http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Optimization of the Secretion Pathway for Heterologous Proteins in Bacillus subtilis
박성훈,Wolfgang Schumann 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.4
Secretion of homologous proteins in large amounts has been accomplished for many proteins, but no efficient secretion system has been described so far which can be generally applied for heterologous proteins. The objective of this review article is to compare the three major secretion pathways in E. coli and in B. subtilis and review the stages of conversion of the secreted proteins from the unfolded polypeptide chains into the correctly folded and fully active protein. Furthermore, bottlenecks in the production of heterologous proteins and the ways to resolve them are briefly discussed.
Disulfide Bonds of Proteins Displayed on Spores of Bacillus subtilis Can Occur Spontaneously
Richter, Anne,Kim, Wooil,Kim, June-Hyung,Schumann, Wolfgang Springer-Verlag 2015 Current microbiology Vol.71 No.1
<P>Surface display using spores of Bacillus subtilis is widely used to anchor antigens and enzymes of different sources. One open question is whether anchored proteins are able to form disulfide bonds. To answer this important question, we anchored the Escherichia coli alkaline phosphatase PhoA on the spore surface using two different surface proteins, CotB and CotZ. This enzyme needs two disulfide bonds to become active. Subsequently, we purified the spores and assayed for alkaline phosphatase activity. In both cases, we were able to recover enzymatic activity. Next, we asked whether formation of disulfide bonds occurs spontaneous or is catalyzed by thiol-disulfide oxidoreductases upon lysis of the cells. The experiment was repeated in a double-knockout mutant δbdbC and δbdbD. Since the disulfide bonds are also present on spores prepared from the double knockout, we conclude that oxidative environment after cell lysis is sufficient for disulfide formation of alkaline phosphatase.</P>