Abstract
Garden cress seed (GCS) (Lepidium sativum) waste present potential economic value owing to their health benefits mediated by a presence of unique biopeptides. This study was conducted to investigate the best possible valorization of garden cress seed (GCS) (Lepidium sativum) waste that generated from edible oil extraction. Physical, structural, morphological, and dielectric properties of protein concentrate and hydrolysate obtained from oil extracted garden cress pomace. The obtained protein and hydrolysate at two different hydrolysis degrees (10% and 15%) were characterized for color properties, amino acid composition, atomic force microscope (AFM) topography, Scanning electron microscope (SEM) microscopy and dielectric profile. Protein hydrolysates showed a significant increase in some of the amino acids (Asp, Glu, Gly, Arg, Cys, and Phe) with an increase in the degree of hydrolysis (%DH). The color values showed a minor increase due to hydrolysis of GCS protein. The SEM and AFM observations of the morphological structure of garden cress seed protein concentrate (GCSPC) and garden cress seed protein hydrolysates (GCSPHs) confirmed flat disk like shape of GCS protein and pore formation due to Alcalase hydrolysis. It was interesting to find that Alcalase hydrolysis reduced the Root Mean Square height and Arithmetic mean height of GCS protein particles. The dielectric constant (ε′) decreased with Alcalase hydrolysis. Enhanced crystallinity of GCS protein was observed due to hydrolysis.
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Acknowledgements
The authors would like to thank Novozymes, in particular, Dr. Sibabrata Banerjee, for their generosity for providing enzymes for the work and also to the project, GE01/07, Kuwait University Nanotechnology Research Facility (KUNRF).
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Mulla, M.Z., Ahmed, J., Habeebullah, S.F.K. et al. Amino acid composition, microstructure and dielectric properties of garden cress (Lepidium sativum) seed protein concentrate and hydrolysate as influenced by degree of hydrolysis. Food Measure 16, 5058–5065 (2022). https://doi.org/10.1007/s11694-022-01588-8
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DOI: https://doi.org/10.1007/s11694-022-01588-8