Large-scale production and purification of an Erwinia ananas ice nucleation protein and evaluation of its ice nucleation activity.
The ice nucleation-active protein of Erwinia ananas IN-10 (inaA protein) was over-expressed as inclusion bodies in Escherichia coli in a yield of 15.3 mg of inaA protein from 60 mg of bacterial cells on a dry-matter basis. The inaA protein was purified from the inclusion bodies by solubilization with detergents to obtain a protein preparation free from sugar and lipid. This preparation had a distinct ice nucleation activity, indicating that the inaA protein per se is able to act as a nucleus.
Watabe
S
S
Department of Agricultural Chemistry, University of Tokyo, Japan.
Abe
K
K
Hirata
A
A
Emori
Y
Y
Watanabe
M
M
Arai
S
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000907:Antibodies, Bacterial / Q000276:immunology; D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis* / Q000276:immunology / Q000302:isolation & purification; D004885:Erwinia / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure; D005069:Evaluation Studies as Topic; D005615:Freezing; D008854:Microscopy, Electron; D008969:Molecular Sequence Data
D000596:Amino Acids; D000907:Antibodies, Bacterial; D001425:Bacterial Outer Membrane Proteins; C063113:ice nucleation protein