ABSTRACT
Hydrophobins (HFBs) and cerato-platanins (CPs) are surface-active extracellular proteins produced by filamentous fungi. This study identified two HFB genes (pshyd1 and pshyd2) and one CP gene (pscp) in the marine fungus Paradendryphiella salina. The proteins PsCP, PsHYD2, and PsHYD1 had molecular weights of 12.70, 6.62, and 5.98 kDa, respectively, with isoelectric points below 7. PsHYD1 and PsHYD2 showed hydrophobicity (GRAVY score 0.462), while PsCP was hydrophilic (GRAVY score - 0.202). Stability indices indicated in-solution stability. Mass spectrometry identified 2,922 proteins, including CP but not HFB proteins. qPCR revealed differential gene expression influenced by developmental stage and substrate, with pshyd1 consistently expressed. These findings suggest P. salina's adaptation to marine ecosystems with fewer hydrophobin genes than other fungi but capable of producing surface-active proteins from seaweed carbohydrates. These proteins have potential applications in medical biocoatings, food industry foam stabilizers, and environmental bioremediation.
Subject(s)
Fungal Proteins , Hydrophobic and Hydrophilic Interactions , Fungal Proteins/genetics , Fungal Proteins/metabolism , Fungal Proteins/chemistry , Ascomycota/genetics , Ascomycota/metabolism , Ascomycota/chemistry , Seaweed/microbiology , Seaweed/chemistry , Aquatic Organisms/genetics , Aquatic Organisms/metabolism , Gene Expression Regulation, Fungal , Seawater/microbiologyABSTRACT
This study aimed, for the first time, to determine the nutritional composition, beta-glucan and ergosterol contents, phenolic compound composition, and biological and functional activities of a novel mycoprotein produced through a bioconversion process of Durvillaea spp., a brown seaweed. An untargeted metabolomics approach was employed to screen metabolites and annotate molecules with nutraceutical properties. Two products, each representing a distinct consortia of co-cultured fungi, named Myco 1 and Myco 2, were analysed in this study. These consortia demonstrated superior properties compared to those of Durvillaea spp., showing significant increases in total protein (~238%), amino acids (~219%), and ß-D-glucans (~112%). The protein contains all essential amino acids, a low fatty acid content, and exhibits high antioxidant activity (21.5-25.5 µmol TE/g). Additionally, Myco 2 exhibited the highest anti-alpha-glucosidase activity (IC50 = 16.5 mg/mL), and Myco 1 exhibited notable anti-lipase activity (IC50 = 10.5 mg/mL). Among the 69 top differentially abundant metabolites screened, 8 nutraceutical compounds were present in relatively high concentrations among the identified mycoproteins. The proteins and polysaccharides in the mycoprotein may play a crucial role in the formation and stabilization of emulsions, identifying it as a potent bioemulsifier. In conclusion, the bioconversion of Durvillaea spp. results in a mycoprotein with high-quality protein, significant nutritional and functional value, and prebiotic and nutraceutical potential due to the production of unique bioactive compounds.