Isolation and identification of amino acids secreted by Bacillus amyloliquefaciens T1 with anti-cyanobacterial effect against cyanobacterium Microcystis aeruginosa

2021 ◽  
Vol 231 ◽  
pp. 329-339
Author(s):  
Bo Xu ◽  
Lihong Miao ◽  
Jing Yu ◽  
Lipeng Ji ◽  
Hao Lu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Microcystis Aeruginosa ◽  
Bacillus Amyloliquefaciens ◽  
Isolation And Identification

ISOLATION AND IDENTIFICATION OF THE FAST-DEATH FACTOR IN MICROCYSTIS AERUGINOSA NRC-1

1959 ◽  
Vol 37 (1) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Body Weight ◽  
Microcystis Aeruginosa ◽  
Sodium Salt ◽  
Cyclic Peptide ◽  
Isolation And Identification ◽  
Toxic Compound ◽  
Molar Ratios ◽  
Crude Preparation

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.

ISOLATION AND IDENTIFICATION OF THE FAST-DEATH FACTOR IN MICROCYSTIS AERUGINOSA NRC-1

1959 ◽  
Vol 37 (3) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Body Weight ◽  
Microcystis Aeruginosa ◽  
Sodium Salt ◽  
Cyclic Peptide ◽  
Isolation And Identification ◽  
Toxic Compound ◽  
Molar Ratios ◽  
Crude Preparation

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.

Amino Acids as Neurotransmitters.: A Symposium to honour Hugh McLennan on his retirement

1991 ◽  
Vol 69 (7) ◽  
pp. 1048-1048
Author(s):  
J. R. Ledsome
Keyword(s):  
Amino Acids ◽  
Spinal Cord ◽  
Amino Acid ◽  
Synaptic Transmission ◽  
Chloride Channels ◽  
Excitatory Amino Acid ◽  
Rapid Development ◽  
Long Term Potentiation ◽  
Isolation And Identification ◽  
University Of British Columbia

A meeting was held at the University of British Columbia on May 28–29, 1990 to honour the many important scientific contributions made by Dr. Hugh McLennan to our understanding of chemical neurotransmission in the brain and spinal cord. The invited speakers were those with whom Dr. McLennan has at one time or another collaborated, and their presentations reflected Hugh's early interest in GÀBA (factor I) as an inhibitory transmitter and his research over the last two decades into the physiology and pharmacology of acidic amino acid receptors.The session on GABA opened with an intriguing discussion by Professor Florey of the history of the isolation and identification of GABA as a neurotransmitter and was followed by papers dealing with the electrophysiological actions of GABA. Professor Curtis discussed its pre- and post-synaptic actions in the spinal cord, while Dr. Mathers presented data derived from GABA-gated chloride channels isolated from cultured neurones. Professor Krnjević was unfortunately unable to attend the symposium.Work presented by Professors Watkins and Lodge and Dr. Curry provided an excellent historical perspective on the birth and rapid development of excitatory amino acid pharmacology, a field to which Dr. McLennan has contributed enormously.Among the topics pertaining to the electrophysiological actions of acidic amino acids was the role of the NMDA receptor both in long-term potentiation (Dr. Collingridge) and in synaptic transmission in the kainic acid-lesioned hippocampus (Dr. Wheal), the effects of antagonists on synaptic transmission in the thalamus (Dr. Hicks), and the modulation by catecholamines of glutamate-induced neuronal excitations (Dr. Marshall).In his closing address Dr. McLennan, with characteristic grace and style, acknowledged the efforts of his co-workers in his many achievements. Those of us who have had the great pleasure of collaborating with Hugh here at UBC or within the scientific community wish him all the best in his retirement.

Isolation and Identification of Bacillus from Spontaneous Fermented Sufu

2013 ◽  
Vol 634-638 ◽  
pp. 1179-1183 ◽  
Author(s):  
Jing Deng ◽  
Hua Chang Wu ◽  
Xing Xiu Zhao ◽  
Jiao Jiao Shi
Keyword(s):  
Bacillus Subtilis ◽  
Bacillus Cereus ◽  
Bacillus Amyloliquefaciens ◽  
Fermented Food ◽  
Identification System ◽  
Isolation And Identification ◽  
Spontaneous Fermentation ◽  
Fermentation Products ◽  
Microbial Identification ◽  
Microbial Identification System

Sufu is a traditional Chinese fermented food. The safety of spontaneous fermentation products has been concerned by more and more people. A total of four isolates with big clear halos on the casein medium plate were isolated from spontaneous fermented Sufu in southern Sichuan. A1 and A3 most likely belong to Bacillus cereus B according to their phenotype and Biolog Microbial Identification System. B2 was classified in group as Bacillus amyloliquefaciens B with the same methods. A2 was identified as Bacillus subtilis according to their phenotype and 16SrRNA. The safety of the strains are also discussed.

Production, isolation and identification of low molecular mass peptides from blue cheese by high performance liquid chromatography

1991 ◽  
Vol 58 (3) ◽  
pp. 363-372 ◽  
Author(s):  
Dolores Gonzalez de Llano ◽  
M. Carmen Polo ◽  
Mercedes Ramos
Keyword(s):  
Amino Acids ◽  
Molecular Mass ◽  
High Performance ◽  
Phosphotungstic Acid ◽  
Soluble Fraction ◽  
Water Soluble ◽  
Isolation And Identification ◽  
Blue Cheese ◽  
Water Soluble Fraction ◽  
Gel Permeation

SummaryThe blue cheese nitrogenous fractions soluble in water and in 5% phosphotungstic acid (PTA) were analysed by HPLC after 3–180 d ripening. In the water-soluble fraction, in addition to four or five major peaks corresponding to amino acids, there were many minor peaks, which increased during ripening. The low molecular mass peptides, soluble in 5% PTA, showed ripening-induced increments. A method combining precipitation with 5% PTA, gel permeation and subsequent HPLC was used to isolate some peptides of cheese. Four peptides containing between seven and ten residues were isolated and their amino acid composition and N-terminal residues determined.

Isolation and identification of antifungal peptides from Bacillus amyloliquefaciens W10

2017 ◽  
Vol 24 (32) ◽  
pp. 25000-25009 ◽  
Author(s):  
Qing-Xia Zhang ◽  
Ying Zhang ◽  
Hai-Huan Shan ◽  
Yun-Hui Tong ◽  
Xi-Jun Chen ◽  
...  
Keyword(s):  
Bacillus Amyloliquefaciens ◽  
Isolation And Identification ◽  
Antifungal Peptides

scholarly journals Sequence of the N-terminal half of Bacillus amyloliquefaciens α-amylase

1980 ◽  
Vol 185 (2) ◽  
pp. 387-395 ◽  
Author(s):  
H Chung ◽  
F Friedberg
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Primary Structure ◽  
Bacillus Amyloliquefaciens ◽  
Proteolytic Enzymes ◽  
Alpha Amylase ◽  
Sequence Determination ◽  
N Terminus

Bacillus amyloliquefaciens alpha-amylase (1,4-alpha-D-glucan glucanohydrolase. EC 3.2.1.1), which is commercially supplied as ‘Bacillus subtilis alpha-amylase’ does not cross-react immunologically with B. subtilis alpha-amylase. This enzyme (from B. amyloliquefaciens) was cleaved by treatment with CNBr into seven fragments. Peptide A was selected for sequence determination. It is the longest one, containing 185 amino acids (i.e. approx. 50% of the total molecule) and connects to the hexapeptide of the N-terminus. Its primary structure was aligned by use of various proteolytic enzymes. The sequence of amino acids 181-184 is identical with that of amino acids 14-17 of the alpha-amylase isolated from B. subtilis (except that amino acid 183 is asparagine rather than aspartic acid).

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