Biochemical Properties of Recombinant Leucine Aminopeptidase II fromBacillus stearothermophilusand Potential Applications in the Hydrolysis of Chinese Anchovy (Engraulis japonicus) Proteins

2011 ◽  
Vol 60 (1) ◽  
pp. 165-172 ◽  
Author(s):  
Fanghua Wang ◽  
Zhengxiang Ning ◽  
Dongming Lan ◽  
Yuanyuan Liu ◽  
Bo Yang ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Biochemical Properties ◽  
Engraulis Japonicus ◽  
Potential Applications ◽  
Hydrolysis Of

scholarly journals Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223

2011 ◽  
Vol 12 (11) ◽  
pp. 7609-7625 ◽  
Author(s):  
Yanfei Shen ◽  
Fanghua Wang ◽  
Dongming Lan ◽  
Yuanyuan Liu ◽  
Bo Yang ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Biochemical Properties ◽  
Bacillus Kaustophilus ◽  
Potential Applications

Quantification of small-scale heterogeneity in aquatic aminopeptidase activity

2020 ◽  
Vol 84 ◽  
pp. 127-140
Author(s):  
BM Gaas ◽  
JW Ammerman
Keyword(s):  
Chlorophyll Fluorescence ◽  
Leucine Aminopeptidase ◽  
Hudson River ◽  
Aminopeptidase Activity ◽  
Small Scale ◽  
Analysis Instrument ◽  
Sequential Samples ◽  
Degree Of Confidence ◽  
The Mean ◽  
Hydrolysis Of

Leucine aminopeptidase (LAP) is one of the enzymes involved in the hydrolysis of peptides, and is sometimes used to indicate potential nitrogen limitation in microbes. Small-scale variability has the potential to confound interpretation of underlying patterns in LAP activity in time or space. An automated flow-injection analysis instrument was used to address the small-scale variability of LAP activity within contiguous regions of the Hudson River plume (New Jersey, USA). LAP activity had a coefficient of variation (CV) of ca. 0.5 with occasional values above 1.0. The mean CVs for other biological parameters—chlorophyll fluorescence and nitrate concentration—were similar, and were much lower for salinity. LAP activity changed by an average of 35 nmol l-1 h-1 at different salinities, and variations in LAP activity were higher crossing region boundaries than within a region. Differences in LAP activity were ±100 nmol l-1 h-1 between sequential samples spaced <10 m apart. Variogram analysis indicated an inherent spatial variability of 52 nmol l-1 h-1 throughout the study area. Large changes in LAP activity were often associated with small changes in salinity and chlorophyll fluorescence, and were sensitive to the sampling frequency. This study concludes that LAP measurements in a sample could realistically be expected to range from zero to twice the average, and changes between areas or times should be at least 2-fold to have some degree of confidence that apparent patterns (or lack thereof) in activity are real.

Synthesis and biochemical properties of the novel, enzymatically stable mRNA cap analogues with versatile potential applications

2005 ◽  
Author(s):  
Marcin Kalek ◽  
Jacek Jemielity ◽  
Ewa Grudzien ◽  
Joanna Zuberek ◽  
Zbigniew M. Darzynkiewicz ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
The Novel ◽  
Potential Applications

Topotactic route to synthesis of novel hydroxylated phases: I. Trioctahedral Micas

Clay Minerals ◽  
1986 ◽  
Vol 21 (2) ◽  
pp. 125-131 ◽  
Author(s):  
S. Komarneni ◽  
R. Roy
Keyword(s):  
Ion Exchange ◽  
Alkaline Earth ◽  
Water Molecules ◽  
Hydration Energy ◽  
Hydrothermal Conditions ◽  
Potential Applications ◽  
Clay Layers ◽  
First Time ◽  
Hydrolysis Of ◽  
Alkaline Earth Cations

AbstractK-depleted phlogopite mica was used as a topotactic precursor and treated with alkali (Li+, K+, , Rb+, Cs+), alkaline-earth (Mg2+, Ca2+, Sr2+, Ba2+) and trivalent (Al3+) cations under hydrothermal conditions of 200°C and 30 MPa pressure. K-, NH4-, Rb- and Cs-aluminosilicate micas were synthesised at 200°C in one day. The synthesis of Cs-aluminosilicate mica, with potential applications in the management of nuclear wastes, has been achieved for the first time by this approach. Ion exchange by Li+, Na+ and alkaline-earth cations under hydrothermal conditions did not produce anhydrous mica phases but resulted in hydrous phases with one or two layers of water molecules between the clay layers. The formation of hydrous phases may be attributed to the high hydration energy of the above cations compared to K+, , RB+ and Cs+. Ion exchange with Al3+ produced a chlorite-like phase because of the hydrolysis of Al3+ under these hydrothermal conditions. These studies are of relevance in the immobilization of wastes where hazardous ions can be fixed in highly stable insoluble phases like mica or chlorite.

scholarly journals Structural and Catalytic Characterization of TsBGL, a β-Glucosidase From Thermofilum sp. ex4484_79

2021 ◽  
Vol 12 ◽  
Author(s):  
Anke Chen ◽  
Dan Wang ◽  
Rui Ji ◽  
Jixi Li ◽  
Shaohua Gu ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Specific Activity ◽  
Maximum Activity ◽  
Homologous Proteins ◽  
Glycosidic Bonds ◽  
Catalytic Sites ◽  
Potential Applications ◽  
Beta Glucosidase ◽  
Hydrolysis Of

Beta-glucosidase is an enzyme that catalyzes the hydrolysis of the glycosidic bonds of cellobiose, resulting in the production of glucose, which is an important step for the effective utilization of cellulose. In the present study, a thermostable β-glucosidase was isolated and purified from the Thermoprotei Thermofilum sp. ex4484_79 and subjected to enzymatic and structural characterization. The purified β-glucosidase (TsBGL) exhibited maximum activity at 90°C and pH 5.0 and displayed maximum specific activity of 139.2μmol/min/mgzne against p-nitrophenyl β-D-glucopyranoside (pNPGlc) and 24.3μmol/min/mgzen against cellobiose. Furthermore, TsBGL exhibited a relatively high thermostability, retaining 84 and 47% of its activity after incubation at 85°C for 1.5h and 90°C for 1.5h, respectively. The crystal structure of TsBGL was resolved at a resolution of 2.14Å, which revealed a classical (α/β)8-barrel catalytic domain. A structural comparison of TsBGL with other homologous proteins revealed that its catalytic sites included Glu210 and Glu414. We provide the molecular structure of TsBGL and the possibility of improving its characteristics for potential applications in industries.

Hydrolysis of Phosphopeptides. II. Leucine Aminopeptidase Hydrolysis of Free and O-Phosphorylated Serine Peptides.

1965 ◽  
Vol 19 ◽  
pp. 1566-1574 ◽  
Author(s):  
Georg Fölsch ◽  
Lars Strid ◽  
Olof Mellander ◽  
Olof Mellander ◽  
Merv Hinton
Keyword(s):  
Leucine Aminopeptidase ◽  
Hydrolysis Of

Silica Encapsulated CdS Tabular Nanocomposites via a Template Directed Agglomeration Mechanism

2008 ◽  
Vol 8 (11) ◽  
pp. 5878-5886 ◽  
Author(s):  
Jun Wang ◽  
Stephen J. Sollenberger ◽  
Ying Yuan ◽  
Timothy J. Yosenick ◽  
James H. Adair
Keyword(s):  
Electron Microscope ◽  
High Resolution ◽  
Coating Layer ◽  
Layer Growth ◽  
Cds Nanoparticles ◽  
Atomic Force ◽  
Transmission Electron ◽  
Potential Applications ◽  
Hydrolysis Of

Silica coated CdS tabular nanocomposites were synthesized through precipitation of CdS nanoparticles in octylamine/water bilayer system followed by in situ hydrolysis of tetraethoxylsilicate (TEOS) precursor. Face diameter of the nanoplatelets was in the range of 50∼250 nm with a variable thickness (3 to 25 nm) dictated by octylamine content or R ratio ([water]/[octylamine]). A uniform SiO2 outer shell of about 15 nm was observed regardless of the size of the high aspect ratio CdS nanoplatelets, which appeared to be agglomerated primarily owing to the confined bilayer template. Morphology and microstructure of the CdS/SiO2 tabular nanocomposites were characterized using atomic force microscope (AFM) and high resolution transmission electron microscope (HRTEM). A noticeable enhancement in absorbance for the UV-vis spectra was observed due to the SiO2 coating layer. Growth mechanism of nanocomposite platelets and potential applications associated with this anisotropic nanocomposite are discussed.

scholarly journals Mutating His29, His125, His133 or His158 abolishes glycosylphosphatidylinositol-specific phospholipase D catalytic activity

2005 ◽  
Vol 391 (2) ◽  
pp. 285-289 ◽  
Author(s):  
Nandita S. Raikwar ◽  
Rosario F. Bowen ◽  
Mark A. Deeg
Keyword(s):  
Catalytic Activity ◽  
Phospholipase D ◽  
Catalytic Domain ◽  
Computer Modelling ◽  
Critical Role ◽  
Biochemical Properties ◽  
Catalytic Site ◽  
Wild Type ◽  
Histidine Residues ◽  
Hydrolysis Of

Glycosylphosphatidylinositol (GPI)-specific phospholipase D (GPI-PLD) specifically cleaves GPIs. This phospholipase D is a secreted protein consisting of two domains: an N-terminal catalytic domain and a predicted C-terminal β-propeller. Although the biochemical properties of GPI-PLD have been extensively studied, its catalytic site has not been identified. We hypothesized that a histidine residue(s) may play a critical role in the catalytic activity of GPI-PLD, based on the observations that (i) Zn2+, which utilizes histidine residues for binding, is required for GPI-PLD catalytic activity, (ii) a phosphohistidine intermediate is involved in phospholipase D hydrolysis of phosphatidylcholine, (iii) computer modelling suggests a catalytic site containing histidine residues, and (iv) our observation that diethyl pyrocarbonate, which modifies histidine residues, inhibits GPI-PLD catalytic activity. Individual mutation of the ten histidine residues to asparagine in the catalytic domain of murine GPI-PLD resulted in three general phenotypes: not secreted or retained (His56 or His88), secreted with catalytic activity (His34, His81, His98 or His219) and secreted without catalytic activity (His29, His125, His133 or His158). Changing His133 but not His29, His125 or His158 to Cys resulted in a mutant that retained catalytic activity, suggesting that at least His133 is involved in Zn2+ binding. His133 and His158 also retained the biochemical properties of wild-type GPI-PLD including trypsin cleavage pattern and phosphorylation by protein kinase A. Hence, His29, His125, His133 and His158 are required for GPI-PLD catalytic activity.

Sign in / Sign up

Export Citation Format

Share Document