Immunoblot analysis of Bacillus subtilis cell extracts with polyclonal antibodies, raised against purified exocellular alpha-amylase, revealed one protein species of 82,000 Da. This protein was found even in cells in which the amyE gene, encoding exocellular alpha-amylase, was disrupted. Isolated from the membrane fraction, the 82,000-M(r) protein displayed an alpha-amylase activity in vitro.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC177296PMC
http://dx.doi.org/10.1128/jb.177.17.5148-5150.1995DOI Listing

Publication Analysis

Top Keywords

exocellular alpha-amylase
12
bacillus subtilis
8
alpha-amylase
5
characterization cell-bound
4
cell-bound alpha-amylase
4
alpha-amylase bacillus
4
subtilis 168
4
168 marburg
4
marburg immunologically
4
immunologically exocellular
4

Similar Publications

Bacillus stercoris PSSR12 (B. stercoris PE), an isolate from rice field soils, was identified via 16s rRNA sequencing. The synthesis of the inulin and inulin producing enzyme (IPE) in B.

View Article and Find Full Text PDF

Efficient genome editing in Aspergillus niger with an improved recyclable CRISPR-HDR toolbox and its application in introducing multiple copies of heterologous genes.

J Microbiol Methods

August 2019

School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, Guangdong, China; Guangdong Provincial Key Laboratory of Fermentation and Enzyme Engineering, South China University of Technology Guangzhou, Guangzhou 510006, Guangdong, China. Electronic address:

Aspergillus niger is an important industrial producer of enzymes due to its high capacity for producing exocellular secretory proteins. The CRISPR/Cas9 system has been developed as a genetic manipulation tool in A. niger.

View Article and Find Full Text PDF

We studied the interactions between conformers of exocellular alpha-amylase and small unilamellar vesicles (SUV) composed of the major membrane lipids of Bacillus subtilis under physiological conditions of pH, temperature and ionic strength. Using fluorescence spectroscopy, surface plasmon resonance (SPR) and phase separation, we show that the native alpha-amylase has no affinity for the SUV, whereas a partially folded form, displaying structural properties in common with the competent state for secretion, binds to the vesicles (KA approximately 10(5) M(-1)). This association prevented its subsequent folding.

View Article and Find Full Text PDF
Article Synopsis
  • The gene sacC from Bacillus subtilis is expressed in a specific strain, leading to the overproduction of levanase during exponential growth when induced by sucrose.
  • The processed levanase protein is released slowly, and its folding/unfolding transitions occur in a similar timeframe, indicating a direct correlation between folding rates and secretion.
  • Comparisons with other proteins suggest that levanase and alpha-amylase are processed more efficiently than levansucrase, possibly due to differences in their signal peptide sequences, while protein release is independent of molecular size.
View Article and Find Full Text PDF

SecA, the translocation ATPase of the preprotein translocase, accounts for 0.25% of the total protein in a degU32(Hy) Bacillus subtilis strain in logarithmic phase. The SecA level remained constant irrespective of the demand for exoprotein production but dropped about 12-fold during the late stationary phase.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!