Optimization and scaling up of extracellular polysaccharide production by submerged culture of Ganoderma lucidum on starch-containing medium using response surface methodology and laboratory bioreactors of various designs.

Basidiomycetes, known for their production of bioactive compounds, traditionally use simple sugars for fermentation. However, their ability to degrade complex plant polysaccharides through enzyme secretion presents potential for the use of renewable raw materials. This study focused on the optimization of exopolysaccharide (EPS) production and efficient substrate consumption by Ganoderma lucidum using response surface methodology (RSM).

Creation of Chitinase Producer and Disruption of Micromycete Cell Wall with the Obtained Enzyme Preparation.

A recombinant strain producing a complex of extracellular enzymes including chitinase from Myceliophtora thermophila was created based on the fungus Penicillium verruculosum. The activity of the enzyme preparations obtained from the cultural fluid of the producer strain was 0.55, 0.

Disulfide Bond Engineering of an Endoglucanase from to Improve Its Thermostability.

Endoglucanases (EGLs) are important components of multienzyme cocktails used in the production of a wide variety of fine and bulk chemicals from lignocellulosic feedstocks. However, a low thermostability and the loss of catalytic performance of EGLs at industrially required temperatures limit their commercial applications. A structure-based disulfide bond (DSB) engineering was carried out in order to improve the thermostability of EGLII from .

Enhancement of the enzymatic cellulose saccharification by Penicillium verruculosum multienzyme cocktails containing homologously overexpressed lytic polysaccharide monooxygenase.

The gene lpmo1 encoding Penicillium verruculosum lytic polysaccharide monooxygenase (PvLPMO9A) was sequenced and homologously overexpressed in P. verruculosum B1-537 (ΔniaD) auxotrophic strain under the control of the cbh1 gene promoter in combination with either the cbh1 signal sequence (sCBH1-X series of samples) or the native lpmo1 signal sequence (sLPMO1-X series). Three enzyme samples of the sCBH1-X series were characterized by a lower overall content of cellobiohydrolases (CBHs: 26-45%) but slightly higher content of endoglucanases (EGs: 17-23%) relative to the reference B1-537 preparation (60% of CBHs and 14% of EGs), while the PvLPMO9A content in them made up 9-21% of the total secreted protein.

Properties of a recombinant GH49 family dextranase heterologously expressed in two recipient strains of Penicillium species.

The dexA gene encoding Penicillium funiculosum dextranase (GenBank accession MH581385) belonging to family 49 of glycoside hydrolases (GH49) was cloned and heterologously expressed in two recipient strains, P. canescens RN3-11-7 and P. verruculosum B1-537.