Biology subjects

Garcia-Moreno, P. J.

Publications and source records attributed to Garcia-Moreno, P. J..

3 recordsLinked to original sources

bioRxiv2022

Bioinformatically predicted emulsifying peptides and potato protein hydrolysate improves the oxidative stability of microencapsulated fish oil

The aim of this study was to investigate the potential of potato proteins and peptides as emulsifiers in the microencapsulation of fish oil by spray-drying. Microcapsules were produced using a potato protein extract, and fractions enriched in patatin and protease inhibitors. Furthermore, bioinformatically predicted emulsifier peptides from abundant potato proteins and a hydrolysate, obtained through targeted proteolysis of the extract, were investigated. During 28 days of storage at 25{degrees}C, peptides and hydrolysate exhibited better emulsifying properties and higher encapsulation efficiencies compared to native proteins and sodium caseinate. Significant differences (p < 0.05) were observed in the peroxide value (PV) and secondary volatile oxidation products between the microcapsules produced with peptides and native proteins. Microcapsules produced with peptides and hydrolysate showed the highest oxidative stability, not exceeding a PV of 10 meq/kg oil, and with concentrations of volatiles below the odor threshold in oil for five of the six studied compounds. These results show the emulsifying potential of potato peptides and hydrolysate for use in microencapsulation of hydrophobic bioactive ingredients such as fish oil.

bioengineering↗

bioRxiv2022

Targeted hydrolysis of native potato protein: A novel route for obtaining hydrolysates with improved interfacial properties

Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel approach for producing a potato protein hydrolysate with improved emulsifying and foaming properties by data-driven, targeted hydrolysis. Based on previous studies, we selected 15 emulsifier peptides derived from abundant potato proteins, which were clustered based on sequence identity. Through in silico analysis, we determined that from a range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavorzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely to release peptides resembling the target peptides. After applying all proteases individually, hydrolysates were assayed for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial properties was found. Tryp produced a hydrolysate (DH=5.4%) with the highest (P<0.05) emulsifying and foaming abilities, good stabilities, and high aqueous solubility. Using LC-MS/MS, we identified >10,000 peptides in each hydrolysate. Through peptide mapping, we show that random overlapping with known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. While Neut hydrolysates had the highest proportion of peptides with target overlap, they showed inferior interfacial activity. In contrast, Tryp was able to release specifically targeted peptides, explaining the high surface activity observed. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this work shows that data-driven, targeted hydrolysis is a viable, interdisciplinary approach to facilitate hydrolysis design for production of functional hydrolysates from alternative protein sources.

biochemistry↗

bioRxiv2020

Proteomic characterization of pilot scale hot-water extracts from the industrial carrageenan red seaweed Eucheuma denticulatum

Seaweeds have a long history as a resource for polysaccharides/hydrocolloids extraction for use in the food industry due to their functionality as stabilizing agents. In addition to the carbohydrate content, seaweeds also contains a significant amount of protein, which may find application in food and feed. Here, we present a novel combination of transcriptomics, proteomics, and bioinformatics to determine the protein composition in two pilot-scale extracts from Eucheuma denticilatum (Spinosum) obtained via hot-water extraction. The extracts were characterized by qualitative and quantitative proteomics using LC-MS/MS and a de-novo transcriptome assembly for construction of a novel proteome. Using label-free, relative quantification, we were able to identify the most abundant proteins in the extracts and determined that the majority of quantified protein in the extracts (>75%) is constituted by merely three previously uncharacterized proteins. Putative subcellular localization for the quantified proteins was determined by bioinformatic prediction, and by correlating with the expected copy number from the transcriptome analysis, we determined that the extracts were highly enriched in extracellular proteins. This implies that the method predominantly extracts extracellular proteins, and thus appear ineffective for cellular disruption and subsequent release of intracellular proteins. Ultimately, this study highlight the power of quantitative proteomics as a novel tool for characterization of alternative protein sources intended for use in foods. Additionally, the study showcases the potential of proteomics for evaluation of protein extraction methods and as powerful tool in the development of an efficient extraction process.

biochemistry↗