cereus repandus/protease

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Biochemical analysis and investigation on the prospective applications of alkaline protease from a Bacillus cereus strain.

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Proteases have prospective financial and environment-friendly applications; hence attention is focused currently on the finding of new protease producing microorganism so as to meet the requirements of industry. A thermophilic bacterial strain producing extracellular protease activity was isolated

Antiplatelet and antithrombotic activity of a fibrin(ogen)olytic protease from Bacillus cereus strain FF01.

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Fibrin(ogen)olytic enzymes offer great promise for the treatment of thrombosis associated disorders. The present study describes the characterization of an extracellular fibrin(ogen)olytic serine protease (named Bacethrombase) purified from the Bacillus cereus strain FF01. The molecular mass of the

Purification and partial characterization of a neutral protease from a virulent strain of Bacillus cereus.

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The factors involved in the pathogenesis of Bacillus cereus (B. cereus) in non-gastrointestinal diseases are poorly investigated. Some researchers suggest that B. cereus proteases may be involved in these illnesses. The aim of this work was to purify and characterize a protease isolated from a

Regulation of extracellular protease production in Bacillus cereus T: characterization of mutants producing altered amounts of protease.

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Twenty-nine mutants of Bacillus cereus T were selected on casein agar for their inability to produce large amounts of extracellular protease. They all formed spores, and 27 were also auxotrophs for purines or pyrimidines. Upon reversion to prototrophy, a large fraction regained the capacity to

Regulation of extracellular protease production in Bacillus cereus.

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Both sporulation and protease production can be inhibited by growing Bacillus cereus T in a medium containing a high concentration of a mixture of amino acids. Mutants selected for the ability to sporulate in this inhibitory medium were found to produce high levels of protease in the normal and

Purification and characterization of Bacillus cereus protease suitable for detergent industry.

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An extracellular alkaline protease from an alkalophilic bacterium, Bacillus cereus, was produced in a large amount by the method of extractive fermentation. The protease is thermostable, pH tolerant, and compatible with commercial laundry detergents. The protease purified and characterized in this

Purification and characterization of a novel extracellular protease from Bacillus cereus KCTC 3674.

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Bacillus cereus KCTC 3674 excretes several kinds of extracellular proteases into the growth medium. Two proteases with molecular masses of approximately 36-kDa and 38-kDa, as shown by SDS-PAGE, were purified from the culture broth. The 38-kDa protease was purified from B. cereus cultivated at 37

Characterization and function of intracellular proteases in sporulating Bacillus cereus.

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Intracellular proteases from sporulating Bacillus cereus have been purified by ammonium sulfate fractionation, heat treatment and DEAE cellulose column chromatography. After the last purification step, two protease activities, with an activity ratio of about thirty to one are resolved. Both

An antibiotic, heavy metal resistant and halotolerant Bacillus cereus SIU1 and its thermoalkaline protease.

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BACKGROUND Many workers have reported halotolerant bacteria from saline conditions capable of protease production. However, antibiotic resistance and heavy metal tolerance pattern of such organisms is not documented very well. Similarly, only a few researchers have reported the pattern of pH change

Cloning of feather-degrading minor extracellular protease from Bacillus cereus DCUW: dissection of the structural domains.

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Bacterial extracellular proteases play an important role in cell survival and cell-cell communication. A high-molecular-mass minor extracellular protease (Vpr) from a feather-degrading bacterium, Bacillus cereus DCUW, has been reported by our laboratory. In the present study, we cloned and expressed

The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.

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The crystal structure of the neutral protease from Bacillus cereus has been refined to an R factor of 17.5% at 0.2-nm resolution. The enzyme, an extracellular metalloendopeptidase, consists of two domains and binds one zinc and four calcium ions. The structure is very similar to that of thermolysin,

Degradation of raw feather by a novel high molecular weight extracellular protease from newly isolated Bacillus cereus DCUW.

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Biotreatment of feather wastes and utilization of the degraded products in feed and foodstuffs has been a challenge. In the present study, we have demonstrated the degradation of feather waste by Bacillus cereus DCUW strain isolated during a functional screening based microbial diversity study on

E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution.

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The X-ray crystal structure of the Bacillus cereus neutral protease (CNP) active-site mutant E144S, in which the putative general base proposed for the thermolysin-like zinc neutral proteases, Glu144, has been replaced by serine, has been determined to a resolution of 2.8 A. This represents the

Purification and characterization of protease and chitinase from Bacillus cereus TKU006 and conversion of marine wastes by these enzymes.

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A chitinase- and protease-producing bacterium was isolated and identified as Bacillus cereus TKU006. The better condition on our tests for protease and chitinase production was found when the culture was shaken at 25 degrees C for 2 days in 25 mL of medium containing 2% shrimp shell powder (w/v),

Molecular characterization, catalytic, kinetic and thermodynamic properties of protease produced by a mutant of Bacillus cereus-S6-3

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The proteolytic strain Bacillus cereus-S6-3 was subjected to mutagenic treatments viz. UV irradiations and methyl methane sulfonate (MMS). The obtained mutant strain, B. cereus-S6-3/UM90 showed 1.34 fold over the parent strain. Molecular characterization of proteases from the parent (PP/S6-3) and

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