Cargando…
Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro
This study investigated the principal leaf protein (rubisco) solubilization and in vitro ruminal enzyme activity in relation to the molecular structure of proanthocyanidins extracted from leaves of Anogeissus pendula and Eugenia jambolana. Six proanthocyanidin fractions were extracted by 50% (v/v) m...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505871/ https://www.ncbi.nlm.nih.gov/pubmed/36144604 http://dx.doi.org/10.3390/molecules27185870 |
_version_ | 1784796581519687680 |
---|---|
author | Singh, Sultan Koli, Pushpendra Bhadoria, Brijesh K. Agarwal, Manjree Lata, Suman Ren, Yonglin Du, Xin |
author_facet | Singh, Sultan Koli, Pushpendra Bhadoria, Brijesh K. Agarwal, Manjree Lata, Suman Ren, Yonglin Du, Xin |
author_sort | Singh, Sultan |
collection | PubMed |
description | This study investigated the principal leaf protein (rubisco) solubilization and in vitro ruminal enzyme activity in relation to the molecular structure of proanthocyanidins extracted from leaves of Anogeissus pendula and Eugenia jambolana. Six proanthocyanidin fractions were extracted by 50% (v/v) methanol–water followed by 70% (v/v) acetone–water and then distilled water from leaves of A. pendula (AP) and E. jambolana (EJ) to yield EJ–70, EJ–50, EJ–DW, AP–70, AP–50 and AP–DW. Fractions were examined for their molecular structure and their effects on sheep ruminal enzymes and solubilization of rubisco in vitro. All fractions significantly (p < 0.05) inhibited the activity of ruminal glutamic oxaloacetic transaminase and glutamic pyruvic transaminase. The fractions AP–50 and EJ–50 significantly inhibited the activity of the R-cellulase enzyme. Most of the fractions inhibited R-glutamate dehydrogenase activity (p < 0.05) by increasing its concentration, while protease activity decreased by up to 58% with increasing incubation time and concentration. The solubilization of rubisco was observed to be comparatively higher in A. pendula (16.60 ± 1.97%) and E. jambolana (15.03 ± 1.06%) than that of wheat straw (8.95 ± 0.95%) and berseem hay (3.04 ± 0.08%). A significant (p < 0.05) increase in protein solubilization was observed when wheat straw and berseem hay were supplemented with A. pendula and E. jambolana leaves at different proportions. The efficiency of microbial protein was significantly (p < 0.05) greater with the supplementation of leaves of A. pendula in comparison to E. jambolana. The overall conclusion is that the proanthocyanidins obtained from E. jambolana exhibited greater inhibitory activities on rumen enzymes, whereas A. pendula recorded higher protein solubilization. Thus, PAs from A. pendula and E. jambolana appear to have the potential to manipulate rumen enzyme activities for efficient utilization of protein and fiber in ruminants. |
format | Online Article Text |
id | pubmed-9505871 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95058712022-09-24 Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro Singh, Sultan Koli, Pushpendra Bhadoria, Brijesh K. Agarwal, Manjree Lata, Suman Ren, Yonglin Du, Xin Molecules Article This study investigated the principal leaf protein (rubisco) solubilization and in vitro ruminal enzyme activity in relation to the molecular structure of proanthocyanidins extracted from leaves of Anogeissus pendula and Eugenia jambolana. Six proanthocyanidin fractions were extracted by 50% (v/v) methanol–water followed by 70% (v/v) acetone–water and then distilled water from leaves of A. pendula (AP) and E. jambolana (EJ) to yield EJ–70, EJ–50, EJ–DW, AP–70, AP–50 and AP–DW. Fractions were examined for their molecular structure and their effects on sheep ruminal enzymes and solubilization of rubisco in vitro. All fractions significantly (p < 0.05) inhibited the activity of ruminal glutamic oxaloacetic transaminase and glutamic pyruvic transaminase. The fractions AP–50 and EJ–50 significantly inhibited the activity of the R-cellulase enzyme. Most of the fractions inhibited R-glutamate dehydrogenase activity (p < 0.05) by increasing its concentration, while protease activity decreased by up to 58% with increasing incubation time and concentration. The solubilization of rubisco was observed to be comparatively higher in A. pendula (16.60 ± 1.97%) and E. jambolana (15.03 ± 1.06%) than that of wheat straw (8.95 ± 0.95%) and berseem hay (3.04 ± 0.08%). A significant (p < 0.05) increase in protein solubilization was observed when wheat straw and berseem hay were supplemented with A. pendula and E. jambolana leaves at different proportions. The efficiency of microbial protein was significantly (p < 0.05) greater with the supplementation of leaves of A. pendula in comparison to E. jambolana. The overall conclusion is that the proanthocyanidins obtained from E. jambolana exhibited greater inhibitory activities on rumen enzymes, whereas A. pendula recorded higher protein solubilization. Thus, PAs from A. pendula and E. jambolana appear to have the potential to manipulate rumen enzyme activities for efficient utilization of protein and fiber in ruminants. MDPI 2022-09-10 /pmc/articles/PMC9505871/ /pubmed/36144604 http://dx.doi.org/10.3390/molecules27185870 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 Singh, Sultan Koli, Pushpendra Bhadoria, Brijesh K. Agarwal, Manjree Lata, Suman Ren, Yonglin Du, Xin Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro |
title | Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro |
title_full | Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro |
title_fullStr | Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro |
title_full_unstemmed | Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro |
title_short | Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro |
title_sort | proanthocyanidins modulate rumen enzyme activities and protein utilization in vitro |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505871/ https://www.ncbi.nlm.nih.gov/pubmed/36144604 http://dx.doi.org/10.3390/molecules27185870 |
work_keys_str_mv | AT singhsultan proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro AT kolipushpendra proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro AT bhadoriabrijeshk proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro AT agarwalmanjree proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro AT latasuman proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro AT renyonglin proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro AT duxin proanthocyanidinsmodulaterumenenzymeactivitiesandproteinutilizationinvitro |