Abstract
Using an antisense control strategy, we isolated an Aspergillus oryzae mutant that produced low levels of carboxypeptidases (CPases). The mutant TFC-1 expressed the antisense RNA of the structural gene of CPase O and showed about 30% of the CPase activity in the parent strain. Gel filtration analysis indicated that this mutant decreased the CPase activities not only of CPase O but also of CPase O-1 and O-2. This result indicated that the antisense RNA was able to control the expression of the CPase genes as a group. Using the mutant as a heterologous protein expression host that produced the low levels of CPases, a stable and higher level of lysozyme expression could be obtained compared with the wild-type. In vitro proteolytic degradation assay also demonstrated that human lysozyme was degraded by purified CPase O.
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Received: 16 June 1997 / Received last revision: 29 August 1997 / Accepted: 15 September 1997
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Zheng, X., Kobayashi, Y. & Takeuchi, M. Construction of a low-serine-type-carboxypeptidase-producing mutant of Aspergillus oryzae by the expression of antisense RNA and its use as a host for heterologous protein secretion. Appl Microbiol Biotechnol 49, 39–44 (1998). https://doi.org/10.1007/s002530051134
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DOI: https://doi.org/10.1007/s002530051134