陕西科技大学学报(自然科学版)
陝西科技大學學報(自然科學版)
협서과기대학학보(자연과학판)
JOURNAL OF SHAANXI UNIVERSITY OF SCIENCE & TECHNOLOGY
2014年
6期
33-38,60
,共7页
朱超%解井坤%花莉%杨冰%沈烁
硃超%解井坤%花莉%楊冰%瀋爍
주초%해정곤%화리%양빙%침삭
偶氮还原酶%三级结构%Bacillus%热稳定性%脱色
偶氮還原酶%三級結構%Bacillus%熱穩定性%脫色
우담환원매%삼급결구%Bacillus%열은정성%탈색
azoreductase%three-dimensional structure%bacillus%thermostability%decolora-tion
位于细菌膜上和胞内的偶氮还原酶可将电子传递给偶氮染料实现其脱色降解,特别是具备热稳定性的偶氮还原酶,在印染废水处理和硝基类芳香化合物污染治理等方面极具应用价值.但是,相关热稳定性偶氮还原酶结构和热稳定性等的研究数据仍然还很有限.Bacillus sp .产偶氮还原酶可在40℃~60℃下依旧保持活性,对其结构和活性关系的深入了解将有助于可应用于极端生产环境的工程化偶氮还原酶的开发.本研究利用同源建模构建了 Bacillus thuringiensis的偶氮还原酶STA的三级结构模型,并和其它黄素依赖型偶氮还原酶结构进行了比对.结果显示,STA单体具有类似黄素氧化还原蛋白的α/β型结构的亲水性蛋白质,还具有一个外‐内螺旋结构的跨膜区域.同时,通过对一株嗜热芽孢杆菌偶氮还原酶粗提液进行变性和脱色试验验证,并结合结构模型分析,推测出多数 Bacillus sp .产偶氮还原酶的热稳定性源于其蛋白质结构中的氢键及疏水相互作用.本研究结果为高温下偶氮还原酶活性的改进提供了理论基础.
位于細菌膜上和胞內的偶氮還原酶可將電子傳遞給偶氮染料實現其脫色降解,特彆是具備熱穩定性的偶氮還原酶,在印染廢水處理和硝基類芳香化閤物汙染治理等方麵極具應用價值.但是,相關熱穩定性偶氮還原酶結構和熱穩定性等的研究數據仍然還很有限.Bacillus sp .產偶氮還原酶可在40℃~60℃下依舊保持活性,對其結構和活性關繫的深入瞭解將有助于可應用于極耑生產環境的工程化偶氮還原酶的開髮.本研究利用同源建模構建瞭 Bacillus thuringiensis的偶氮還原酶STA的三級結構模型,併和其它黃素依賴型偶氮還原酶結構進行瞭比對.結果顯示,STA單體具有類似黃素氧化還原蛋白的α/β型結構的親水性蛋白質,還具有一箇外‐內螺鏇結構的跨膜區域.同時,通過對一株嗜熱芽孢桿菌偶氮還原酶粗提液進行變性和脫色試驗驗證,併結閤結構模型分析,推測齣多數 Bacillus sp .產偶氮還原酶的熱穩定性源于其蛋白質結構中的氫鍵及疏水相互作用.本研究結果為高溫下偶氮還原酶活性的改進提供瞭理論基礎.
위우세균막상화포내적우담환원매가장전자전체급우담염료실현기탈색강해,특별시구비열은정성적우담환원매,재인염폐수처리화초기류방향화합물오염치리등방면겁구응용개치.단시,상관열은정성우담환원매결구화열은정성등적연구수거잉연환흔유한.Bacillus sp .산우담환원매가재40℃~60℃하의구보지활성,대기결구화활성관계적심입료해장유조우가응용우겁단생산배경적공정화우담환원매적개발.본연구이용동원건모구건료 Bacillus thuringiensis적우담환원매STA적삼급결구모형,병화기타황소의뢰형우담환원매결구진행료비대.결과현시,STA단체구유유사황소양화환원단백적α/β형결구적친수성단백질,환구유일개외‐내라선결구적과막구역.동시,통과대일주기열아포간균우담환원매조제액진행변성화탈색시험험증,병결합결구모형분석,추측출다수 Bacillus sp .산우담환원매적열은정성원우기단백질결구중적경건급소수상호작용.본연구결과위고온하우담환원매활성적개진제공료이론기출.
Azo dyes pose serious threat to public health because of its toxicity and carcinoge‐nicity .Azoreductase locating on membrane and inside bacterial is capable of decolouring and degrading azodyes released by industrial effluents ,especially the ones with thermostability which are promising in the treatment of printing and dying wastewater and the nitro aromatic compound pollution control .But the data available on the structure and thermoactive azore‐ductase enzyme and its degradation pathway are still very less .We constructed the three‐di‐mensional structure model of STA using homology modeling method .Model analysis ,evalua‐tion and the comparisons with the structures of other bacteria‐oriented FMN independent azoreductases showed that STA was a hydrophilic proteins with typical α/βstructure and a helix transmembrane zone .The denaturation and decoloration experiments conducted with the raw azoreductase from a thermoactive strain of Bacillus confirms the conclusion draw n in silicon study that the thermostability of this azoreductase depends on its hydrophobic interac‐tion and hydrogen bond .These results will pave way for further increase in azoreductase ac‐tivity under the high temperature and for better utilization of this dye degradation mecha‐nism .