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The essential oils from aromatic plants are today considered a suitable tool to protect stored grains from fungal attacks. The purpose of this work is to study the effect of formulations of thyme and oregano essential oil (EO) adsorbed on purified (Gh-P) and sulfuric acid-activated (Gh-A) ghassoul on the biological activity of fungal pathogens. Purified and activated ghassoul were characterized by XRD and FTIR, and EOs used in this study were issued from two medicinal plants known in Morocco and commercially available. Their chemical compositions were analyzed by the GC-MS technique. The main constituents of thyme EO were thymol (67.13%), ρ-cymene (4.85%), Z-caryophyllene (1.77%), and γ-terpinene (2.74%). Oregano EO contained carvacrol (59.82%), γ-terpinene (10.85%), and α-pinene (9.89%). This work focused on the study of the antifungal activity of EOs mixed with purified and sulfuric acid-activated ghassoul, in order to look for new natural bioactive products and assess their antifungal activity. Penicillium sp. was used as a pathogen agent for biological activity on Czapek agar medium. The results showed that the active ghassoul formulations had significant antifungal activity against Penicillium sp. Gh-A-thyme, Gh-A-thymol, and Gh-A-oregano had an inhibitory potential of more than 75% and excelled to retain it over time even after five months. On the other hand, the three purified ghassoul formulations (Gh-P-thyme, Gh-P-thymol, and Gh-P-oregano) showed an initial inhibitory power of less than 22%, which was decreasing over time.

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Description of the subject. Extracellular enzymes from filamentous fungi are increasingly used in eco-friendly biotransformation processes. Their relevant technological role and their stability towards extreme process conditions make of them the first sustainable solution for the elaboration of bio-based products from biomass conversion. Objectives. This paper describes the isolation of filamentous fungi from decaying plant material in the region of Meknes (northern central Morocco) and the assessment of their ability to breakdown lignocellulose. The objective is to select performant fungi with enzymatic machinery adapted to local environment and with potential for the breakdown of the regional specific lignocellulosic by-products into potentially high-value molecules. Method. Cereals, decaying wood, olive-pomace and -pulp and their composts were used to isolate lignocellulolytic fungi. One hundred twenty-seven pure strains were isolated and screened at 25 °C on selective media with cellulose or lignin as the sole carbon source. Performant strains were validated for the production of ligno-cellulolytic enzymes and identified using molecular technique. Results. Twenty-eight fungi had mycelial diameter on cellulose ≥ 6 cm and cellulolytic index ≥ 0.9. Twenty-two strains had the same profile on lignin medium. The production of endoglucanase, lignin peroxidase and manganese peroxidase enzymes was confirmed in performant strains using qualitative assay and molecular identification revealed that the best performing fungi were Mucor circinelloides, Mucor racemosus, Penicillium brasilianum, Penicillium crustosum, Paecilomyces sp., Fusarium oxysporum, Fusarium solani, Aspergillus fischeri, Curvularia spicifera, Humicola grisea, Trichoderma atroviride and Cosmospora viridescens. Measurement of ligno-cellulolytic activities revealed that Penicillium and Fusarium strains mainly from wood decay and compost had the best profiles among performing strains. Conclusions. Isolated fungi are high decomposers of biomass and represent a prominent solution to develop green bioprocesses in the region.

This study, for the first time, reports the functional expression of lipase B derived from the yeast Candida antarctica (CALB) in Corynebacterium strain using the Escherichia coli plasmid PK18. The CALB gene fragment encoding a 317-amino-acid protein was successfully obtained from the total RNA of C. antarctica. CALB was readily produced in the Corynebacterium strain without the use of induction methods described in previous studies. This demonstrated the extracellular production of CALB in the Corynebacterium strain. CALB produced in the Corynebacterium MB001 strain transformed with pEC-CALB recombinant plasmid exhibited maximum extracellular enzymatic activity and high substrate affinity. The optimal pH and temperature for the hydrolysis of 4-nitrophenyl laurate by CALB were 9.0 and 40℃, respectively. The enzyme was stable at pH 10.7 in the glycine-KOH buffer and functioned as an alkaline lipase. The CALB activity was inhibited in the presence of high concentration of Mg 2+ , which indicated that CALB is not a metalloenzyme. These properties are key for the industrial application of the enzyme.

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