Luteolin and its C-monoglycosides fromLupinus polyphyllus
The leaves of Lupinus polyphyllus Lindley, a wild-growing biennial plant, in the flowering phase were fixed with steam and dried in a thermostat at 55-60°C. The dry comminuted material (2 kg) was repeatedly extracted with 70% ethanol at room temperature by the steeping method, and the extract was distilled in vacuum. The concentrated residue was treated with 600 ml of hot water and filtered and the resulting filtrate was extracted successively with diethyl ether, yielding fraction i, and ethyl acetate, yielding fraction 2.
The Ultraviolet Spectra of Flavones and Flavonols
The methanol spectra of flavones and flavonols exhibit two major absorption peaks in the region 240 – 400 nm1. These two peaks are commonly referred to as Band I (usually 300 – 380 nm, Table V-1 records the λmaxvalues for Band I for all flavones and flavonols examined in the present investigation), and Band II (usually 240 – 280 nm). Band I is considered to be associated with absorption due to the B-ring cinnamoyl system, and Band II with absorption involving the A-ring benzoyl system (see III) [1].
Erratum to: 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.