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Antifungal characterizations of a novel endo-ß-1,6-glucanase from Flavobacterium sp. NAU1659.
Xie, TingTing; Shen, Jiming; Geng, Zhitao; Wu, Fan; Dong, Yiwei; Cui, Zhongli; Liang, Yongheng; Ye, Xianfeng.
Afiliación
  • Xie T; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Shen J; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Geng Z; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Wu F; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Dong Y; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Cui Z; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Liang Y; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China.
  • Ye X; Key Laboratory of Agricultural Environmental Microbiology of Ministry of Agriculture and Rural Affairs, Nanjing Agricultural University, No.1 Weigang, Nanjing, 210095, China. yxf@njau.edu.cn.
Appl Microbiol Biotechnol ; 108(1): 437, 2024 Aug 12.
Article en En | MEDLINE | ID: mdl-39133429
ABSTRACT
ß-1,6-Glucan plays a crucial role in fungal cell walls by linking the outer layer of mannoproteins and the inner layer of ß-1,3-glucan, contributing significantly to the maintenance of cell wall rigidity. Therefore, the hydrolysis of ß-1,6-glucan by ß-1,6-glucanase directly leads to the disintegration of the fungal cell wall. Here, a novel ß-1,6-glucanase FlGlu30 was identified from the endophytic Flavobacterium sp. NAU1659 and heterologously expressed in Escherichia coli BL21 (DE3). The optimal reaction conditions of purified FlGlu30 were 50℃ and pH 6.0, resulting in a specific activity of 173.1 U/mg using pustulan as the substrate. The hydrolyzed products of FlGlu30 to pustulan were mainly gentianose within 1 h of reaction. With the extension of reaction time, gentianose was gradually hydrolyzed to glucose, indicating that FlGlu30 is an endo-ß-1,6-glucanase. The germination of Magnaporthe oryzae Guy11 spores could not be inhibited by FlGlu30, but the appressorium formation of spores was completely inhibited under the concentration of 250.0 U/mL FlGlu30. The disruptions of cell wall and accumulation of intracellular reactive oxide species (ROS) were observed in FlGlu30-treated M. oryzae Guy11 cells, suggesting the significant importance of ß-1,6-glucan as a potential antifungal target and the potential application of FlGlu30. KEY POINTS • ß-1,6-Glucan is a key component maintaining the rigid structure of fungal cell wall. • ß-1,6-Glucanase is an antifungal protein with significant potential applications. • FlGlu30 is the first reported ß-1, 6-glucanase derived from Flavobacterium.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Flavobacterium / Pared Celular / Escherichia coli / Glicósido Hidrolasas / Antifúngicos Idioma: En Revista: Appl Microbiol Biotechnol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Alemania
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Flavobacterium / Pared Celular / Escherichia coli / Glicósido Hidrolasas / Antifúngicos Idioma: En Revista: Appl Microbiol Biotechnol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Alemania