Expression and functional analysis of a hyperglycosylated glucoamylase in a parental host, Aspergillus awamori var. kawachi.
A modified glucoamylase gene (glaA) with an extra Thr- and Ser-rich Gp-I domain (T. Semimaru, M. Goto, K. Furukawa, and S. Hayashida, Appl. Environ. Microbiol. 61:2885-2890, 1995) was introduced into a mutant parental host, Aspergillus awamori var. kawachi, in which the original glaA gene had been completely deleted and replaced with the hygromycin phosphotransferase gene. The modified glaA was successfully expressed and secreted. The modified glucoamylase possessed higher digestibility of raw corn starch and higher stabilities in response to heat and extreme pH.
Goto
M
M
Department of Agricultural Chemistry, Kyushu University, Fukuoka, Japan. m_goto@agr.kyushu-u.ac.jp
Ekino
K
K
Furukawa
K
K
D001230:Aspergillus / Q000235:genetics* / Q000378:metabolism*; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D015966:Gene Expression Regulation, Fungal; D005087:Glucan 1,4-alpha-Glucosidase / Q000235:genetics* / Q000378:metabolism*; D016296:Mutagenesis; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics; D010957:Plasmids / Q000235:genetics; D011995:Recombination, Genetic; D017384:Sequence Deletion; D012694:Serine / Q000235:genetics; D013912:Threonine / Q000235:genetics; D003313:Zea mays / Q000378:metabolism
D013912:Threonine; D012694:Serine; D017853:Phosphotransferases (Alcohol Group Acceptor); C063242:hygromycin-B kinase; D005087:Glucan 1,4-alpha-Glucosidase