Do post-translational and processing-born food protein modifications affect protein digestibility and their immune properties?
Конференцијски прилог (Објављена верзија)
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Protein post-translational modifications and those induced by food processing (PTMs) occur in many
forms and can widely influence protein structure and behaviour. Yet, their structural and functional
aspects in protein architecture are mainly overlooked. Until recently, this was mostly a consequence
of insurmountable obstacles related to their global proteome identification and quantification via
mass spectrometry-based proteomics. However, recent advancement in high-resolution tandem mass
spectrometry, coupled with dedicated software, such as PEAKS Studio for an unspecified identification
of PTMs, enabled their confident mapping. In our recent works we have established a method for
global, open and relative quantitative profiling of PTMs without enrichment step, demonstrating its
usefulness in environmental (1), biomedical (2) and food technology (3) sciences.
PTMs could influence enzyme hydrolytic efficiency. This was a starting point to grow the idea of porcine
trypsin bei...ng used in proteomics to serve as a probe to decipher differences in scissile bond hydrolysis
caused by PTMs, based on steric and charge changes introduced as a possible hindrance or facilitation
to its active site. We further hypothesized that the effects observed would be even more pronounced
with human trypsin, since it is less efficient compared to the porcine counterpart. Therefore, we have
reassessed our porcine-derived trypsin-generated proteomic data of the major peanut allergen Ara h 1
from the raw and roasted peanut, to look for possible facilitating/hindrance effects on trypsin digestion
efficacy caused by PTMs positioned on K/R residues, by developing a manual method to analyse the
extent of trypsin hydrolytic efficiency on modified and unmodified sequences. The algorithm based on
machine learning of the big proteomic data in public repositories could be made to determine enzyme
cleavage efficiency in relation to PTMs presence based on our developed manual method and it could
be applied in other life science fields. This topic is important for understanding of peanut (food) allergy
and human gastrointestinal digestion of proteins and PTMs introduced by food processing
Кључне речи:
post-translational modification / protein / scissile bonds / trypsin / protease / PTMs / site-specific / mass spectrometry / peanut allergensИзвор:
3rd Black Sea Association of Food Science and Technology- B-FoST 2023 Congress, 13th-14th December, 2023, Belgrade, Serbia, 2024, 19-19Издавач:
- Black Sea Association of food science and technology (B-FoST)
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - CONF AU - Smiljanić, Katarina PY - 2024 UR - http://cherry.chem.bg.ac.rs/handle/123456789/6435 AB - Protein post-translational modifications and those induced by food processing (PTMs) occur in many forms and can widely influence protein structure and behaviour. Yet, their structural and functional aspects in protein architecture are mainly overlooked. Until recently, this was mostly a consequence of insurmountable obstacles related to their global proteome identification and quantification via mass spectrometry-based proteomics. However, recent advancement in high-resolution tandem mass spectrometry, coupled with dedicated software, such as PEAKS Studio for an unspecified identification of PTMs, enabled their confident mapping. In our recent works we have established a method for global, open and relative quantitative profiling of PTMs without enrichment step, demonstrating its usefulness in environmental (1), biomedical (2) and food technology (3) sciences. PTMs could influence enzyme hydrolytic efficiency. This was a starting point to grow the idea of porcine trypsin being used in proteomics to serve as a probe to decipher differences in scissile bond hydrolysis caused by PTMs, based on steric and charge changes introduced as a possible hindrance or facilitation to its active site. We further hypothesized that the effects observed would be even more pronounced with human trypsin, since it is less efficient compared to the porcine counterpart. Therefore, we have reassessed our porcine-derived trypsin-generated proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to look for possible facilitating/hindrance effects on trypsin digestion efficacy caused by PTMs positioned on K/R residues, by developing a manual method to analyse the extent of trypsin hydrolytic efficiency on modified and unmodified sequences. The algorithm based on machine learning of the big proteomic data in public repositories could be made to determine enzyme cleavage efficiency in relation to PTMs presence based on our developed manual method and it could be applied in other life science fields. This topic is important for understanding of peanut (food) allergy and human gastrointestinal digestion of proteins and PTMs introduced by food processing PB - Black Sea Association of food science and technology (B-FoST) C3 - 3rd Black Sea Association of Food Science and Technology- B-FoST 2023 Congress, 13th-14th December, 2023, Belgrade, Serbia T1 - Do post-translational and processing-born food protein modifications affect protein digestibility and their immune properties? SP - 19 EP - 19 UR - https://hdl.handle.net/21.15107/rcub_cherry_6435 ER -
@conference{ author = "Smiljanić, Katarina", year = "2024", abstract = "Protein post-translational modifications and those induced by food processing (PTMs) occur in many forms and can widely influence protein structure and behaviour. Yet, their structural and functional aspects in protein architecture are mainly overlooked. Until recently, this was mostly a consequence of insurmountable obstacles related to their global proteome identification and quantification via mass spectrometry-based proteomics. However, recent advancement in high-resolution tandem mass spectrometry, coupled with dedicated software, such as PEAKS Studio for an unspecified identification of PTMs, enabled their confident mapping. In our recent works we have established a method for global, open and relative quantitative profiling of PTMs without enrichment step, demonstrating its usefulness in environmental (1), biomedical (2) and food technology (3) sciences. PTMs could influence enzyme hydrolytic efficiency. This was a starting point to grow the idea of porcine trypsin being used in proteomics to serve as a probe to decipher differences in scissile bond hydrolysis caused by PTMs, based on steric and charge changes introduced as a possible hindrance or facilitation to its active site. We further hypothesized that the effects observed would be even more pronounced with human trypsin, since it is less efficient compared to the porcine counterpart. Therefore, we have reassessed our porcine-derived trypsin-generated proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to look for possible facilitating/hindrance effects on trypsin digestion efficacy caused by PTMs positioned on K/R residues, by developing a manual method to analyse the extent of trypsin hydrolytic efficiency on modified and unmodified sequences. The algorithm based on machine learning of the big proteomic data in public repositories could be made to determine enzyme cleavage efficiency in relation to PTMs presence based on our developed manual method and it could be applied in other life science fields. This topic is important for understanding of peanut (food) allergy and human gastrointestinal digestion of proteins and PTMs introduced by food processing", publisher = "Black Sea Association of food science and technology (B-FoST)", journal = "3rd Black Sea Association of Food Science and Technology- B-FoST 2023 Congress, 13th-14th December, 2023, Belgrade, Serbia", title = "Do post-translational and processing-born food protein modifications affect protein digestibility and their immune properties?", pages = "19-19", url = "https://hdl.handle.net/21.15107/rcub_cherry_6435" }
Smiljanić, K.. (2024). Do post-translational and processing-born food protein modifications affect protein digestibility and their immune properties?. in 3rd Black Sea Association of Food Science and Technology- B-FoST 2023 Congress, 13th-14th December, 2023, Belgrade, Serbia Black Sea Association of food science and technology (B-FoST)., 19-19. https://hdl.handle.net/21.15107/rcub_cherry_6435
Smiljanić K. Do post-translational and processing-born food protein modifications affect protein digestibility and their immune properties?. in 3rd Black Sea Association of Food Science and Technology- B-FoST 2023 Congress, 13th-14th December, 2023, Belgrade, Serbia. 2024;:19-19. https://hdl.handle.net/21.15107/rcub_cherry_6435 .
Smiljanić, Katarina, "Do post-translational and processing-born food protein modifications affect protein digestibility and their immune properties?" in 3rd Black Sea Association of Food Science and Technology- B-FoST 2023 Congress, 13th-14th December, 2023, Belgrade, Serbia (2024):19-19, https://hdl.handle.net/21.15107/rcub_cherry_6435 .