N-terminal sequence of amino acids and some properties of an acid-stable alpha-amylase from citric acid-koji (Aspergillus usamii var.).
An acid-stable alpha-amylase (AA) was purified from an acidic extract of citric acid-koji (A. usamii var.). The N-terminal sequence of the first 20 amino acids of the enzyme was identical with that of AA from A. niger, but the two enzymes differed in molecular weight. HPLC analysis for identifying the anomers of products indicated that the AA hydrolyzed maltopentaose (G5) at the third glycoside bond predominantly, which differed from Taka-amylase A and the neutral alpha-amylase (NA) from the citric acid-koji.
Suganuma
T
T
Department of Biochemical Science and Technology, Kagoshima University, Japan.
Tahara
N
N
Kitahara
K
K
Nagahama
T
T
Inuzuka
K
K
D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D004269:DNA, Bacterial / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009844:Oligosaccharides / Q000378:metabolism; D000516:alpha-Amylases / Q000737:chemistry / Q000235:genetics*
D004269:DNA, Bacterial; D009844:Oligosaccharides; C019193:maltopentaose; D000516:alpha-Amylases