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 <i>Anogeissus pendula</i> and <i>Eugenia jambolana</i>. Six proanthocyanidin f...
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MDPI AG
2022-09-01
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| Series: | Molecules |
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| author | Sultan Singh Pushpendra Koli Brijesh K. Bhadoria Manjree Agarwal Suman Lata Yonglin Ren Xin Du |
| author_facet | Sultan Singh Pushpendra Koli Brijesh K. Bhadoria Manjree Agarwal Suman Lata Yonglin Ren Xin Du |
| author_sort | Sultan Singh |
| collection | DOAJ |
| 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 <i>Anogeissus pendula</i> and <i>Eugenia jambolana</i>. Six proanthocyanidin fractions were extracted by 50% (<i>v</i>/<i>v</i>) methanol–water followed by 70% (<i>v</i>/<i>v</i>) acetone–water and then distilled water from leaves of <i>A. pendula</i> (AP) and <i>E. jambolana</i> (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 (<i>p</i> < 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 <i>R</i>-cellulase enzyme. Most of the fractions inhibited <i>R</i>-glutamate dehydrogenase activity (<i>p</i> < 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 <i>A. pendula</i> (16.60 ± 1.97%) and <i>E. jambolana</i> (15.03 ± 1.06%) than that of wheat straw (8.95 ± 0.95%) and berseem hay (3.04 ± 0.08%). A significant (<i>p</i> < 0.05) increase in protein solubilization was observed when wheat straw and berseem hay were supplemented with <i>A. pendula</i> and <i>E. jambolana</i> leaves at different proportions. The efficiency of microbial protein was significantly (<i>p</i> < 0.05) greater with the supplementation of leaves of <i>A. pendula</i> in comparison to <i>E. jambolana</i>. The overall conclusion is that the proanthocyanidins obtained from <i>E. jambolana</i> exhibited greater inhibitory activities on rumen enzymes, whereas <i>A. pendula</i> recorded higher protein solubilization. Thus, PAs from <i>A. pendula</i> and <i>E. jambolana</i> appear to have the potential to manipulate rumen enzyme activities for efficient utilization of protein and fiber in ruminants. |
| first_indexed | 2024-03-09T23:01:54Z |
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| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T23:01:54Z |
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| spelling | doaj.art-4d9c57d124384fe7804107cd7399837a2023-11-23T18:00:15ZengMDPI AGMolecules1420-30492022-09-012718587010.3390/molecules27185870Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In VitroSultan Singh0Pushpendra Koli1Brijesh K. Bhadoria2Manjree Agarwal3Suman Lata4Yonglin Ren5Xin Du6ICAR-Indian Grassland and Fodder Research Institute, Jhansi 284003, IndiaICAR-Indian Grassland and Fodder Research Institute, Jhansi 284003, IndiaICAR-Indian Grassland and Fodder Research Institute, Jhansi 284003, IndiaCollege of Science, Health, Engineering and Education, Murdoch University, 90 South Street, Murdoch, WA 6150, AustraliaICAR-Indian Grassland and Fodder Research Institute, Jhansi 284003, IndiaCollege of Science, Health, Engineering and Education, Murdoch University, 90 South Street, Murdoch, WA 6150, AustraliaCollege of Science, Health, Engineering and Education, Murdoch University, 90 South Street, Murdoch, WA 6150, AustraliaThis 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 <i>Anogeissus pendula</i> and <i>Eugenia jambolana</i>. Six proanthocyanidin fractions were extracted by 50% (<i>v</i>/<i>v</i>) methanol–water followed by 70% (<i>v</i>/<i>v</i>) acetone–water and then distilled water from leaves of <i>A. pendula</i> (AP) and <i>E. jambolana</i> (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 (<i>p</i> < 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 <i>R</i>-cellulase enzyme. Most of the fractions inhibited <i>R</i>-glutamate dehydrogenase activity (<i>p</i> < 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 <i>A. pendula</i> (16.60 ± 1.97%) and <i>E. jambolana</i> (15.03 ± 1.06%) than that of wheat straw (8.95 ± 0.95%) and berseem hay (3.04 ± 0.08%). A significant (<i>p</i> < 0.05) increase in protein solubilization was observed when wheat straw and berseem hay were supplemented with <i>A. pendula</i> and <i>E. jambolana</i> leaves at different proportions. The efficiency of microbial protein was significantly (<i>p</i> < 0.05) greater with the supplementation of leaves of <i>A. pendula</i> in comparison to <i>E. jambolana</i>. The overall conclusion is that the proanthocyanidins obtained from <i>E. jambolana</i> exhibited greater inhibitory activities on rumen enzymes, whereas <i>A. pendula</i> recorded higher protein solubilization. Thus, PAs from <i>A. pendula</i> and <i>E. jambolana</i> appear to have the potential to manipulate rumen enzyme activities for efficient utilization of protein and fiber in ruminants.https://www.mdpi.com/1420-3049/27/18/5870flavonoidsproanthocyanidins<i>Anogeissus pendula</i><i>Eugenia jambolana</i>ruminal enzymesrubisco |
| spellingShingle | Sultan Singh Pushpendra Koli Brijesh K. Bhadoria Manjree Agarwal Suman Lata Yonglin Ren Xin Du Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro Molecules flavonoids proanthocyanidins <i>Anogeissus pendula</i> <i>Eugenia jambolana</i> ruminal enzymes rubisco |
| 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 | flavonoids proanthocyanidins <i>Anogeissus pendula</i> <i>Eugenia jambolana</i> ruminal enzymes rubisco |
| url | https://www.mdpi.com/1420-3049/27/18/5870 |
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