Research Keyword: cellulase activity

PRMT5 promotes cellulase production by regulating the expression of cellulase gene eg2 through histone methylation in Ganoderma lucidum

mycolabadmin

Scientists discovered that a protein called PRMT5 helps mushrooms (Ganoderma lucidum) produce more cellulase enzymes, which break down plant materials like corn straw and corn cobs. By controlling a specific gene called eg2 through a chemical modification on histone proteins, PRMT5 increases enzyme production. This discovery could help industries produce cellulase more efficiently and sustainably convert agricultural waste into useful sugars for biofuels and other products.

Read More »

GlSlt2 positively regulates GlMyb-mediated cellulose utilization in Ganoderma lucidum

mycolabadmin

Scientists discovered how a medicinal mushroom called Ganoderma lucidum breaks down cellulose from plant waste. The study found that a protein called GlSlt2 activates another protein called GlMyb, which then turns on genes that produce cellulase enzymes. These enzymes break down cellulose into sugar that the fungus can use for growth. This discovery could help improve the conversion of agricultural waste into biofuels and other useful products.

Read More »

Isolation and screening of wood-decaying fungi for lignocellulolytic enzyme production and bioremediation processes

mycolabadmin

Researchers isolated wood-decaying fungi from forests in Latvia to identify species that produce powerful enzymes capable of breaking down complex plant materials. These enzymes have practical applications in cleaning contaminated water, treating textile industry waste, and converting plant biomass into useful products. The study found that certain environmental fungi, particularly Trametes pubescens, produced enzymes at levels exceeding those of commercially used strains, suggesting they could be valuable tools for environmental cleanup and industrial processes.

Read More »

PRMT5 promotes cellulase production by regulating the expression of cellulase gene eg2 through histone methylation in Ganoderma lucidum

mycolabadmin

Scientists discovered that a protein called PRMT5 controls how much cellulase enzyme the medicinal mushroom Ganoderma lucidum produces. When PRMT5 activates a specific gene called eg2 through a molecular modification of histone proteins, the mushroom produces more cellulase. This enzyme is valuable for breaking down plant waste into useful sugars for industrial and bioenergy applications. This research could help develop better enzyme-producing strains for industries that need cellulase.

Read More »

Efficient conversion of tea residue nutrients: Screening and proliferation of edible fungi

mycolabadmin

Tea waste from instant tea production is typically discarded, but researchers discovered that edible fungi can efficiently convert this waste into nutritious fungal protein. By testing six different mushroom species, they found that Monascus kaoliang B6 was the most effective, using special enzymes to break down the tough plant fibers and convert nutrients into fungal biomass. This process offers an eco-friendly solution to tea industry waste while producing valuable food ingredients.

Read More »

PRMT5 promotes cellulase production by regulating the expression of cellulase gene eg2 through histone methylation in Ganoderma lucidum

mycolabadmin

Scientists discovered that a protein called PRMT5 in Ganoderma lucidum mushroom plays a key role in producing cellulase enzymes that break down plant cellulose. By controlling a specific gene (eg2) through a process called histone methylation, PRMT5 increases cellulase production. This finding could help develop more efficient ways to convert agricultural waste like corn straw into useful sugars for biofuels and other industrial products.

Read More »
Scroll to Top