期刊文献+

嗜热芽孢杆菌产耐热蛋白酶稳定性的研究 被引量:4

Stability of a thermostable protease from a thermophilic Bacillus
下载PDF
导出
摘要 实验室成功地分离保存了一株产蛋白酶的耐热芽孢杆菌.该菌所产的蛋白酶最适pH 7.5,在pH4.0-9.0时较稳定.最适温度为70℃,80℃以下时热稳定性较好,在稳定的pH或温度下能保持1 h以上活性不变.通过添加Ca^2+,Li^+,Co^2+,Mg^2+等12种金属离子证实该酶为金属激活蛋白酶,其中Li+提高该酶活性最显著.氧化剂过氧化氢可以提高该酶的活力,表面活性剂如Tween 80和Triton X-100对酶活力影响不大.该蛋白酶对各种常用的商品洗涤剂耐受能力较强,在洗涤工业中具有较好的应用前景. A thermophilic Bacillus which can produce a thermostable protease was separated and preserved. The protease had a good stability between pH 4.0-9.0. Its optimum pH was pH 7.5. It was of good stability when below 80℃. The optimum temperature was 70 ℃ ; and its aetivity almost had no change in stable pH or temperature over an hour. The protease proved to be a metalloprotease by adding 12 kinds of metal ions such as Ca^2+ ,Li^+ ,Co^2+ ,Mg^2+ ; and Li^+ increased the activity of the protease most. H2O2 could reinforce the activity of the protease; and surfactants such as Tween 80 and Triton X-100 had little influence on it. The protease markedly exhibits its tolerance against a variety of detergents. Therefore it can be used as an excellent additive in industrial applications, especially in the detergent industry.
出处 《中国计量学院学报》 2009年第2期149-153,共5页 Journal of China Jiliang University
基金 浙江省自然科学基金资助项目(No.Y405083)
关键词 嗜热芽孢杆菌 耐高温蛋白酶 稳定性 thermophilic Bacillus thermostable protease stability
  • 相关文献

参考文献13

  • 1RAO M B,TANKSALE A M,GHATGE M S,et al.Molecular and biotechnological aspects of microbial protease[J].Microbiology and Molecular Biology Reviews,1998,62 (3),597-635.
  • 2汪少芸,黄景洁,常景立,袁凤英,陈桂灵,饶平凡.新型复合酶制备鳀鱼蛋白水解物的研究[J].中国食品学报,2008,8(2):123-127. 被引量:12
  • 3伍先绍,贺稚非,刘琳,龚霄.碱性蛋白酶产生菌株的筛选及其酶学性质研究进展[J].中国食品添加剂,2008,19(3):58-61. 被引量:10
  • 4HANS J,CHUNG S C.Production of an oxidant and SDSstable alkaline protease from an alkaophilic Bacillus classic 1-52 by submerged fermentation,Feasibility as a laundry detergent additive[J].Enzyme and Microbial Technology,2006.38(1-2):176-183.
  • 5SANDRO G,ASHOK P,CLARICE A O,et al,Characterization and stability of proteases from Penicillium sp.produced by solid--state fermentation[J].Enzyme and Microbial Technology,2003,32(2):246-251.
  • 6SHAHRZAD B,MARIA M A,AMARE G,etal.Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp[J].Enzyme and Microbial Technology,2003,32(5):525-531.
  • 7袁玉荪,朱婉华,陈均辉.生物化学实验[M].北京:人民教育出版社,1981:46.
  • 8MEERA V,SARAMMA A V.Characterization of alkaline protease from Vibrio fluvialis strain VM10 isolated from a mangrove sediment sample and its application as a laundry detergent additive[J].Process Biochemistry,2006,41 (6):1239-1243.
  • 9HAN S J,YOON M K,JANG W C,et al.Stabilization method of an alkaline protease from inactivation by heat,SDS and hydrogen peroxide[J].Enzyme and Microbial Technology,2005,36(5-6):766-772.
  • 10母智深,白英,赵广华,胡小松.荧光假单胞杆菌胞外蛋白酶的纯化及热稳定性[J].高等学校化学学报,2008,29(4):762-766. 被引量:8

二级参考文献60

  • 1赵新淮,冯志彪.蛋白质水解物水解度的测定[J].食品科学,1994,15(11):65-67. 被引量:525
  • 2陈静,王淑军,黄炜,牛天贵,陆兆新.产低温碱性蛋白酶海洋适冷菌SY的筛选[J].微生物学杂志,2005,25(4):38-42. 被引量:14
  • 3刘朝谊,郭凯,许峰,张键俊,王淑军.低温海洋微生物产碱性蛋白酶菌株的筛选[J].淮海工学院学报(自然科学版),2006,15(2):59-62. 被引量:5
  • 4邓祖新.SAS系统和数据分析[M].北京:电子工业出版社,2001.
  • 5[美]F.奥斯伯,R.布伦特.R.E.金斯顿..精编分子生物学实验指南[M]..北京:科学出版社,,1998..39-40..
  • 6大连轻工业学院编.食品分析[M].北京:中国轻工业出版社,1994,73-216.
  • 7Wretlind B., O.R. Pavlovskis. Genetic mapping and characterization of Pseudornonas aeruginosa mutants defective in the formation of extracellular proteins [J] . J. Bacteriol, 1984, 158: 801~808.
  • 8Fukushima, et al. Structural gen and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 Elastase [J]. Journal of Bacteriology, 1989, 171:1698-1 704.
  • 9Robert A, et al. Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gen [J] . Journal of Bacteriology, 1988, 170:4 309-4 314.
  • 10Yamamoto S., Fukushima J, Atsumi Y, et al., Cloning and characterization of elastase structural gene from Pseudomonas aerugirtosa IFO3455 [J] . Biochem. Biophys. Res., Communi., 1988, 152 (3): 1 117-1 122.

共引文献27

同被引文献58

引证文献4

二级引证文献8

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部