Jeong Woo Soo, Seo Dong Ho, Jung Jong Hyun, Jung Dong Hyun, Lee Dong-Woo, Park Young-Seo, Park Cheonseok
Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University, Yongin 17104, Republic of Korea.
Korea Food Research Institute, Seongnam 13539, Republic of Korea.
J Microbiol Biotechnol. 2017 Feb 28;27(2):271-276. doi: 10.4014/jmb.1609.09022.
A highly thermostable β-(1-4)-glucanase (NA23_08975) gene () from AW-1, a native-feather degrading thermophilic eubacterium, was cloned and expressed in . The recombinant FiG (rFiG) protein showed strong activity toward β--glucan from barley (367.0 IU/mg), galactomannan (174.0 IU/mg), and 4-nitrophenyl-cellobioside (66.1 IU/mg), but relatively weak activity was observed with hydroxyethyl cellulose (5.3 IU/mg), carboxymethyl cellulose (2.4 IU/mg), and xylan from oat spelt (1.4 IU/mg). rFiG exhibited optimal activity at 90°C and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at 85°C. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.
从嗜热羽毛降解真细菌AW-1中克隆出一个高度耐热的β-(1-4)-葡聚糖酶(NA23_08975)基因，并在[具体表达宿主未给出]中表达。重组FiG(rFiG)蛋白对大麦β-葡聚糖(367.0 IU/mg)、半乳甘露聚糖(174.0 IU/mg)和4-硝基苯基纤维二糖苷(66.1 IU/mg)表现出较强活性，但对羟乙基纤维素(5.3 IU/mg)、羧甲基纤维素(2.4 IU/mg)和燕麦麸木聚糖(1.4 IU/mg)的活性相对较弱。rFiG在90°C和pH 5.0时表现出最佳活性。此外，该酶具有极高的热稳定性，在85°C下的半衰期为113小时。这些结果表明，rFiG可用于水解纤维素和半纤维素生物质底物以生产生物燃料。
