Influence of a cell-wall-associated protease on production of alpha-amylase by Bacillus subtilis

Article Abstract:

Research was conducted to examine a potential role of products of wprA in the integrity of secretory proteins during late stages in the secretion pathway. The potential of wprA mutants to increase the productivity of Bacillus subtilis for secretory proteins was also investigated. Results identified one role for the products of the B. subtilis wprA gene. Findings have important implications for the use of B. subtilis and other members of the genus as hosts for the secretion of native and nonnative Bacillus proteins.

Proteases, Bacillus subtilis, Bacterial cell walls, Proteolysis

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Purification and characterization of an extracellular alpha-amylase from Clostridium perfringens Type A

Article Abstract:

The alpha-amylase enzyme secreted by Clostridium perfringens is most active at 6.5 pH and 30 degrees centigrade (C). If calcium is present the enzyme becomes inactive at 45 to 50 degrees C but if calcium is absent it becomes inactive at 35 to 40 degrees C. The pI of the enzyme is 4.75 and the molecular mass is estimated to be 76kDa. This enzyme reduces carbohydrates to oligonucleotides and is necessary for the bacteria to produce spores and form enterotoxins. These enterotoxins cause many diseases in humans.

Analysis, Clostridium

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Purification and properties of a maltotetraose- and maltotriose-producing amylase from Chloroflexus aurantiacus

Article Abstract:

Amylase from Chloroflexus aurantiacus was extracted, purified and analyzed. The enzyme has a molecular weight of 210,000 Da and has no subunit. Optimal pH for activity was determined as 7.5, and optimal temperature was 71 degrees Celsius. The enzyme appears to require calcium for optimal activity, and is inhibited by mercury, zinc, copper, manganese and nickel. Products of its hydrolysis of soluble starch were maltotetraose and maltotriose, suggesting that it is a type of alpha-amylase.

Physiological aspects, Bacteria, Photosynthetic, Photosynthetic bacteria

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