Two chitinolytic fungal strains, Trichoderma aureoviride DY-59 and Rhizopus microsporus VS-9, were isolated from soil samples of Korea and Vietnam, respectively. DY-59 and VS-9 crude chitinases secreted by these fungi in the 0.5% swollen chitin culture medium had an optimal pH of 4 and the optimal temperatures of 40 degrees C and 60 degrees C, respectively. Enzymatic hydrolysis products from crab swollen chitin were N-acetyl-beta-D-glucosamine (GlcNAc) by DY-59 chitinase, and GlcNAc and N, N'-diacetylchitobiose (GlcNAc)2 by VS-9 chitinases. The chitinases degraded the cell wall of Fusarium solani hyphae to produce oligosaccharides, among which GlcNAc, (GlcNAc)2, and pentamer (GlcNAc)5 were identified by high-pressure liquid chromatography. DY-59 and VS-9 chitinases inhibited F. solani microconidial germination by more than 70% and 60% at final protein concentrations of 5 and 27 microg mL(-1), respectively, at 30 degrees C for 20 h treatment.
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http://dx.doi.org/10.1007/s00284-007-9033-4 | DOI Listing |
Chemosphere
October 2024
Department of Forensic Medicine and Clinical Toxicology, Faculty of Medicine, Benha University, Egypt.
Environ Geochem Health
August 2024
School of Agriculture and Environment, UWA, The University of Western Australia, Perth, WA, 6009, Australia.
J Fungi (Basel)
April 2024
Institute of Biochemical Technology and Nanotechnology (IBTN), Peoples' Friendship University of Russia na. P.Lumumba (RUDN), 6 Miklukho-Maklaya St., 117198 Moscow, Russia.
When cultivating on wheat bran or deactivated fungal mycelium as a model of "natural growth", the ability of to synthesize extracellular L-lysine-α-oxidase (LysO) simultaneously with cell-wall-degrading enzymes (proteases, xylanase, glucanases, chitinases, etc.), responsible for mycoparasitism, was shown. LysO, in turn, causes the formation of HO and pipecolic acid.
View Article and Find Full Text PDFWorld J Microbiol Biotechnol
June 2022
Amity Institute of Biotechnology, Amity University Uttar Pradesh, Lucknow Campus, Lucknow, 226028, India.
Amino Acids
January 2021
Department of Biochemistry, Peoples' Friendship University, Moscow, Russia.
L-lysine α-oxidase (LO) is an L-amino acid oxidase with antitumor, antimicrobial and antiviral properties. Pharmacokinetic (PK) studies were carried out by measuring LO concentration in plasma and tissue samples by enzyme immunoassay. L-lysine concentration in samples was measured spectrophotometrically using LO.
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