Phospholipase A1, process for its preparation and the use thereof
AssigneeSankyo Company, Limited
InventorsAtsushi Hattori, Noriyoshi Uchida, Masahiro Kitaoka
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Abstract
A Phospholipase A1 which is capable of hydrolyzing a phospholipid to produce a 2-acyl lysophospholipid and is obtainable from species of the fungus Aspergillus.
Claims18
A phospholipase A1obtained from species of the fungus Aspergillus, having the following characteristics:
- which hydrolyzes phospholipid between about pH 2.5 and about pH 6.0,
- having a stability to a temperature of an upper limit of between 45.degree. and 90.degree. C.,
- which is stable at a temperature of less than 90.degree. C.,
- which has a molecular weight of between about 30,000 and 40,000 daltons, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis,
- which has pI under isoelectric point electrophoresis at about pH 2.8 to about pH 4.5,
- which has an optimum temperature for activity of from pH 3.2 to about pH 5.5, and
- which has an optimum temperature for activity of from about 30.degree. to 65.degree. C.
A phospholipase A1a obtained from Aspergillus oryzae SANK 11870 FERM BP-3887 and having the following characteristics:
- molecular weight:
- 37,000 daltons, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate;
- isoelectric point:
- a pI at pH 3.9, as determined by isoelectric point electrophoresis
- optimum active pH:
- a pH of 3.5 to 4.5 in the presence of an alkyl aryl polyether alcohol non-ionic detergent or a pH of 4.5 to 5.5 in the absence of said alkyl aryl polyether alcohol non-ionic detergent
- stable pH region:
- a pH 5.5 or higher, with respect to an enzyme solution containing approximately 10 units/ml of enzyme in a 33 mM acetic acid/sodium acetate buffer solution, or a pH of 10.5 or less, with respect to an enzyme solution containing approximately 10 units/ml of enzyme in a 33 mM glycine/sodium chloride--sodium hydroxide buffer solution;
- and
- optimum temperature:
- 5.degree. C. to 60.degree. C.
A phospholipase A1b obtained from Aspergillus oryzae SANK 11870 FERM BP-3887 and having the following characteristics:
- molecular weight:
- 35,000 daltons, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate;
- isoelectric point:
- a pI at pH 4.3, as determined by isoelectric point electrophoresis;
- optimum active pH:
- a pH of 3.5 to 4.5 in the presence of an alkyl aryl polyether alcohol non-ionic detergent or a pH of 4.5 to 5.5 in the absence of said alkyl aryl polyether alcohol non-ionic detergent
- stable pH region:
- a pH of 5.5 or higher, with respect to an enzyme solution containing approximately 10 units/ml of enzyme in a 33 mM acetic acid/sodium acetate buffer solution, or a pH of 10.5 or less, with respect to an enzyme solution containing approximately 10 units/ml of enzyme in a 33 mM glycine/sodium chloride--sodium hydroxide buffer solution;
- and
- optimum temperature:
- 50.degree. C. to 60.degree. C.
A phospholipase A1 obtained from Aspergillus niger ATCC 9642 and having the following characteristics:
- molecular weight:
- 32,000 daltons, as measured using a Superose 12.TM. column;
- isoelectric point:
- a pI at pH 3.0, as determined by isoelectric point electrophoresis;
- optimum active pH:
- a pH of 4.0 to 5.0 in the presence of an alkyl aryl polyether alcohol non-ionic detergent and a pH of 4.5 to 5.0 in the absence of said alkyl aryl polyether alcohol non-ionic detergent;
- and
- optimum temperature:
- 50.degree. C. to 60.degree. C.
Dependencies are inferred from the claim text.