Purification and characterization of purple acid phosphatase PAP1 from dry powder of sweet potato.
Purple acid phosphatase (PAP) was purified from sweet potato dry powder, which is used as a food additive. Spectrometric and enzymatic analyses, and analysis of the amino-terminal sequence indicated that the purified purple acid phosphatase was PAP1. High activity in neutral and acidic conditions, broad substrate specificity, and good thermal stability of PAP1 suggest the possibility of practical applications of PAP1.
Kusudo
Tatsuya
T
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Japan.
Sakaki
Toshiyuki
T
Inouye
Kuniyo
K
D000135:Acid Phosphatase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006023:Glycoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D027723:Ipomoea batatas / Q000201:enzymology*; D000073718:Pancreatitis-Associated Proteins; D013379:Substrate Specificity
D006023:Glycoproteins; D000073718:Pancreatitis-Associated Proteins; C000612141:REG3A protein, human; C091137:purple acid phosphatase; D000135:Acid Phosphatase