Purification and properties of enantioselective lipase from a newly isolated Bacillus cereus C71

2007 ◽  
Vol 42 (6) ◽  
pp. 988-994 ◽  
Author(s):  
Chen Shaoxin ◽  
Qian Lili ◽  
Shi Bingzhao
Keyword(s):  
Bacillus Cereus ◽  
Purification And Properties

scholarly journals Purification and properties of two extracellular β-lactamases from Bacillus cereus 569/H

1970 ◽  
Vol 118 (3) ◽  
pp. 457-465 ◽  
Author(s):  
S. Kuwabara
Keyword(s):  
Molecular Weight ◽  
Bacillus Cereus ◽  
Zinc Sulphate ◽  
Deae Cellulose ◽  
Casein Hydrolysate ◽  
Crystalline Form ◽  
Casamino Acid ◽  
Fractional Precipitation ◽  
Purification And Properties ◽  
Rapid Production

1. When Bacillus cereus 569/H was grown in a casamino acid (casein-hydrolysate) medium containing zinc sulphate rapid production of extracellular β-lactamase II preceded that of β-lactamase I. 2. β-Lactamase I was separated from β-lactamase II by fractional precipitation with ammonium sulphate. 3. β-Lactamase I was purified by a process involving chromatography on Celite and DEAE-cellulose and β-lactamase II by chromatography on DEAE-cellulose after denaturation of β-lactamase I by heat. Both enzymes were obtained in crystalline form. 4. β-Lactamase II prepared in this way appeared to have a higher molecular weight than β-lactamase I and required Zn2+ as a cofactor for both cephalosporinase and penicillinase activities.

scholarly journals Separation, purification and properties of β-lactamase I and β-lactamase II from Bacillus cereus 569/H/9

1974 ◽  
Vol 143 (1) ◽  
pp. 115-127 ◽  
Author(s):  
Richard B. Davies ◽  
E. P. Abraham ◽  
J. Melling
Keyword(s):  
Molecular Weight ◽  
Bacillus Cereus ◽  
Large Scale ◽  
Cysteine Residue ◽  
Peptide Fragment ◽  
Tryptic Digest ◽  
Purification And Properties ◽  
Carbohydrate Complex ◽  
Entire Sequence ◽  
Main Components

1. A procedure was devised which is suitable for the isolation of β-lactamase I and β-lactamase II from Bacillus cereus 569/H/9 on a large scale. After adsorption on to Celite both enzymes were eluted in good yield and separated by chromatography on Sephadex CM-50. 2. β-Lactamase I was separated into three main components by isoelectric focusing and into two components by chromatography. 3. The Zn2+-requiring β-lactamase II obtained by this procedure had a lower molecular weight (22000) than β-lactamase I (28000) and also differed from the latter in containing one cysteine residue. 4. The β-lactamase II contained no carbohydrate, but showed the thermostability of the enzyme isolated earlier as a protein–carbohydrate complex. 5. Amino acid analyses and tryptic-digest ‘maps’ indicate that some degree of homology between β-lactamase I and β-lactamase II is possible, but that β-lactamase I is not composed of the entire sequence of β-lactamase II together with an additional peptide fragment. 6. A 6-methylpenicillin and a 7-methylcephalosporin showed much lower affinities for both enzymes than did penicillins and cephalosporins themselves.

Purification and Properties of an Amylase from Bacillus cereus NY-14

1985 ◽  
Vol 49 (12) ◽  
pp. 3369-3376
Author(s):  
Naohiro Yoshigi ◽  
Takahide Chikano ◽  
Minora Kamimura
Keyword(s):  
Bacillus Cereus ◽  
Purification And Properties

scholarly journals Purification and Properties of the Raw Starch Degrading α-amylase of Mutant strain: Bacillus cereus 1306

2004 ◽  
Vol 2 (2) ◽  
pp. 46-54
Author(s):  
Manoj Trivedi ◽  
S. K. Mandal
Keyword(s):  
Bacillus Cereus ◽  
Incubation Temperature ◽  
Gel Filtration ◽  
Tween 80 ◽  
Maximum Activity ◽  
Raw Starch ◽  
Purification And Properties ◽  
Amylase Production ◽  
Ph Range ◽  
Triton X

The raw starch-degrading α-amylase Produced by Bacillus cereus 1306 was purified to homogeneity by acetone precipitation and gel filtration chromatography.The Molecular weight of α-amylase was estimated to be 58KDa. The enzyme displayed maximum activity 85 Units/ml at pH 7.0 and an incubation temperature of 37˚C and Stable in the pH range of 5.0-9.0. Activity was inhibited in the presence of Hg2+,Cu2+,Fe3+ but no inhibition was observed in the presence of Zn2+. Medium containing CaCl2.2H2O enhanced amylase production over that on Ca2+-deficient medium. The detergent Tween-80 and Triton X-100 increased Biomass but Significantly Suppressed amylase production. The enzyme released large amount of glucose and maltose on hydrolysis of starch.

Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties

1992 ◽  
Vol 1118 (2) ◽  
pp. 130-133 ◽  
Author(s):  
Francesco Sgarrella ◽  
Antonella Del Corso ◽  
Maria Grazia Tozzi ◽  
Marcella Camici
Keyword(s):  
Bacillus Cereus ◽  
Purification And Properties
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