functional properties of camel milk powders, their shelf-life and nutritional value. Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752. PB - The Faculty of Sciences, University of Novi Sad, Serbian proteomic association C3 - The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia T1 - Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment SP - 7 EP - 7 UR - https://hdl.handle.net/21.15107/rcub_cherry_5129 ER -
@conference{ author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola and Smiljanić, Katarina and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja", year = "2019", abstract = "Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand for camel milk has increased worldwide.Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we characterized proteins of soluble fraction of freeze/spray dried camel milk powders. Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic techniques and circular dichroism. Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry. Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Mass spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1 (GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne (CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on immunoglobulin heavy chain. Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray drying treatment which further may affect techno-functional properties of camel milk powders, their shelf-life and nutritional value. Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752.", publisher = "The Faculty of Sciences, University of Novi Sad, Serbian proteomic association", journal = "The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia", title = "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment", pages = "7-7", url = "https://hdl.handle.net/21.15107/rcub_cherry_5129" }
Peruško, M., Simović, A., Stevanović, N., Smiljanić, K., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia The Faculty of Sciences, University of Novi Sad, Serbian proteomic association., 7-7. https://hdl.handle.net/21.15107/rcub_cherry_5129
Peruško M, Simović A, Stevanović N, Smiljanić K, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia. 2019;:7-7. https://hdl.handle.net/21.15107/rcub_cherry_5129 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola, Smiljanić, Katarina, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment" in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia (2019):7-7, https://hdl.handle.net/21.15107/rcub_cherry_5129 .