Characterization of Xanthan Gum Degrading Enzymes from a Heat-stable, Salt-tolerant Bacterial Consortium

1993 ◽  
pp. 55-63 ◽  
Author(s):  
Jeffrey A. Ahlgren
Keyword(s):  
Xanthan Gum ◽  
Bacterial Consortium ◽  
Salt Tolerant ◽  
Degrading Enzymes ◽  
Heat Stable

Purification and partial amino acid sequence of thuricin S, a new anti-Listeriabacteriocin from Bacillus thuringiensis

2007 ◽  
Vol 53 (2) ◽  
pp. 284-290 ◽  
Author(s):  
Sonia Chehimi ◽  
François Delalande ◽  
Sophie Sablé ◽  
Mohamed-Rabeh Hajlaoui ◽  
Alain Van Dorsselaer ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Proteinase K ◽  
Terminal Sequence ◽  
Partial Amino Acid Sequence ◽  
Ph Values ◽  
Heat Stable ◽  
Isolation And Characterization ◽  
Terminal Amino ◽  
Edman Sequencing

We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3–10.5). The monoisotopic mass of thuricin S purified by high perfomance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.

Cloning, Expression, and Enzyme Characterization of an Acid Heat-Stable Phytase from Aspergillus fumigatus WY-2

2007 ◽  
Vol 55 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Yan Wang ◽  
Xiaorong Gao ◽  
Qiao Su ◽  
Wei Wu ◽  
Lijia An
Keyword(s):  
Aspergillus Fumigatus ◽  
Enzyme Characterization ◽  
Heat Stable

Isolation and characterization of the heat stable enterotoxin from a pathogenic bovine strain of Escherichia coli

1984 ◽  
Vol 9 (4) ◽  
pp. 399-414 ◽  
Author(s):  
Charles Gerday ◽  
Marianne Herman ◽  
Jacques Olivy ◽  
Nicole Gerardin-Otthiers ◽  
Dominique Art ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heat Stable ◽  
Isolation And Characterization ◽  
Bovine Strain

Synthesis and Characterization of Silver-Histidine Complex Doped Montmorillonite Antibacterial Agent

2012 ◽  
Vol 510 ◽  
pp. 757-761 ◽  
Author(s):  
Shu’e Duan ◽  
Yun Hui Zhai ◽  
Ying Juan Qu
Keyword(s):  
Antibacterial Agent ◽  
Sea Water ◽  
Antibacterial Activities ◽  
Exchange Capacity ◽  
Salt Tolerant ◽  
X Ray Diffraction ◽  
Ion Exchange Reaction ◽  
Cationic Exchange ◽  
Loading Amount

In this paper a novel colorless and salt-tolerant silver-histidine complex doped montmorillonite (Na-MMT) antibacterial agent (SHMMT) power was synthesized by ion exchange reaction using silver-histidine complex ion [Ag (his)] + as precursor, and characterized by atomic absorption spectrophotometer (AAS) and power X-ray diffraction (XRD). The antibacterial activities against Pseudoalteromonas carrageenovora were examined by a modified broth dilution test and the plate counting method. The salt-tolerant property was determined by the antibacterial activities of the sea water soaked SHMMT. The results showed that the Ag loading amount of SHMMT powder reached 1.7mmol/g, far more than the cationic exchange capacity (CEC) of Na-MMT. SHMMT powder had high bacterial activity eventhough it was soaked in the sea water for 30 days. 1

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