An Antifungal Chitosanase from SH21

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2021 Apr 3

PMID 33806149

Citations 6

Authors

Yuanxiang Pang

Jianjun Yang

Xinyue Chen

Yu Jia

Tong Li

Junhua Jin

Hui Liu

Linshu Jiang

Yanling Hao

Hongxing Zhang

Yuanhong Xie

Affiliations

Soon will be listed here.

Abstract

SH21 was observed to produce an antifungal protein that inhibited the growth of . To purify this protein, ammonium sulfate precipitation, gel filtration chromatography, and ion-exchange chromatography were used. The purity of the purified product was 91.33% according to high-performance liquid chromatography results. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis revealed that the molecular weight of the protein is 30.72 kDa. The results of the LC-MS/MS analysis and a subsequent sequence-database search indicated that this protein was a chitosanase, and thus, we named it chitosanase SH21. Scanning and transmission electron microscopy revealed that chitosanase SH21 appeared to inhibit the growth of by causing hyphal ablation, distortion, or abnormalities, and cell-wall depression. The minimum inhibitory concentration of chitosanase SH21 against was 68 µg/mL. Subsequently, the corresponding gene was cloned and sequenced, and sequence analysis indicated an open reading frame of 831 bp. The predicted secondary structure indicated that chitosanase SH21 has a typical a-helix from the glycoside hydrolase (GH) 46 family. The tertiary structure shared 40% similarity with that of N174. This study provides a theoretical basis for a topical cream against fungal infections in agriculture and a selection marker on fungi.

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