Alternative Proteins as a Source of Bioactive Peptides: The Edible Snail and Generation of Hydrolysates Containing Peptides with Bioactive Potential for Use as Functional Foods

• Main Authors: Maria Hayes, Leticia Mora
• Format: Article
• Language: English
• Published: MDPI AG 2021-01-01
• Series: Foods
• Subjects: edible garden snail; <i>Helix aspersa</i>; protein; hydrolysis; Alcalase^®; heart health
• Online Access: https://www.mdpi.com/2304-8158/10/2/276

Members of the Phylum Mollusca include shellfish such as oysters and squid but also the edible garden snail known as <i>Helix aspersa</i>. This snail species is consumed as a delicacy in countries including France (where they are known as petit-gris), southern Spain (where they are known as Bobe), Nigeria, Greece, Portugal and Italy but is not a traditional food in many other countries. However, it is considered an excellent protein source with a balanced amino acid profile and an environmentally friendly, sustainable protein source. The aim of this work was to develop a different dietary form of snail protein by generating protein hydrolysate ingredients from the edible snail using enzyme technology. A second aim was to assess the bioactive peptide content and potential health benefits of these hydrolysates. <i>H. aspersa</i> hydrolysates were made using the enzyme Alcalase^® and the nutritional profile of these hydrolysates was determined. In addition, the bioactive peptide content of developed hydrolysates was identified using mass spectrometry. The potential heart health benefits of developed snail hydrolysates were measured in vitro using the Angiotensin-I-converting Enzyme (ACE-1; EC 3.4.15.1) inhibition assay, and the ACE-1 inhibitory drug Captopril© was used as a positive control. The generated <i>H. aspersa</i> hydrolysates were found to inhibit ACE-1 by 95.60% (±0.011) when assayed at a concentration of 1 mg/mL (<i>n</i> = 9) compared to the positive control Captopril© which inhibited ACE-1 by 96.53% (±0.0156) when assayed at a concentration of 0.005 mg/mL (<i>n</i> = 3). A total of 113 unique peptide sequences were identified following MS analysis with peptides identified ranging from 628.35 Da (peptide GGGLVGGI—protein accession number sp|P54334|XKDO_BACSU) to 2343.14 Da (peptide GPAGVPGLPGAKGDHGFPGSSGRRGD—protein accession number sp|Q7SIB2|CO4A1_BOVIN) in size using the BIOPEP-UWM database.