scholarly journals Cloning, Expression, and Characterization of a New Glycosaminoglycan Lyase from Microbacterium sp. H14

Marine Drugs ◽  
2019 ◽  
Vol 17 (12) ◽  
pp. 681
Author(s):  
Junhao Sun ◽  
Xu Han ◽  
Guanrui Song ◽  
Qianhong Gong ◽  
Wengong Yu
Keyword(s):  
Enzyme Activity ◽  
Metal Ions ◽  
Animal Experiments ◽  
Basic Research ◽  
Facilitated Diffusion ◽  
Divalent Metal Ions ◽  
Polysaccharide Lyase ◽  
Functional Studies ◽  
Dose Dependent

Glycosaminoglycan (GAG) lyase is an effective tool for the structural and functional studies of glycosaminoglycans and preparation of functional oligosaccharides. A new GAG lyase from Microbacterium sp. H14 was cloned, expressed, purified, and characterized, with a molecular weight of approximately 85.9 kDa. The deduced lyase HCLaseM belonged to the polysaccharide lyase (PL) family 8. Based on the phylogenetic tree, HCLaseM could not be classified into the existing three subfamilies of this family. HCLaseM showed almost the same enzyme activity towards hyaluronan (HA), chondroitin sulfate A (CS-A), CS-B, CS-C, and CS-D, which was different from reported GAG lyases. HCLaseM exhibited the highest activities to both HA and CS-A at its optimal temperature (35 °C) and pH (pH 7.0). HCLaseM was stable in the range of pH 5.0–8.0 and temperature below 30 °C. The enzyme activity was independent of divalent metal ions and was not obviously affected by most metal ions. HCLaseM is an endo-type enzyme yielding unsaturated disaccharides as the end products. The facilitated diffusion effect of HCLaseM is dose-dependent in animal experiments. These properties make it a candidate for further basic research and application.

scholarly journals Expression and characterization of thermotolerant lipase with broad pH profiles isolated from an AntarcticPseudomonassp strain AMS3

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e2420 ◽  
Author(s):  
Wahhida Latip ◽  
Raja Noor Zaliha Raja Abd Rahman ◽  
Adam Thean Chor Leow ◽  
Fairolniza Mohd Shariff ◽  
Mohd Shukuri Mohamad Ali
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Organic Solvent ◽  
Divalent Metal ◽  
Single Step ◽  
Divalent Metal Ions ◽  
Gene Encoding ◽  
Affinity Tags ◽  
Ph Range

A gene encoding a thermotolerant lipase with broad pH was isolated from an AntarcticPseudomonasstrain AMS3. The recombinant lipase AMS3 was purified by single-step purification using affinity chromatography, yielding a purification fold of approximately 1.52 and a recovery of 50%. The molecular weight was approximately ∼60 kDa including the strep and affinity tags. Interestingly, the purified Antarctic AMS3 lipase exhibited broad temperature profile from 10–70 °C and stable over a broad pH range from 5.0 to pH 10.0. Various mono and divalent metal ions increased the activity of the AMS3 lipase, but Ni2+decreased its activity. The purified lipase exhibited the highest activity in the presence of sunflower oil. In addition, the enzyme activity in 25% v/v solvents at 50 °C particularly to n-hexane, DMSO and methanol could be useful for catalysis reaction in organic solvent and at broad temperature.

Synthesis and characterization of bis(imino)pyridine complexes of divalent Mg and Zn

2016 ◽  
Vol 45 (14) ◽  
pp. 5989-5998 ◽  
Author(s):  
Thomas W. Myers ◽  
Tobias J. Sherbow ◽  
James C. Fettinger ◽  
Louise A. Berben
Keyword(s):  
Electronic Structure ◽  
Metal Ions ◽  
Torsion Angle ◽  
Divalent Metal ◽  
Synthesis And Characterization ◽  
Divalent Metal Ions ◽  
Structural Comparison ◽  
Bond Lengths ◽  
Pyridine Complexes

The synthesis and electronic structure of bis(imino)pyridine (I2P) complexes of the divalent metal ions, Zn(ii) and Mg(ii) are reported, and a correlation between the ligand Cim–Cpy bond lengths with the ligand torsion angle is described. Structural comparison with a new complex of Al(iii) and previously reported Al(iii) complexes is included.

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