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Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa

The global plant-based protein demand is rapidly expanding in line with the increase in the world’s population. In this study, ultrasonic-assisted extraction (UAE) was applied to extract protein from Wolffia globosa as an alternative source. Enzymatic hydrolysis was used to modify the protein proper...

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Autores principales: Siriwat, Warin, Ungwiwatkul, Sunisa, Unban, Kridsada, Laokuldilok, Thunnop, Klunklin, Warinporn, Tangjaidee, Pipat, Potikanond, Saranyapin, Kaur, Lovedeep, Phongthai, Suphat
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10606862/
https://www.ncbi.nlm.nih.gov/pubmed/37893708
http://dx.doi.org/10.3390/foods12203815
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author Siriwat, Warin
Ungwiwatkul, Sunisa
Unban, Kridsada
Laokuldilok, Thunnop
Klunklin, Warinporn
Tangjaidee, Pipat
Potikanond, Saranyapin
Kaur, Lovedeep
Phongthai, Suphat
author_facet Siriwat, Warin
Ungwiwatkul, Sunisa
Unban, Kridsada
Laokuldilok, Thunnop
Klunklin, Warinporn
Tangjaidee, Pipat
Potikanond, Saranyapin
Kaur, Lovedeep
Phongthai, Suphat
author_sort Siriwat, Warin
collection PubMed
description The global plant-based protein demand is rapidly expanding in line with the increase in the world’s population. In this study, ultrasonic-assisted extraction (UAE) was applied to extract protein from Wolffia globosa as an alternative source. Enzymatic hydrolysis was used to modify the protein properties for extended use as a functional ingredient. The successful optimal conditions for protein extraction included a liquid to solid ratio of 30 mL/g, 25 min of extraction time, and a 78% sonication amplitude, providing a higher protein extraction yield than alkaline extraction by about 2.17-fold. The derived protein was rich in essential amino acids, including leucine, valine, and phenylalanine. Protamex and Alcalase were used to prepare protein hydrolysates with different degrees of hydrolysis, producing protein fragments with molecular weights ranging between <10 and 61.5 kDa. Enzymatic hydrolysis caused the secondary structural transformations of proteins from β-sheets and random coils to α-helix and β-turn structures. Moreover, it influenced the protein functional properties, particularly enhancing the protein solubility and emulsifying activity. Partial hydrolysis (DH3%) improved the foaming properties of proteins; meanwhile, an excess hydrolysis degree reduced the emulsifying stability and oil-binding capacity. The produced protein hydrolysates showed potential as anti-cancer peptides on human ovarian cancer cell lines.
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spelling pubmed-106068622023-10-28 Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa Siriwat, Warin Ungwiwatkul, Sunisa Unban, Kridsada Laokuldilok, Thunnop Klunklin, Warinporn Tangjaidee, Pipat Potikanond, Saranyapin Kaur, Lovedeep Phongthai, Suphat Foods Article The global plant-based protein demand is rapidly expanding in line with the increase in the world’s population. In this study, ultrasonic-assisted extraction (UAE) was applied to extract protein from Wolffia globosa as an alternative source. Enzymatic hydrolysis was used to modify the protein properties for extended use as a functional ingredient. The successful optimal conditions for protein extraction included a liquid to solid ratio of 30 mL/g, 25 min of extraction time, and a 78% sonication amplitude, providing a higher protein extraction yield than alkaline extraction by about 2.17-fold. The derived protein was rich in essential amino acids, including leucine, valine, and phenylalanine. Protamex and Alcalase were used to prepare protein hydrolysates with different degrees of hydrolysis, producing protein fragments with molecular weights ranging between <10 and 61.5 kDa. Enzymatic hydrolysis caused the secondary structural transformations of proteins from β-sheets and random coils to α-helix and β-turn structures. Moreover, it influenced the protein functional properties, particularly enhancing the protein solubility and emulsifying activity. Partial hydrolysis (DH3%) improved the foaming properties of proteins; meanwhile, an excess hydrolysis degree reduced the emulsifying stability and oil-binding capacity. The produced protein hydrolysates showed potential as anti-cancer peptides on human ovarian cancer cell lines. MDPI 2023-10-18 /pmc/articles/PMC10606862/ /pubmed/37893708 http://dx.doi.org/10.3390/foods12203815 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Siriwat, Warin
Ungwiwatkul, Sunisa
Unban, Kridsada
Laokuldilok, Thunnop
Klunklin, Warinporn
Tangjaidee, Pipat
Potikanond, Saranyapin
Kaur, Lovedeep
Phongthai, Suphat
Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa
title Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa
title_full Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa
title_fullStr Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa
title_full_unstemmed Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa
title_short Extraction, Enzymatic Modification, and Anti-Cancer Potential of an Alternative Plant-Based Protein from Wolffia globosa
title_sort extraction, enzymatic modification, and anti-cancer potential of an alternative plant-based protein from wolffia globosa
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10606862/
https://www.ncbi.nlm.nih.gov/pubmed/37893708
http://dx.doi.org/10.3390/foods12203815
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