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Search Results: 1 - 10 of 130531 matches for " LI Duo-Chuan "
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Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential
Duo-Chuan Li,An-Na Li,Anastassios C. Papageorgiou
Enzyme Research , 2011, DOI: 10.4061/2011/308730
Abstract: Thermophilic fungal cellulases are promising enzymes in protein engineering efforts aimed at optimizing industrial processes, such as biomass degradation and biofuel production. The cloning and expression in recent years of new cellulase genes from thermophilic fungi have led to a better understanding of cellulose degradation in these species. Moreover, crystal structures of thermophilic fungal cellulases are now available, providing insights into their function and stability. The present paper is focused on recent progress in cloning, expression, regulation, and structure of thermophilic fungal cellulases and the current research efforts to improve their properties for better use in biotechnological applications. 1. Introduction Cellulose is one of the main components of plant cell wall material and is the most abundant and renewable nonfossil carbon source on Earth. Degradation of cellulose to its constituent monosaccharides has attracted considerable attention for the production of food and biofuels [1, 2]. The degradation of cellulose to glucose is achieved by the cooperative action of endocellulases (EC 3.1.1.4), exocellulases (cellobiohydrolases, CBH, EC 3.2.1.91; glucanohydrolases, EC 3.2.1.74), and beta-glucosidases (EC 3.2.1.21). Endocellulases hydrolyze internal glycosidic linkages in a random fashion, which results in a rapid decrease in polymer length and a gradual increase in the reducing sugar concentration. Exocellulases hydrolyze cellulose chains by removing mainly cellobiose either from the reducing or the non-reducing ends, which leads to a rapid release of reducing sugars but little change in polymer length. Endocellulases and exocellulases act synergistically on cellulose to produce cellooligosaccharides and cellobiose, which are then cleaved by beta-glucosidase to glucose [3]. Thermophilic fungi are species that grow at a maximum temperature of 50°C or above, and a minimum of 20°C or above [4]. Based on their habitat, thermophilic fungi have received significant attention in recent years as a source of new thermostable enzymes for use in many biotechnological applications, including biomass degradation. Thermophilic cellulases are key enzymes for efficient biomass degradation. Their importance stems from the fact that cellulose swells at higher temperatures, thereby becoming easier to break down. A number of thermophilic fungi have been isolated in recent years and the cellulases produced by these eukaryotic microorganisms have been purified and characterized at both structural and functional level. This review aims at presenting
Three new records of thermophilic fungi in China
中国嗜热真菌三个新记录种

ZHAO Chun-Qing,LI Duo-Chuan,
赵春青
,李多川

微生物学报 , 2007,
Abstract:
A review of taxanomic research on thermophilic fungi
嗜热真菌的分类研究概况

ZHAO Chun-Qing,LI Duo-Chuan,
赵春青
,李多川

微生物学报 , 2007,
Abstract:
Three new records of thermophilic fungi in China
中国嗜热真菌三个新记录种

ZHAO Chun-Qing,LI Duo-Chuan,
赵春青
,李多川

菌物学报 , 2007,
Abstract: 透明嗜热腐殖霉菌 图1,2 Humicola hyalothermophila Moubasher,Mazen & Abdel-Hafez,Transactions of the British Mycological Society,72:509,1979.Fig.1,2 在不同温度的PDA培养基上培养5d,19℃下无生长现象;45℃生长迅速;50℃生长较为缓慢。
A review of taxanomic research on thermophilic fungi
嗜热真菌的分类研究概况

ZHAO Chun-Qing,LI Duo-Chuan,
赵春青
,李多川

菌物学报 , 2007,
Abstract: 1嗜热真菌的概念作为环境中基本的、限制性的物理因素之一,温度对生物在地球表面的生存及分布起着非常重要的、甚至是决定性的作用。真菌象其它微生物种群一样,在其数千万年的进化历程中,对不同的温度范围有
FOUR SPECIES OF THERMOPHILIC FUNGI NEWLY REPORTED FROM CHINA
四个嗜热真菌中国新记录种

WANG Dong-Mei,LI Duo-Chuan?,
王冬梅
,李多川

菌物学报 , 2005,
Abstract: 报道四个嗜热真菌中国新记录种:嗜热子囊菌光孢变种Thermoascus aurantiacus var.levisporus;埃默森篮状菌Talaromyces emersonii;杜邦青霉Penicillium dupontii及丝衣霉状拟青霉Paecilomyces byssochlamydioides,对其进行了描述和讨论。研究标本保存在山东农业大学植物病理学标本室(HSAUP)。
Three new records of thermotolerant fungi from China
中国耐热真菌三个新记录种

ZHANG Yong,LI Duo-Chuan,
张勇
,李多川

菌物学报 , 2011,
Abstract: 报道3个耐热真菌中国新记录种,瘤突毛壳Chaetomium strumarium,耐热梭孢壳Thielavia subthermophila,榛色钩囊菌Hamigera avellanea。根据所采集的标本和菌种对这些种进行了描述和讨论。研究标本保存在山东农业大学植物病理学标本室(HSAUP)。
Five new records of thermotolerant fungi from China
耐热真菌五个中国新记录种

ZHANG Yong,LI Duo-Chuan,
张勇
,李多川

菌物学报 , 2013,
Abstract: 通过形态特征观察、rDNA-ITS序列测定及分析,报道5个耐热真菌中国新记录种,即加纳木霉Trichoderma ghanense,芬尼新萨托菌Neosartorya fennelliae,草莓状炭团菌Hypoxylon fragiforme,焦特普尔毛壳Chaetomium jodhpurense,黄色毛壳Chaetomium luteum。根据所采集的标本和菌种对这些种进行了描述和讨论。研究标本保存在山东农业大学植物病理学标本室(HSAUP)。
Purification and properties of a thermostable chitinase from thermophilic fungus Thermomyces lanuginosus
疏绵状嗜热丝孢菌热稳定几丁质酶的纯化及其性质研究

GUO Run-fang,LI Duo-chuan,WANG Rong,
郭润芳
,李多川,王荣

微生物学报 , 2005,
Abstract: A thermostable extracellular chitinase from culture supernatant of a thermophilic fungus Thermomyces lanuginosus was purified to SDS-PAGE homogeneity, by using ammonium sulfate fraction, DEAE-Sepharose Fast flow chromatography, Phenyl-Sepharose Fast Flow chromatography. A molecular mass of the purified enzyme was between 48-49.8 kD determined by SDS-PAGE and gel filtration chromatography. The chitinase exhibited optimum catalytic activity at pH 4.5 and 55 degrees C respectively. It was thermostable at 50 degrees C and retained 24% activity after 20 min at 70 degrees C. The half life time of the enzyme at 65 degrees C was 25 min. Different metal ions showed different effects on the chitinase activity. Ca2+, Ba2+, Na+, K+ enhanced the enzyme activity, whereas Fe2+, Ag+, Hg2+, Cu2+ caused obvious inhibition. The Km and Vmax values of chitinase on colloidal chitin were 9.56 mg/mL and 22.12 micromol/min respectively. The chitinase showed antifungal activity aginst tested fungi to different degree.
Purification and properties of β-glucosidase from Chaetomium thermophilum
嗜热毛壳菌一种β-葡萄糖苷酶的分离纯化及特性

TENG Fang-Chao,LI Duo-Chuan,LI Ya-Ling,LI Zhe-Jiang,
滕芳超
,李多川,李亚玲,李浙江

菌物学报 , 2006,
Abstract: 研究了嗜热毛壳菌Chaetomiumthermophilum液体发酵产生的一种胞外β-葡萄糖苷酶的分离纯化及特性。粗酶液经硫酸铵沉淀、DEAE-SepharoseFastFlow阴离子层析、Phenyl-Sepharose疏水层析、SephacrylS-100分子筛层析等步骤后获得凝胶电泳均一的β-葡萄糖苷酶。经10%SDS-PAGE和凝胶过滤层析方法分别测得该酶的分子量大小约为118.0kDa和120.1kDa。该酶反应的最适温度为70℃,最适pH值为4.0~5.0。有高的热稳定性,在60℃保温1小时酶活性不丧失,在70℃时的半衰期为16min,在90℃保温10min仍具有7.6%的活性。且能在pH4.0~11.0之间保持稳定。金属离子对β-葡萄糖苷酶的活性影响较大,其中Ca2 、Ba2 对酶有激活作用,而Zn2 、Cu2 、Al3 、Ag 、Hg2 对酶有显著的抑制作用。
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