Open Access

This systematic review critically examines existing literature on the effects of spontaneous fermentation on the nutritional and antinutritional properties of the aforementioned food staples, focusing on the changes in nutrients, digestibility, and antinutrients. The literature search flow was conducted following the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRiSMA-2020) approach. Only peer-reviewed journal articles published in English between 2002 and 2024 were sourced from Scopus, Web of Science, and PubMed. A total of 67 articles were considered eligible after the title, abstract, full text, and quality assessment. It was evident from the various studies consulted in this review that traditional fermentation, though being an ancient food processing practice, remains an important approach for increasing the level of nutrients, reducing antinutritional factors, and enhancing the nutrient digestibility of cereals, legumes, roots, tuber, and plantain. This has made fermented foods an important part of diet and nutrition in many cultures around the world, especially in the global south, with limited access to sophisticated food processing techniques and infrastructure. Overall, the findings suggest that incorporating spontaneous fermentation into the preparation of cereals, legumes, roots, and tuber crops can be a valuable strategy for enhancing the nutritional value and health-promoting properties of these dietary staples.

Substitution of a peptide bond for an imine transforms the irreversible macrocyclization of peptides into a reversible process. The inherent cyclization tendency of a linear peptide is then analyzable through the equilibrium between the aldehyde and the imine by virtue of the higher reactivity of the corresponding linear peptide aldehyde. The tryptophan side chain of segetalin A aldehyde forms a 12‐membered cyclic indole hemiaminal instead of the 18‐membered macrocyclic imine expected. Herein, we analyzed this uncommon hemiaminal that shows that the biosynthesis of cyclic peptides is not necessarily based on linear precursor peptides with a high inherent macrolactamization tendency.

The idea of privileged scaffolds – that there seem to be more bioactive compounds found around some structures than others – is well established for small drug molecules, but has little significance for standalone peptide secondary structures whose adaptable shapes escape the definition of a 3D motif in the absence of a protein scaffold. Here, we joined two independent biological functions in a single highly restricted peptide to support the hypothesis that the β-hairpin shape is the common basis of two otherwise unrelated biological recognition processes. To achieve this, the hydrophobic cluster HWX4LV from the decapeptide cyclic hairpin model peptide C1-C10 cyclo-CHWEGNKLVC was included in the bicyclic peptide 2. The designed β-hairpin peptide C4-C17, C8-C13 bicyclo-KHQCHWECTZGRCRLVCGRSGS (2, Z = citrulline), serves, on the one hand, as a specific epitope for rheumatoid autoantibodies and, on the other hand, shows a not negligible antibiotic effect against the bacterial strain E. coli AS19.