Biochemical and Pharmacokinetic Properties of PEGylated Cystathionine γ-Lyase from Aspergillus carneus KF723837.

Cystathionine γ-lyase (CGL) was purified to its electrophoretic homogeneity from Aspergillus carneus by various chromatographic approaches. The purified enzyme has four identical subunits of 52 kDa based on SDS and native PAGE analyses. To improve its structural stability, purified CGL was modified by covalent binding to polyethylene glycol moieties.

Screening, morphological and molecular characterization of fungi producing cystathionine γ-lyase.

The potency for production of cystathionine γ-lyase (CGL) by the fungal isolates was screened. Among the tested twenty-two isolates, Aspergillus carneus was the potent CGL producer (6.29 U/mg), followed by A.

Characterization of homocysteine γ-lyase from submerged and solid cultures of Aspergillus fumigatus ASH (JX006238).

Among 25 isolates, Aspergillus fumigatus ASH (JX006238) was identified as a potent producer of homocysteine gamma- lyase. The nutritional requirements to maximize the enzyme yield were optimized under submerged (SF) and solid-state fermentation (SSF) conditions, resulting in a 5.2- and 2.

L-methioninase production by filamentous fungi: I-screening and optimization under submerged conditions.

Findings show 21 fungal isolates belonging to eight genera recovered from Egyptian soils that have the potential to attack L-methionine under submerged conditions. Aspergillus flavipes had the most methioninolytic activity, giving the highest yield of L-methioninase (10.78 U/mg protein), rate of methionine uptake (93.