Expression of active and inactive recombinant soluble trehalase using baculovirus-silkworm expression system and their glycan structures.
Silkworm soluble trehalase was expressed as a fusion protein with an N-terminal or C-terminal hexahistidine tag in a baculovirus-silkworm expression system and assayed for enzymatic activity. Only N-terminally tagged trehalase showed a high activity. This study is the first to report in vitro functional expression of recombinant insect soluble trehalase.
Ujita
Minoru
M
Laboratory of Biological Chemistry, Department of Applied Biological Chemistry, Faculty of Agriculture, Meijo University, Tempaku-ku, Nagoya 468-8502, Japan. ujita@meijo-u.ac.jp
Yamanaka
Mayumi
M
Maeno
Yumiko
Y
Yoshida
Koki
K
Ohshio
Wakana
W
Ueno
Yoshinori
Y
Banno
Yutaka
Y
Fujii
Hiroshi
H
Okumura
Hiroki
H
D000818:Animals; D016367:Baculoviridae / Q000235:genetics*; D012831:Bombyx / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D003001:Cloning, Molecular; D015870:Gene Expression; D005822:Genetic Vectors; D006639:Histidine; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics; D014198:Trehalase / Q000096:biosynthesis* / Q000235:genetics
C471213:His-His-His-His-His-His; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D006639:Histidine; D014198:Trehalase