Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries

FEBS Journal ◽  
2015 ◽  
Vol 282 (15) ◽  
pp. 2879-2894 ◽  
Author(s):  
Erica Elisa Ferrandi ◽  
Christopher Sayer ◽  
Michail N. Isupov ◽  
Celeste Annovazzi ◽  
Carlotta Marchesi ◽  
...  
Keyword(s):  
Hot Spring ◽  
Epoxide Hydrolases ◽  
Metagenomic Libraries

scholarly journals Biochemical and Structural Characterization of Two Cif-Like Epoxide Hydrolases from Burkholderia cenocepacia

2021 ◽  
Author(s):  
Noor M. Taher ◽  
Kelli L. Hvorecny ◽  
Cassandra M. Burke ◽  
Morgan S.A. Gilman ◽  
Gary E. Heussler ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Burkholderia Cenocepacia ◽  
Epoxide Hydrolases

scholarly journals Occurrence of fatty acid epoxide hydrolases in soybean (Glycine max). Purification and characterization of the soluble form

1992 ◽  
Vol 282 (3) ◽  
pp. 711-714 ◽  
Author(s):  
E Blée ◽  
F Schuber
Keyword(s):  
Glycine Max ◽  
Gel Filtration ◽  
Soluble Form ◽  
Soluble Enzyme ◽  
Purification And Characterization ◽  
Epoxide Hydrolases ◽  
Major Activity ◽  
Apparent Homogeneity ◽  
A Minor

Epoxide hydrolases catalysing the hydration of cis-9,10-epoxystearate into threo-9,10-dihydroxystearate have been detected in soybean (Glycine max) seedlings. The major activity was found in the cytosol, a minor fraction being strongly associated with microsomes. The soluble enzyme, which was purified to apparent homogeneity by (NH4)2SO4 fractionation, hydrophobic, DEAE- and gel-filtration chromatographies, has a molecular mass of 64 kDa and a pI of 5.4.

Characterization of a thermostable manganese-containing superoxide dismutase from inshore hot spring thermophile Thermus sp. JM1

2011 ◽  
Vol 30 (6) ◽  
pp. 95-103 ◽  
Author(s):  
Yanbing Zhu ◽  
Hebin Li ◽  
Xuqin Zhang ◽  
Chunyan Zhang ◽  
Jionghua Xiang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Hot Spring

scholarly journals PRODUCTION AND CHARACTERIZATION OF CHITINASE ENZYMES FROM SULILI HOT SPRING IN SOUTH SULAWESI, Bacillus sp. HSA,3-1a

2010 ◽  
Vol 10 (2) ◽  
pp. 256-260 ◽  
Author(s):  
Hasnah Natsir ◽  
Abd. Rauf Patong ◽  
Maggy Thenawidjaja Suhartono ◽  
Ahyar Ahmad
Keyword(s):  
Hot Spring ◽  
Thermophilic Bacteria ◽  
Extracellular Enzyme ◽  
Colloidal Chitin ◽  
Bacillus Sp ◽  
Optimum Temperature ◽  
South Sulawesi ◽  
Sds Page ◽  
Physiological Analysis

Chitinase is an extracellular enzyme which is capable in hydrolyzing insoluble chitin to its oligomeric and monomeric components. The enzyme produced by thermophilic bacteria was screened and isolated from Sulili hot spring in Pinrang, South Sulawesi, Indonesia. The gram positive spore forming rod shape bacteria was identified as Bacillus sp. HSA,3-1a through morphological and physiological analysis. The production of chitinase enzyme was conducted at various concentration of colloidal chitin at a pH of 7.0 and a temperature of 55 °C. The bacteria optimally was produced the enzyme at a colloidal chitin concentration of 0.5% after 72 h of incubation. The optimum temperature, pH and substrate concentration of chitinase were 60 °C, 7.0 and 0.3%, respectively. The enzyme was stable at a pH of 7.0 and a temperature of 60 °C after 2 h of incubation. The chitinase activities was increased by addition of 1 mM Mg2+, Ca2+ and Mn2+ ions, whereas the activities were  decreased by 1 mM Co2+, Fe2+ and Zn2 ions. The molecular weight of the crude enzyme was determined using SDS-PAGE analysis. Five protein fractions were obtained from SDS-PAGE, with MWs of 79, 71, 48, 43 and 22 kDa.   Keywords: colloidal chitin, thermophilic bacteria, chitinase

scholarly journals PURIFICATION AND PARTIAL CHARACTERIZATION OF L-ASPARAGINASE ENZYME PRODUCED BY NEWLY ISOLATE BACILLUS SP.

2017 ◽  
Vol 18 (2) ◽  
pp. 1-10 ◽  
Author(s):  
Dzun Noraini Jimat ◽  
Intan Baizura Firda Mohamed ◽  
Azlin Suhaida Azmi ◽  
Parveen Jamal
Keyword(s):  
Specific Activity ◽  
Hot Spring ◽  
Gel Filtration ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Bacillus Sp ◽  
Sds Page ◽  
Fast Flow ◽  
Microbial Strain

A newly bacterial producing L-asparaginase was successful isolated from Sungai Klah Hot Spring, Perak, Malaysia and identified as Bacillus sp. It was the best L-asparaginase producer as compared to other isolates. Production of L-asparaginase from the microbial strain was carried out under liquid fermentation. The crude enzyme was then centrifuged and precipitated with ammonium sulfate before further purified with chromatographic method. The ion exchange chromatography HiTrap DEAE-Sepharose Fast Flow column followed by separation on Superose 12 gel filtration were used to obtain pure enzyme. The purified enzyme showed 10.11 U/mg of specific activity, 50.07% yield with 2.21 fold purification. The purified enzyme was found to be dimer in form, with a molecular weight of 65 kDa as estimated by SDS-PAGE. The maximum activity of the purified L-asparaginase was observed at pH 9 and temperature of 60°C.

scholarly journals Isolation and characterization of a thermophilic sulfur- and iron-reducing thaumarchaeote from a terrestrial acidic hot spring

2019 ◽  
Vol 13 (10) ◽  
pp. 2465-2474 ◽  
Author(s):  
Shingo Kato ◽  
Takashi Itoh ◽  
Masahiro Yuki ◽  
Mai Nagamori ◽  
Masafumi Ohnishi ◽  
...  
Keyword(s):  
Hot Spring ◽  
Isolation And Characterization

scholarly journals Cultivation and Genomic, Nutritional, and Lipid Biomarker Characterization of Roseiflexus Strains Closely Related to Predominant In Situ Populations Inhabiting Yellowstone Hot Spring Microbial Mats

2010 ◽  
Vol 192 (12) ◽  
pp. 3033-3042 ◽  
Author(s):  
Marcel T. J. van der Meer ◽  
Christian G. Klatt ◽  
Jason Wood ◽  
Donald A. Bryant ◽  
Mary M. Bateson ◽  
...  
Keyword(s):  
National Park ◽  
Microbial Mats ◽  
Hot Spring ◽  
Small Subunit ◽  
Small Subunit Rrna ◽  
Anoxygenic Phototrophs ◽  
Lipid Biomarker ◽  
Genes Encoding

ABSTRACT Roseiflexus sp. strains were cultivated from a microbial mat of an alkaline siliceous hot spring in Yellowstone National Park. These strains are closely related to predominant filamentous anoxygenic phototrophs found in the mat, as judged by the similarity of small-subunit rRNA, lipid distributions, and genomic and metagenomic sequences. Like a Japanese isolate, R. castenholzii, the Yellowstone isolates contain bacteriochlorophyll a, but not bacteriochlorophyll c or chlorosomes, and grow photoheterotrophically or chemoheterotrophically under dark aerobic conditions. The genome of one isolate, Roseiflexus sp. strain RS1, contains genes necessary to support these metabolisms. This genome also contains genes encoding the 3-hydroxypropionate pathway for CO2 fixation and a hydrogenase, which might enable photoautotrophic metabolism, even though neither isolate could be grown photoautotrophically with H2 or H2S as a possible electron donor. The isolates exhibit temperature, pH, and sulfide preferences typical of their habitat. Lipids produced by these isolates matched much better with mat lipids than do lipids produced by R. castenholzii or Chloroflexus isolates.

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