Location: Plant Genetics ResearchTitle: Adenanthera pavonina, a potential plant-based protein resource: seed protein composition and immunohistochemical localization of trypsin inhibitors
|KIM, SUNHYUNG - University Of Missouri|
|PEREIRA, ADRIANO - University Of Missouri|
|JURKEVICH, ALEXANDER - University Of Missouri|
Submitted to: Food Chemistry: X
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/9/2021
Publication Date: 3/30/2022
Publication URL: https://handle.nal.usda.gov/10113/7672936
Citation: Krishnan, H.B., Kim, S., Pereira, A.E., Jurkevich, A., Hibbard, B.E. 2022. Adenanthera pavonina, a potential plant-based protein resource: seed protein composition and immunohistochemical localization of trypsin inhibitors. Food Chemistry: X. 13. Article 100253. https://doi.org/10.1016/j.fochx.2022.100253.
Interpretive Summary: Adenanthera pavonina is being considered as alternative food source especially in developing countries. Due to population pressure, low agricultural production, and food shortages, researchers are promoting the use of underutilized plant sources for meeting the nutritional needs of human and animals. Adenanthera seeds contain high percentage of protein (22-31%) and oil (11-13%). Despite its nutritional potential in combating malnutrition and food security only limited biochemical studies have been conducted on A. pavonina seed proteins. In this study, we have partially purified some of the abundant seed proteins of A. pavonina and subjected them to biochemical and immunological characterization. Additionally, we also examined the effect of trypsin inhibitors extracted from A. pavonina seeds on western corn rootworm larvae, a devastating corn insect pest in the United States. Our studies demonstrate that A. pavonina seeds contain large amounts of trypsin inhibitor, an anti-nutritional factor. The results of our study will benefit researchers working on improving the nutritional value of the underutilized legumes.
Technical Abstract: Adenanthera pavonina, an underutilized tropical tree, is being promoted as an alternative food source for meeting the nutritional needs of human and animals. In this study, we have shown that trypsin inhibitors as one of the predominant proteins in the seeds of A. pavonina. DE-52 column chromatography resulted in the identification of four peaks with trypsin inhibitor activity. SDS-PAGE and immunoblot analyses revealed DE-52 peaks A and B were enriched in 17 and 15 kDa proteins and these proteins cross-reacted against soybean trypsin inhibitor antibodies. Simulated gastric fluid digestion revealed that the 15–17 kDa proteins are resistant to pepsin digestion. Roasting the seeds lowered the trypsin inhibitor activity while boiling intact seeds elevated the enzyme activity. However, the trypsin inhibitor activity was completely abolished when the seeds were boiled without their seed coats. Immunohistochemical detection and confocal microscopy demonstrated that trypsin inhibitors were localized in the cell cytosol.