Antifungal characterizations of a novel endo-β-1,6-glucanase from Flavobacterium sp. NAU1659

• DOI: 10.1007/s00253-024-13269-1
• Publication Date: 2024-08-12T10:02:55Z
• Authors: TingTing Xie; Jiming Shen; Zhitao Geng; Fan Wu; Yiwei Dong; Zhongli Cui; Yongheng Liang; Xianfeng Ye
• Keywords: Glucanase

Abstract β-1,6-Glucan plays a crucial role in fungal cell walls by linking the outer layer of mannoproteins and inner β-1,3-glucan, contributing significantly to maintenance wall rigidity. Therefore, hydrolysis β-1,6-glucan β-1,6-glucanase directly leads disintegration wall. Here, novel Fl Glu30 was identified from endophytic Flavobacterium sp. NAU1659 heterologously expressed Escherichia coli BL21 (DE3). The optimal reaction conditions purified were 50℃ pH 6.0, resulting specific activity 173.1 U/mg using pustulan as substrate. hydrolyzed products mainly gentianose within 1 h reaction. With extension time, gradually glucose, indicating that is an endo-β-1,6-glucanase. germination Magnaporthe oryzae Guy11 spores could not be inhibited Glu30, but appressorium formation completely under concentration 250.0 U/mL Glu30. disruptions accumulation intracellular reactive oxide species (ROS) observed Glu30-treated M. cells, suggesting significant importance potential antifungal target application Key points • key component maintaining rigid structure β-1,6-Glucanase protein with applications. FlGlu30 first reported β-1, 6-glucanase derived Flavobacterium.