Cloning and characterization of a thermostable and pH-stable cellobiohydrolase from Neocallimastix patriciarum J11

2013 ◽  
Vol 90 (2) ◽  
pp. 153-159 ◽  
Author(s):  
Hui-Chang Wang ◽  
Yo-Chia Chen ◽  
Ching-Tsan Huang ◽  
Ruey-Shyang Hseu
Keyword(s):  
Neocallimastix Patriciarum

Isolation and characterization of cellulolytic anaerobic fungi and associated mycoplasmas from the rumen of a steer fed a roughage diet

1990 ◽  
Vol 36 (7) ◽  
pp. 513-517 ◽  
Author(s):  
H. Kudo ◽  
K. D. Jakober ◽  
R. C. Phillippe ◽  
K.-J. Cheng ◽  
D. J. S. Barr ◽  
...  
Keyword(s):  
Key Words ◽  
New Genus ◽  
Anaerobic Fungi ◽  
Ecological Role ◽  
New Genus And Species ◽  
Fermentation Products ◽  
Isolation And Characterization ◽  
Neocallimastix Patriciarum

The isolation of 12 strains of cellulolytic fungi from the rumen of a roughage-fed steer is described. These represented three different genera, including one new genus and species (Orpinomyces bovis). The organisms were indistinguishable on the basis of fermentation products from cellulose, and their fermentation patterns were very similar to those of rumen fungi isolated in other countries. Mycoplasmas were found to be associated with 7 of the 12 isolates. The ecological role of the association of the mycoplasmas with rumen fungi is still unknown. Key words: Orpinomyces bovis, Piromyces communis, Neocallimastix patriciarum.

Characterization of aNeocallimastixpatriciarumxylanase gene and its product

1999 ◽  
Vol 45 (11) ◽  
pp. 970-974 ◽  
Author(s):  
Jin-Hao Liu ◽  
Brent L Selinger ◽  
Cheng-Fang Tsai ◽  
Kuo-Jaon Cheng
Keyword(s):  
Catalytic Domain ◽  
Xylanase Activity ◽  
Binding Domain ◽  
Glycosyl Hydrolases ◽  
Cellulose Binding Domain ◽  
Xylanase Gene ◽  
Neocallimastix Patriciarum ◽  
Cellulose Binding ◽  
Linker Domain

A xylanase gene (xynC) isolated from the anaerobic ruminal fungus Neocallimastix patriciarum was characterized. The gene consists of an N-terminal catalytic domain that exhibited homology to family 11 of glycosyl hydrolases, a C-terminal cellulose binding domain (CBD) and a putative dockerin domain in between. Each domain was linked by a short linker domain rich in proline and alanine. Deletion analysis demonstrated that the CBD was essential for optimal xylanase activity of the enzyme, while the putative dockerin domain may not be required for enzyme function.Key words: xylanase, cellulose binding domain, Neocallimastix patriciarum.

Expression of Xylanase Gene from Pyromyces finnis in Pichia pastoris and Characterization of Recombinant Protein

2019 ◽  
Vol 35 (4) ◽  
pp. 24-32 ◽  
Author(s):  
L.N. Borschevskaya ◽  
T.L. Gordeeva ◽  
S.P. Sineoky
Keyword(s):  
Pichia Pastoris ◽  
Specific Activity ◽  
Ministry Of Education ◽  
Kurchatov Institute ◽  
Putative Signal Peptide ◽  
Neocallimastix Patriciarum ◽  
Optimum Ph ◽  
Sequence Encoding ◽  
Positive Effect

The heterologous expression and characteristics of a new xylanase from Pyromyces finnis have been described. The endo-l,4-β-xylanase XylP (EC 3.2.1.8) consists of 223 amino acids and 19 residues of a putative signal peptide in the N-terminal region. The amino acid sequence of the mature protein has the greatest homology with the sequence of the native catalytic N-terminal domain of Neocallimastix patriciarum endo-l,4-β-xylanase (84%). A synthetic nucleotide sequence encoding a mature XylP protein was expressed in Pichia pastoris. The purified recombinant enzyme showed activity with birch xylan and arabinoxylan. When using birch xylan as a substrate, the optimum pH for the enzyme was 5.0, and the optimum temperature was 50 °C. The specific activity of the xylanase was 4700 U/mg protein, and Km and Vmax were equal to 0.51 mg/mL and 7395.3 umol/(min∙mg), respectively. The recombinant XylP protein showed moderate thermal stability and high pH stability, resistance to digestive enzymes and protein inhibitors of grain xylanases. It was also shown that the Mg2+, Co2+ and Li+ ions have a positive effect on the enzyme activity. xylanase, xylan, feed enzyme, Pichia pastoris, Pyromyces finnis The work was performed with the financial support of the Ministry of Education and Science of Russia (Unique Project Identifier RFMEFI60717X0180) using the Unique Scientific Installation -National Bioresource Center «All-Russian Collection of Industrial Microorganisms», NRC «Kurchatov Institute» - GOSNIIGENETIKA

scholarly journals Functional characterization of cellulases identified from the cow rumen fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic analyses

2011 ◽  
Vol 4 (1) ◽  
pp. 24 ◽  
Author(s):  
Tzi-Yuan Wang ◽  
Hsin-Liang Chen ◽  
Mei-Yeh J Lu ◽  
Yo-Chia Chen ◽  
Huang-Mo Sung ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Neocallimastix Patriciarum ◽  
Rumen Fungus

scholarly journals Molecular cloning and characterization of a bifunctional xylanolytic enzyme from Neocallimastix patriciarum

2009 ◽  
Vol 85 (5) ◽  
pp. 1451-1462 ◽  
Author(s):  
Cheng-Kang Pai ◽  
Zong-Yuan Wu ◽  
Ming-Ju Chen ◽  
Yi-Fang Zeng ◽  
Jr-Wei Chen ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Neocallimastix Patriciarum ◽  
Xylanolytic Enzyme

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

AEM analysis of crystallization in Ti-based amorphous alloys

1983 ◽  
Vol 41 ◽  
pp. 270-271
Author(s):  
A.R. Pelton ◽  
A.F. Marshall ◽  
Y.S. Lee
Keyword(s):  
Magnetic Properties ◽  
Amorphous Alloys ◽  
Amorphous Materials ◽  
Isothermal Annealing ◽  
Amorphous Matrix ◽  
Nucleation And Growth ◽  
Current Interest ◽  
Amorphous Films ◽  
Electrical And Magnetic Properties

Amorphous materials are of current interest due to their desirable mechanical, electrical and magnetic properties. Furthermore, crystallizing amorphous alloys provides an avenue for discerning sequential and competitive phases thus allowing access to otherwise inaccessible crystalline structures. Previous studies have shown the benefits of using AEM to determine crystal structures and compositions of partially crystallized alloys. The present paper will discuss the AEM characterization of crystallized Cu-Ti and Ni-Ti amorphous films.Cu60Ti40: The amorphous alloy Cu60Ti40, when continuously heated, forms a simple intermediate, macrocrystalline phase which then transforms to the ordered, equilibrium Cu3Ti2 phase. However, contrary to what one would expect from kinetic considerations, isothermal annealing below the isochronal crystallization temperature results in direct nucleation and growth of Cu3Ti2 from the amorphous matrix.

Characterization of Coherent, Ordered Precipitates in Nickel-Base Alloys

1973 ◽  
Vol 31 ◽  
pp. 144-145
Author(s):  
B. H. Kear ◽  
J. M. Oblak
Keyword(s):  
Stable Phase ◽  
Nickel Base Superalloy ◽  
Alloy 718 ◽  
Commercial Alloy ◽  
Precipitate Morphology ◽  
Continuous Precipitation ◽  
Nickel Base ◽  
Base Superalloy ◽  
Strengthening Precipitate

A nickel-base superalloy is essentially a Ni/Cr solid solution hardened by additions of Al (Ti, Nb, etc.) to precipitate a coherent, ordered phase. In most commercial alloy systems, e.g. B-1900, IN-100 and Mar-M200, the stable precipitate is Ni3 (Al,Ti) γ′, with an LI2structure. In A lloy 901 the normal precipitate is metastable Nis Ti3 γ′ ; the stable phase is a hexagonal Do2 4 structure. In Alloy 718 the strengthening precipitate is metastable γ″, which has a body-centered tetragonal D022 structure.Precipitate MorphologyIn most systems the ordered γ′ phase forms by a continuous precipitation re-action, which gives rise to a uniform intragranular dispersion of precipitate particles. For zero γ/γ′ misfit, the γ′ precipitates assume a spheroidal.

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