Antifungal activity and patterns of N-acetyl-chitooligosaccharide degradation via chitinase produced from Serratia marcescens PRNK-1
| Autor: | Seung-Hee Choi, Chaeyeong Moon, Yong-Su Song, Sin-Hyoung Hong, Woo-Jin Jung, Dong-Jun Seo |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Hyphal growth Antifungal Agents 030106 microbiology Hyphae Oligosaccharides Chitin Cockroaches Microbiology Rhizoctonia Rhizoctonia solani 03 medical and health sciences Fusarium Fusarium oxysporum Enzyme Stability Animals Incubation Phylogeny Serratia marcescens Enzyme Assays Chitosan Molecular mass biology Chemistry Chitinases Temperature Methyltransferases Hydrogen-Ion Concentration biology.organism_classification Enzyme assay carbohydrates (lipids) Molecular Weight 030104 developmental biology Infectious Diseases Biochemistry Chitinase biology.protein |
| Zdroj: | Microbial pathogenesis. 113 |
| ISSN: | 1096-1208 |
| Popis: | Serratia marcescens PRNK-1, which has strong chitinolytic activity, was isolated from cockroaches (Periplaneta americana L.). The chitinase from S. marcescens PRNK-1 was characterized after incubation in a 0.5% colloidal chitin medium at 30 °C for 3 days. The molecular weights of three bands after staining for chitinase activity were approximately 34, 41, and 48 kDa on an SDS-PAGE gel. S. marcescens PRNK-1 strain strongly inhibited hyphal growth of Rhizoctonia solani and Fusarium oxysporum. Thin-layer chromatography (TLC) and high performance liquid chromatograph (HPLC) analyses were conducted to investigate the degradation patterns of N-acetyl-chitooligosaccharides by PRNK-1 chitinase. The N-acetyl-chitooligosaccharides: N-acetyl-chitin dimer (GlcNAc)2, N-acetyl-chitin trimer (GlcNAc)3, and N-acetyl-chitin tetramer (GlcNAc)4 were degraded to (GlcNAc)1-3 on a TLC plate. In an additional experiment, (GlcNAc)6 was degraded to (GlcNAc)1-4 on a TLC plate. The optimal temperature for chitinase activity of the PRNK-1 was 50 °C, producing 32.8 units/mL. As seen via TLC, the highest degradation of (GlcNAc)4 by PRNK-1 chitinase occurred with 50 °C incubation. The optimal pH for chitinase activity of PRNK-1 was pH 5.5, producing 24.6 units/mL. As seen via TLC, the highest degradation of (GlcNAc)4 by PRNK-1 chitinase occurred at pH 5.0–6.0. These results indicate that chitinase produced from S. marcescens PRNK-1 strain showed strong antifungal activity and potential of production of N-acetyl-chitooligosaccharides. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect