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glutaminase/cereus

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Partitioning studies of L-glutaminase production by Bacillus cereus MTCC 1305 in different PEG-salt/dextran.

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Partitioning studies of L-glutaminase production by Bacillus cereus MTCC 1305 was carried out in different PEG-salt/PEG-dextran system. The partitioning value of L-glutaminase increased with increasing molecular weight of PEG from 2000-4000 kDa and decreased with higher molecular weight of 6000 kDa.

Biochemical characterization and antitumor study of L-glutaminase from Bacillus cereus MTCC 1305.

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L-Glutaminase (E.C.3.5.2.1) extracellularly produced by Bacillus cereus MTCC 1305 was purified to apparent homogeneity with a fine band. The molecular weight of native enzyme and its subunit were found to be approximately 140 and 35 kDa, respectively, which indicates its homotetrameric nature. The
Response surface methodology and artificial neural network were used to optimize cultural conditions of L-glutaminase production from Bacillus cereus MTCC 1305. ANN model was superior to RSM model with higher value of coefficient of determination (99.97ANN>97.78RSM), predicted distribution

Gene cloning and expression of the l-asparaginase from Bacillus cereus BDRD-ST26 in Bacillus subtilis WB600.

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l-Asparaginase (ASN; EC 3.5.1.1) shows great commercial value because of its ability to reduce toxic levels of acrylamide in foods. To achieve high-efficiency production of l-asparaginase, an open reading frame of 978 bp encoding asparaginase (BcA) was amplified from Bacillus cereus BDRD-ST26,
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