Dataset Information

The seed mitochondrial proteome of Lupinus albus provides insight into energy metabolism during germination

ABSTRACT: Despite their essential role in fueling the onset of metabolism, the composition and functional state of seed mitochondria are still a matter of debate. Using white lupin (Lupinus albus) as a model, we provide a comprehensive proteomic characterization of seed mitochondria in a legume with protein-rich reserves. Highly enriched mitochondrial fractions isolated from quiescent seeds revealed fully assembled oxidative phosphorylation (OXPHOS) complexes and supercomplexes, demonstrating that mitochondria are preconfigured for immediate energy production upon imbibition. Quantitative proteomics identified 1,162 mitochondrial proteins and highlighted marked tissue-specific differences compared to leaves, including distinct transporter profiles and a dehydrogenase complement supporting amino acid and fatty acid catabolism. Early germination was accompanied by remodeling of coenzyme metabolism and transport capacity, while core respiratory complexes remained stable. Notably, ~12% of the proteome consisted of uncharacterized proteins, many of which displayed dynamic changes during early germination, suggesting yet undiscovered, potentially legume-specific mitochondrial functions.

INSTRUMENT(S):

ORGANISM(S): Lupinus Albus

TISSUE(S): Seed, Leaf

SUBMITTER: Björn Heinemann

LAB HEAD: Prof. Dr. Tatjana Hildebrandt

PROVIDER: PXD068370 | Pride | 2025-09-18

REPOSITORIES: pride

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Source:

			Action	DRS
	LupinSeedMito_MQ_combined.zip	Other
	LupinSeedMito_MQ_output_MS-RAW.zip	Other
	Sample_Information.xlsx	Xlsx

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Project description:Germination offers advantages to improve legume protein digestibility as it disintegrates seed structure and hydrolyzes proteins and anti-nutrients. Seed permeability (related to polyphenol content of seed coats) is an important factor affecting the duration of seed germination and its impact in protein digestibility and bioactivity. The objective was to compare the effect of seed germination on protease activity, structure and proteolysis of four selected legumes with contrasting seed coat polyphenol profiles (gray zero tannin [GZL], beluga [BL] and dehulled red [DL] lentils; and zero tannin/low vicine-convicine fava bean [ZF]). Protein hydrolysis was characterized during germination and digestion with respect to proteins, peptides and free amino acids (FAA). In vitro antihypertensive and antioxidant activities of digests were investigated, and peptidomic characterization (HPLC-MS/MS) and identification of bioactive fragments in intestinal digests were performed. Regardless of seed type, germination increased protease activity and reduced levels of phytic acid, trypsin inhibitors and tannins (only in BL). Significant proteolysis of the 7S and 11S globulins and concomitant increase peptides and FAA was observed in all sprouted legumes. Digestion kinetics in sprouts revealed a faster generation of FAA and peptides than in dry seeds, with changes more evident for DL associated to faster imbibition, germination and sprout growth. In contrast, BL sprouts showed the lowest protein digestibility, likely due to lower protease activity levels, seed structure disintegration and higher anti-nutrient levels in comparison to GZL, DL and ZF. Moreover, digestion of sprouts resulted in a higher number of resistant peptides in DL and ZF that matched with previously reported bioactive sequences, suggesting a promising health potential of legume sprouts that was confirmed in vitro. Results suggested that the germination process improved protein digestibility and health promoting potential of lentil and fava bean proteins although these changes were more evident in DL due to its rapid imbibition, faster germination and sprout development. This study will provide important information for either plant breeders to develop legume varieties with permeable seed coats or food producers that could use dehulled seeds for efficient production of sprouts as sustainable food sources of plant proteins with improved nutritional and healthy properties.

Dataset Information

The seed mitochondrial proteome of Lupinus albus provides insight into energy metabolism during germination

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