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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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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. |
format | Online Article Text |
id | pubmed-9369619 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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