Bis[3-chloro-6-(3,5-dimethyl-1H-pyrazol-1-yl)picolinato]nickel(II) tetrahydrate
In the title complex, [Ni(C11H9ClN3O2)2]·4H2O, the Ni atom is coordinated by four N atoms and two O atoms derived from two tridentate 3-chloro-6-(3,5-dimethyl-1H-pyrazol-1-yl)picolinate ligands. The cis-N4O2 donor set defines a distorted octahedral geometry. In the crystal structure, the complex and water molecules are linked by O—H⋯O hydrogen bonds.
Bis[3‐chloro‐6‐(3,5‐dimethyl‐1H‐pyrazol‐1‐yl‐κN2)picolinato‐κ2N,O]cobalt(II) 2.5‐hydrate
In the title compound, [Co(C11H9ClN3O2)2]·2.5H2O, the CoII atom, which lies on a twofold rotation axis, is coordinated by four N atoms and two O atoms from two ligands in a distorted octa­hedral geometry. In the crystal structure, mol­ecules are linked together by inter­molecular O—H⋯O hydrogen bonds.
Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785
A maltotriose-forming amylase (G3Amy) from Kitasatospora sp. MK-1785 was successfully isolated from a soil sample by inhibiting typical extracellular α-amylases using a proteinaceous α-amylase inhibitor. G3Amy was purified from the MK-1785 culture supernatant and characterized. G3Amy produced maltotriose as the principal product from starch and was categorized as an exo-α-amylase. G3Amy could also transfer maltotriose to phenolic and alcoholic compounds. Therefore, G3Amy can be useful for not only maltotriose manufacture but also maltooligosaccharide-glycoside synthesis. Further, the G3Amy gene was cloned and expressed in Escherichia coli cells. Analysis of its deduced amino acid sequence revealed that G3Amy consisted of an N-terminal GH13 catalytic domain and two C-terminal repeat starch-binding domains belonging to CBM20. It is suggested that natural G3Amy was subjected to proteolysis at N-terminal region of the anterior CBM20 in the C-terminal region. As with natural G3Amy, recombinant G3Amy could produce and transfer maltotriose from starch.