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Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications

Hemp (Cannabis sativa L.) processing by-products (hemp cake and hemp seed hulls) were studied for their protein content, extraction of protein isolates (PIs), and their in vitro protein digestibility (IVPD). Crude protein contents of hemp cake and hemp seed hulls were 30.4% and 8.6%, respectively, c...

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Autores principales: Banskota, Arjun H., Tibbetts, Sean M., Jones, Alysson, Stefanova, Roumiana, Behnke, Joerg
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9369619/
https://www.ncbi.nlm.nih.gov/pubmed/35956747
http://dx.doi.org/10.3390/molecules27154794
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author Banskota, Arjun H.
Tibbetts, Sean M.
Jones, Alysson
Stefanova, Roumiana
Behnke, Joerg
author_facet Banskota, Arjun H.
Tibbetts, Sean M.
Jones, Alysson
Stefanova, Roumiana
Behnke, Joerg
author_sort Banskota, Arjun H.
collection PubMed
description Hemp (Cannabis sativa L.) processing by-products (hemp cake and hemp seed hulls) were studied for their protein content, extraction of protein isolates (PIs), and their in vitro protein digestibility (IVPD). Crude protein contents of hemp cake and hemp seed hulls were 30.4% and 8.6%, respectively, calculated based on generalized N-to-P conversion factor (N × 5.37). Extraction efficiency of PIs from defatted biomass ranged from 56.0 to 67.7% with alkaline extraction (0.1 M NaOH) followed by isoelectric precipitation (1.0 M HCl). Nitrogen analysis suggested that the total protein contents of PIs extracted using three different alkaline conditions (0.5 M, 0.1 M, and pH 10.0 with NaOH) were >69.7%. The hemp by-product PIs contained all essential amino acids (EAAs) required for fish with leucine, valine, and phenylalanine belonging to the five dominant amino acids. Overall, glutamate was the dominant non-EAA followed by aspartate. Coomassie staining of an SDS-PAGE gel revealed strong presence of the storage protein edestin. High IVPD of >88% was observed for PIs extracted from hemp seeds and by-products when evaluated using a two-phase in vitro gastric/pancreatic protein digestibility assay. PIs extracted from by-products were further tested for their antioxidant activities. The tested PIs showed dose-dependent DPPH radical scavenging activity and possessed strong ORAC values > 650 μM TE/g.
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spelling pubmed-93696192022-08-12 Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications Banskota, Arjun H. Tibbetts, Sean M. Jones, Alysson Stefanova, Roumiana Behnke, Joerg Molecules Article Hemp (Cannabis sativa L.) processing by-products (hemp cake and hemp seed hulls) were studied for their protein content, extraction of protein isolates (PIs), and their in vitro protein digestibility (IVPD). Crude protein contents of hemp cake and hemp seed hulls were 30.4% and 8.6%, respectively, calculated based on generalized N-to-P conversion factor (N × 5.37). Extraction efficiency of PIs from defatted biomass ranged from 56.0 to 67.7% with alkaline extraction (0.1 M NaOH) followed by isoelectric precipitation (1.0 M HCl). Nitrogen analysis suggested that the total protein contents of PIs extracted using three different alkaline conditions (0.5 M, 0.1 M, and pH 10.0 with NaOH) were >69.7%. The hemp by-product PIs contained all essential amino acids (EAAs) required for fish with leucine, valine, and phenylalanine belonging to the five dominant amino acids. Overall, glutamate was the dominant non-EAA followed by aspartate. Coomassie staining of an SDS-PAGE gel revealed strong presence of the storage protein edestin. High IVPD of >88% was observed for PIs extracted from hemp seeds and by-products when evaluated using a two-phase in vitro gastric/pancreatic protein digestibility assay. PIs extracted from by-products were further tested for their antioxidant activities. The tested PIs showed dose-dependent DPPH radical scavenging activity and possessed strong ORAC values > 650 μM TE/g. MDPI 2022-07-27 /pmc/articles/PMC9369619/ /pubmed/35956747 http://dx.doi.org/10.3390/molecules27154794 Text en © 2022 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
Banskota, Arjun H.
Tibbetts, Sean M.
Jones, Alysson
Stefanova, Roumiana
Behnke, Joerg
Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications
title Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications
title_full Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications
title_fullStr Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications
title_full_unstemmed Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications
title_short Biochemical Characterization and In Vitro Digestibility of Protein Isolates from Hemp (Cannabis sativa L.) By-Products for Salmonid Feed Applications
title_sort biochemical characterization and in vitro digestibility of protein isolates from hemp (cannabis sativa l.) by-products for salmonid feed applications
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9369619/
https://www.ncbi.nlm.nih.gov/pubmed/35956747
http://dx.doi.org/10.3390/molecules27154794
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