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Effect of common foods as supplements for the mycelium growth of Ganoderma lucidum and Pleurotus ostreatus on solid substrates.

ABSTRACT: The transition from a linear to a circular economy is urgently needed to mitigate environmental impacts and loss of biodiversity. Among the many potential solutions, the development of entirely natural-based materials derived from waste is promising. One such material is mycelium-bound composites obtained from the growth of fungi onto solid lignocellulosic substrates, which find applications such as insulating foams, textiles, packaging, etc. During growth, the fungus degrades and digests the substrate to create a web-like stiff network called mycelium. The development of the mycelium is influenced by several factors, including the substrate composition. As food waste accounts for nearly 44% of total municipal solid waste, incorporating food in the substrate composition could be a means to increase the nutrients absorbed by the fungus. In this paper, we study the effects of the addition of food supplements on the growth of two fungal species, Ganoderma lucidum and Pleurotus ostreatus. The substrates, the food supplements, and the mycelia are characterized using Fourier-transform infrared spectroscopy, scanning electron microscopy, and optical microscopy. Our results show that addition of barley as a supplement significantly boosts the growth of G. lucidum and P. ostreatus. Using a common food as a nutritious enrichment for the development of mycelium is a simple and straightforward strategy to create waste-based mycelium-bound biocomposites for a large range of applications, on-site, therefore promoting a circular economy.

SUBMITTER: Soh E

PROVIDER: S-EPMC8631619 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Lacasses are multicopper oxidases that can catalyze aromatic and non-aromatic compounds concomitantly with reduction of molecular oxygen to water. Fungal laccases have generated a growing interest due to their biotechnological potential applications, such as lignocellulosic material delignification, biopulping and biobleaching, wastewater treatment, and transformation of toxic organic pollutants. In this work we selected fungal genes encoding for laccase enzymes GlLCC1 in Ganoderma lucidum and POXA 1B in Pleurotus ostreatus. These genes were optimized for codon use, GC content, and regions generating secondary structures. Laccase proposed computational models, and their interaction with ABTS [2, 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid)] substrate was evaluated by molecular docking. Synthetic genes were cloned under the control of Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase (GAP) constitutive promoter. P. pastoris X-33 was transformed with pGAPZ?A-LaccGluc-Stop and pGAPZ?A-LaccPost-Stop constructs. Optimization reduced GC content by 47 and 49% for LaccGluc-Stop and LaccPost-Stop genes, respectively. A codon adaptation index of 0.84 was obtained for both genes. 3D structure analysis using SuperPose revealed LaccGluc-Stop is similar to the laccase crystallographic structure 1GYC of Trametes versicolor. Interaction analysis of the 3D models validated through ABTS, demonstrated higher substrate affinity for LaccPost-Stop, in agreement with our experimental results with enzymatic activities of 451.08 ± 6.46 UL-1 compared to activities of 0.13 ± 0.028 UL-1 for LaccGluc-Stop. This study demonstrated that G. lucidum GlLCC1 and P. ostreatus POXA 1B gene optimization resulted in constitutive gene expression under GAP promoter and ?-factor leader in P. pastoris. These are important findings in light of recombinant enzyme expression system utility for environmentally friendly designed expression systems, because of the wide range of substrates that laccases can transform. This contributes to a great gamut of products in diverse settings: industry, clinical and chemical use, and environmental applications.

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Effect of common foods as supplements for the mycelium growth of Ganoderma lucidum and Pleurotus ostreatus on solid substrates.

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