Production and biochemical characterization of Pleurotus ostreatus NRC 620 laccase and evaluation of its efficacy in apple juice clarification.

The highest activity of the Pleurotus ostreatus NRC620 laccase enzyme occurred in the broth of mushroom growth after 25 days of incubation at 28 °C and static conditions. The optimum pH and temperature of the enzyme activity were revealed at pH 3.0, and 70 °C, respectively, and retained 68.

Biochemical characterization and insights into the potency of the acidic Aspergillus niger NRC114 purified α-galactosidase in removing raffinose family oligosaccharides from soymilk yogurt.

Background: Because humans lack α-galactosidase, foods containing certain oligosaccharides from the raffinose family, such as soybeans and other legumes, may disrupt digestion and cause flatulence.

Results: Aspergillus niger NRC114 α-galactosidase was purified using protein precipitation, gel filtration, and ion exchange chromatography steps, which resulted in a 123-fold purification. The purified enzyme was found to be 64 kDa using the SDS-PAGE approach.

A statistical strategy for optimizing the production of α-galactosidase by a newly isolated Aspergillus niger NRC114 and assessing its efficacy in improving soymilk properties.

Background: α-Galactosidase is widely distributed in plants, microorganisms, and animals, and it is produced by different fungal sources. Many studies have confirmed the valuable applications of α-galactosidase enzymes for various biotechnological purposes, like the processing of soymilk.

Results: Aspergillus niger NRC114 was exploited to produce the extracellular α-galactosidase.

Correction to: Biosynthesis and characterization of silver nanoparticles induced by fungal proteins and its application in different biological activities.

In the publication of this article [1], the title of Figure 6 was missing. The original article has been corrected.

Application of response surface methodology to optimize the extracellular fungal mediated nanosilver green synthesis.

This study aims to optimize the biosynthesis of nanosilver particles mediated by ATCC36838 using response surface methodology (RSM). Silver nanoparticles (AgNPs) were biosynthesized effectively in terms of the factors impacting silver ion (Ag) reduction to metallic nanosilver (Ag) using culture filtrate under shaking condition. The results of statistics calculations revealed that 2 mM silver nitrate and 28% (v/v) of culture filtrate at pH 7.

Purification and biochemical characterization of two isolated laccase isoforms from Agaricus bisporus CU13 and their potency in dye decolorization.

Agaricus bisporus CU13 laccase was purified using ammonium sulfate precipitation (40-80%), Sephadex G100, and DEAE Sephadex A50 anion exchange column chromatography, respectively. Two laccase isoenzymes (Lacc1 & Lacc2) with purification folds of 1.40 and 5.

Optimization of silver nanoparticles biosynthesis mediated by NRC1731 through application of statistical methods: enhancement and characterization.

The fungal-mediated silver nanoparticles (AgNPs) biosynthesis optimization via the application of central composite design (CCD) response surface to develop an effective ecofriendly and inexpensive green process was the aim of the current study. Nanosilver biosynthesis using the NRC1731 cell-free filtrate (CFF) was studied through involving the most parameters affecting the AgNPs green synthesis and its interactions effects. The statistical optimization models showed that using 59.

Some properties of two aldolases in extracts of Aspergillus oryzae.

Fructose 1,6-diphosphate (FDP) aldolase and 2-keto-3-deoxy-D-gluconate (KDG) aldolase the two key enzymes of Embden-Meyerhof-Parnas (EMP) and the nonphosphorolytic Entner-Doudoroff (ED) pathways respectively, were identified in cell-free extracts of four Aspergillus oryzae strains grown on D-glucose as sole source of carbon. A. oryzae NRRL 3435 gave the highest enzymatic activity for the two enzymes and selected for further studies.

Hydrolytic cleavage of purine ribonucleosides in Aspergillus phoenicis.

Cell-free extracts of nitrate-grown Aspergillus phoenicis could catalyze the hydrolytic cleavage of the N-glycosidic bond of inosine, guanosine and adenosine to the corresponding base and ribose by the nucleoside hydrolase. No evidence was obtained concerning the hydrolytic degradation of N-glycosidic bond of pyrimidine ribonucleosides namely cytidine and uridine by the same extracts. Optimum pH and temperature for adenosine, guanosine and inosine hydrolysis were the same at pH 3.