Substrates of Opposite Polarities and Downstream Processing for Efficient Production of the Biosurfactant Mannosylerythritol Lipids from Moesziomyces spp.

Biosurfactants can replace fossil-driven surfactants with positive environmental impacts, owing to their low eco-toxicity and high biodegradability. However, their large-scale production and application are restricted by high production costs. Such costs can be reduced using renewable raw materials and facilitated downstream processing. Here, a novel strategy for mannosylerythritol lipid (MEL) production explores the combination of hydrophilic and hydrophobic carbon sources sideways with a novel downstream processing strategy, based on nanofiltration technology. Co-substrate MEL production by Moesziomyces antarcticus was threefold higher than using D-glucose with low levels of residual lipids. The use of waste frying oil instead of soybean oil (SBO) in co-substrate strategy resulted in similar MEL production. Moesziomyces antarcticus cultivations, using 3.9 M of total carbon in substrates, yields 7.3, 18.1, and 20.1 g/L of MEL, and 2.1, 10.0, and 5.1 g/L of residual lipids, for D-glucose, SBO, and a combination of D-Glucose and SBO, respectively. Such approach makes it possible to reduce the amount of oil used, offset by the equivalent molar increase in D-glucose, improving sustainability and decreasing residual unconsumed oil substrates, facilitating downstream processing. Moesziomyces spp. also produces lipases that broken down the oil and, thus, residual unconsumed oils are in the form of free fatty-acids or monoacylglycerol, which are smaller molecules than MEL. Therefore, nanofiltration of ethyl acetate extracts from co-substrate-based culture broths allows to improve MEL purity (ratio of MEL per total MEL and residual lipids) from 66 to 93% using 3-diavolumes.

Industrial sustainability of microbial keratinases: production and potential applications.

Keratinases are proteolytic enzymes with a particular ability to cleave peptide bonds in keratin, and in other proteins. Due to their broad-spectrum of activity, keratinases are considered viable substitutes for chemical and thermal treatments of protein-rich industrial by-products. Among these protein residues, special attention has been given to keratinous materials (feathers, hair, horns, etc.), which disposal through harsh conditions methods, such as acid/alkaline hydrolysis or incineration, is not considered ecologically safe. Microbial keratinolytic enzymes allow for keratin degradation under mild conditions, resulting in keratin hydrolysates containing undamaged amino acids and peptides. In this review article, we offer perspectives on the relevance of these unique biocatalysts and their revolutionary ascent in industries that generate keratin-rich wastes. Additionally, we share insights for applications of keratinases and protein hydrolysates in agriculture, animal feed, cosmetics, phamaceuticals, detergent additives, leather processing, and others. Due to the scientific importance of keratinases and their potential use in green technologies, searching for bacterial and fungal species that efficiently produce these enzymes may contribute to the sustainability of industries.