• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

几种嗜热真菌中苹果酸脱氢酶的温度稳定性比较特性

Comparative temperature-stability properties of malate dehydrogenases from some thermophilic fungi.

作者信息

Wali A S, Mattoo A K, Modi V V

出版信息

Int J Pept Protein Res. 1979 Aug;14(2):99-106. doi: 10.1111/j.1399-3011.1979.tb01732.x.

DOI:10.1111/j.1399-3011.1979.tb01732.x
PMID:489257
Abstract

Temperature-activity and temperature-stability relationships of malate dehydrogenases from eight thermophilic fungi were determined. Temperature optima for maximum activity of the enzymes varied between 50 degrees and 60 degrees and the Arrhenius plots were linear between 5 degrees and 50 degrees. The energies of activation ranged from 2.1 Kcal/mol for the enzyme from Sporotrichum thermophile to 9.1 Kcal/mol for that from Penicillium duponti. Heat inactivation kinetics at 50 degrees revealed heat lability of the enzyme from most of the thermophilic fungi. The t1/2's (min) were less than 10 for the enzymes from P. duponti, S. thermophile and Thermoascus aurantiacus; less than 30 for those from Chaetomium thermophile var. coprophile, H. lanuginosa and C. thermophile var. dissitum; and greater than 30 for those from Mucor pusillus and H. insolens. Salts of Na+, K+ and NH4+, and citrate protected the enzymes from H. lanuginosa, C. thermophile var. dissitum and M. pusillus against heat inactivation.

摘要

测定了来自8种嗜热真菌的苹果酸脱氢酶的温度-活性和温度-稳定性关系。这些酶最大活性的最适温度在50℃至60℃之间变化,并且在5℃至50℃之间阿累尼乌斯曲线呈线性。活化能范围从嗜热枝孢霉的酶的2.1千卡/摩尔到杜邦青霉的酶的9.1千卡/摩尔。50℃下的热失活动力学表明大多数嗜热真菌的酶对热不稳定。杜邦青霉、嗜热枝孢霉和橘黄嗜热毁丝霉的酶的t1/2(分钟)小于10;嗜热毛壳粪生变种、绒毛栓菌和嗜热毛壳不同变种的酶的t1/2小于30;微小毛霉和不溶性栓菌的酶的t1/2大于30。Na+、K+和NH4+的盐以及柠檬酸盐可保护绒毛栓菌、嗜热毛壳不同变种和微小毛霉的酶免受热失活。

相似文献

1
Comparative temperature-stability properties of malate dehydrogenases from some thermophilic fungi.几种嗜热真菌中苹果酸脱氢酶的温度稳定性比较特性
Int J Pept Protein Res. 1979 Aug;14(2):99-106. doi: 10.1111/j.1399-3011.1979.tb01732.x.
2
Studies on thermophilic cellulolytic fungi.嗜热纤维素分解真菌的研究。
Appl Microbiol. 1975 Aug;30(2):276-81. doi: 10.1128/am.30.2.276-281.1975.
3
Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile).产黄青霉(嗜温菌)和杜邦青霉(嗜热菌)中硫酸盐激活酶的比较稳定性、催化特性及化学性质
J Bacteriol. 1985 Nov;164(2):674-83. doi: 10.1128/jb.164.2.674-683.1985.
4
Purification and properties of Penicillium glucose 6-phosphate dehydrogenase.青霉葡萄糖-6-磷酸脱氢酶的纯化及性质
Biochem J. 1972 Jul;128(4):817-31. doi: 10.1042/bj1280817.
5
Purification and properties of malate dehydrogenase from the extreme thermophile Bacillus caldolyticus.嗜热栖热芽孢杆菌苹果酸脱氢酶的纯化及性质
Orig Life. 1980 Jun;10(2):185-92. doi: 10.1007/BF00928668.
6
Stimulation of growth and glucose catabolite enzymes by succinate in some thermophilic fungi.
Arch Microbiol. 1978 Jul;118(1):49-53. doi: 10.1007/BF00406073.
7
The beta-glucosidase system of the thermophilic fungus Chaetomium thermophile var. coprophile n. var.
Biochim Biophys Acta. 1973 Nov 2;329(1):5-16. doi: 10.1016/0304-4165(73)90003-2.
8
Thermophilic mycoflora of cigarettes and cured tobacco leaves.香烟和烤烟叶片中的嗜热真菌区系
Mycopathologia. 1980 May 1;71(1):9-16. doi: 10.1007/BF00625306.
9
Properties and function of malate enzyme from Pseudomonas putida.恶臭假单胞菌苹果酸酶的性质与功能
Biochimie. 1983 Nov-Dec;65(11-12):629-35. doi: 10.1016/s0300-9084(84)80026-7.
10
Incidence and detection of thermotolerant and thermophilic fungi from maize with particular reference to Thermoascus species.玉米中耐热和嗜热真菌的发生率及检测,特别提及嗜热ascus菌属。
Int J Food Microbiol. 1997 Apr 1;35(2):137-45. doi: 10.1016/s0168-1605(96)01212-3.

引用本文的文献

1
Thermophilic fungi: their physiology and enzymes.嗜热真菌:它们的生理学与酶
Microbiol Mol Biol Rev. 2000 Sep;64(3):461-88. doi: 10.1128/MMBR.64.3.461-488.2000.