scholarly journals Alpha Amylase from Bacillus pacificus Associated with Brown Algae Turbinaria ornata: Cultural Conditions, Purification, and Biochemical Characterization

Processes ◽  
2020 ◽  
Vol 9 (1) ◽  
pp. 16
Author(s):  
Mona Alonazi ◽  
Aida Karray ◽  
Ahmed Yacine Badjah-Hadj-Ahmed ◽  
Abir Ben Bacha
Keyword(s):  
Biochemical Characterization ◽  
Alpha Amylase ◽  
Bacterial Symbionts ◽  
Terminal Sequence ◽  
Turbinaria Ornata ◽  
Substrate Analogs ◽  
Cultural Conditions ◽  
Initial Ph ◽  
Application Data ◽  
High Degree

We aimed in the current study, the identification of a marine bacterial amylase produced by Bacillus pacificus, which was associated with Turbinaria ornata. Cultural conditions were optimized for the highest amylase production on Tryptic soy broth media supplemented with starch 1% at initial pH 9, 55 °C for 24 h. The newly purified amylase was characterized for a possible biotechnological application. Data indicated that the obtained amylase with a molecular weight of 40 kD and the N-terminal sequence of the first 30 amino acids of amBp showed a high degree of homology with known alpha amylase, and was stable at 60 °C of pH 11. Among the tested substrate analogs, amBp was almost fully active on Alylose and Alylopectine (97%), but moderately hydrolyzed glycogen < sucrose < maltose < lactose. Therefore, the current amylase mainly generated maltohexaose from starch. Mg2+ and Zn2+ improved amylase activity up to 170%. While ethylenediamine tetraacetic acid (EDTA) similarly induced the greatest activity with purified amylase, PCMB had the least effect. Regarding all these characteristics, amylase from marine bacterial symbionts amBp has a new promising feature for probable therapeutic, industrial, and nutritional applications.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

scholarly journals PGPR Characteristics of Rhizospheric Bacteria to Understand the Mechanisms of Faba Bean Growth

Proceedings ◽  
2021 ◽  
Vol 66 (1) ◽  
pp. 27
Author(s):  
Rim Tinhinen Maougal ◽  
Maya Kechid ◽  
Chaima Ladjabi ◽  
Abdelhamid Djekoun
Keyword(s):  
Plant Growth ◽  
Faba Bean ◽  
Biochemical Characterization ◽  
Plant Growth Promoting Rhizobacteria ◽  
Bacterial Strains ◽  
Rhizospheric Bacteria ◽  
Plant Growth Promoting ◽  
Pgpr Traits ◽  
Taxonomic Groups ◽  
High Degree

Rhizobacteria play an important role in maintaining soil balance. Among these bacteria, there are those taht have shown their ability to promote the growth of plants, known as Plant Growth Promoting Rhizobacteria (PGPR). In our work, we are interested in characterizing 110 bacterial strains isolated in the field in the region of Ben Badis (Constantine Algeria) from 5 varieties of faba bean. Phenotypic and biochemical characterization showed that most of the isolates are cream-colored, slightly raised, flat and opaque, Gram−, catalase+ and oxidase−, and Bacillus form. PCA analysis allowed us to select 40 isolates with a high degree of variability to continue our work. The results obtained have directed us towards different taxonomic groups (rhizobium, Pseudomonas, Bacillus etc.). The evaluation of the PGPR potential of bacteria (phytostimulation, biofertilization and biocontrol), showed that 100% of bacteria are able to produce auxin at different concentrations, with the highest concentration (177.77 µg/mL) for the isolate 6, and that more than 50% of isolates are capable of producing nitrogen, ammonia and phytate mineralization. These PGPR traits have a direct effect on plant growth of five varieties of the faba bean and can be used to select the best performing bacteria for inoculation tests.

OBSERVATIONS ON AMYLOLYTIC BACTERIA: III. CULTURAL CONDITIONS INFLUENCING THE BREAKDOWN OF STARCH BY STENOTHERMOPHILIC BACTERIA BELONGING TO BACILLUS STEAROTHERMOPHILUS

1952 ◽  
Vol 30 (4) ◽  
pp. 360-370 ◽  
Author(s):  
Egon Stark ◽  
P. A. Tetrault
Keyword(s):  
Yeast Extract ◽  
Bacillus Stearothermophilus ◽  
Soluble Starch ◽  
The Other ◽  
Ph Changes ◽  
Proteose Peptone ◽  
Cultural Conditions ◽  
Initial Ph ◽  
Commercial Medium ◽  
Agar Media

Thirty-five cultures of Bacillus stearothermophilus hydrolyzed five starches under various cultural conditions. Hydrolysis occurred regardless of the type, brand, or batch of starch; regardless of the initial pH or of the subsequent pH changes of the medium. Starch in broth was better attacked than in agar media. Some cultures hydrolyzed 0.5%, but not 1% starch; others hydrolyzed easily 10% soluble starch. Length of incubation was important. Certain cultures never formed acid or sugar from starch. Dextrinization was a more reliable indication of starch hydrolysis than was the formation of acid or sugar. Soluble starch gave more consistent results in repeated experiments than did nonsoluble starches. The type of protein medium determines strongly the formation of amylase. Trypticase was the best commercial medium, yeast extract came second. The other 10 media yielded fewer amylolytic cultures. Yeast extract added to media enhanced amylase formation, except with trypticase. Tryptose, proteose-peptone, and neopeptone inhibited the growth of most cultures.

Isolation, Identification and Degradation Characterization of Synthetic Dyes Degrading Strain

2012 ◽  
Vol 610-613 ◽  
pp. 3140-3143
Author(s):  
Hui Xing Liang
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Synthetic Dyes ◽  
Complex Chemical ◽  
Chemical Structures ◽  
Cultural Conditions ◽  
Cultural Medium ◽  
Initial Ph

Dyes are usually difficult to be decolorized due to their complex chemical structures. In this work, a bacterium which had the ability of decoloration on synthetic dyes was isolated from Yancheng printworks and was identified as Pseudomonas aeruginosa. The effects of concentration of the dye concentration, cultural time, cultural temperature and initial pH of cultural medium on the efficiency of decoloration were investigated. The result showed that the optimal cultural conditions was: dye concentration was 50mg.L-1, cultural time was 72 h, cultural temperature was 28°C, initial pH of cultural medium was 7.0.

Cultural conditions optimization for production of β-galactosidase from Bacillus licheniformis ATCC 12759 under solid-state fermentation

2018 ◽  
Vol 43 (3) ◽  
pp. 240-247 ◽  
Author(s):  
Nurullah Akcan
Keyword(s):  
Solid State ◽  
Moisture Content ◽  
Bacillus Licheniformis ◽  
Solid State Fermentation ◽  
Incubation Temperature ◽  
Fermentation Medium ◽  
Inoculum Level ◽  
Cultural Conditions ◽  
Initial Ph ◽  
Fermentation Parameters

AbstractObjective:The aim of this work was to study the optimal cultivation conditions for β-galactosidase production byBacillus licheniformisATCC 12759.Materials and methods:The screening of β-galactosidase production fromB. licheniformisATCC 12759 was performed by solid state fermentation method on media rich with rice bran (RB). Different factors were tested for the optimization of β-galactosidase production.Results:Certain fermentation parameters involving incubation time, incubation temperature, inoculum level, moisture content, initial pH, agitation speed, size of fermentation medium and optimum temperature of β-galactosidase activity were studied separately. Maximal amount of β-galactosidase production was obtained when solid-state fermentation (SSF) was carried out using RB, having inoculum level 35%, moisture content of 20%, initial pH 7.5 at 37°C for 48 h.Conclusion:Results indicated that optimal fermentation conditions play a key role in the maximum production of β-galactosidase fromB. licheniformisATCC 12759. This study shows the potential of the studied enzymes to be promoting candidates for the degradation of lactose and production of important bioproducts.

Biochemical Characterization of Raw-starch-digesting Alpha Amylase Purified from Bacillus amyloliquefaciens

2008 ◽  
Vol 158 (3) ◽  
pp. 653-662 ◽  
Author(s):  
Dhanya Gangadharan ◽  
K. Madhavan Nampoothiri ◽  
Swetha Sivaramakrishnan ◽  
Ashok Pandey
Keyword(s):  
Bacillus Amyloliquefaciens ◽  
Biochemical Characterization ◽  
Alpha Amylase ◽  
Raw Starch

scholarly journals A Novel pH and Thermo-Tolerant Halophilic Alpha-amylase From Moderate Halophile Nesterenkonia Sp.Strain F: Gene Analysis, Molecular Cloning, Heterologous Expression and Biochemical Characterization

2021 ◽  
Author(s):  
Nastarn Solat ◽  
mohammad shafiei
Keyword(s):  
Type Species ◽  
Biochemical Characterization ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Alpha Amylase ◽  
Moderate Halophile ◽  
F Gene ◽  
Moderately Halophilic Bacterium ◽  
Wide Range ◽  
High Concentrations

Abstract A novel pH and thermo-tolerate halophilic alpha-amylase from moderately halophilic bacterium, Nesterenkonia sp.strain F was cloned and expressed in Escherichia coli. 16S rRNA sequence of the strain shared 99.46 % similarities with closely related type species. Also, the genome sequence shared ANI values below 92 % and dDDH values below 52 % with the closely related type species. Consequently, it is proposed that strain F represents a novel species. The AmyF gene was 1390 bp long and encodes an alpha-amylase of 463 amino acid residues with pI of 4.62. The deduced AmyF shared very low sequence similarity (<24%) with functionally characterized recombinant halophilic alpha- amylases. The recombinant alpha-amylase was successfully purified from Ni-NTA columns with a molecular mass of about 52 KDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme was active over a wide range of temperature (25–75 °C) and pH (4–9) with optimum activity at 45 °C and 7.5, respectively. Also, although it was active over a various concentrations of NaCl and KCl (0–4 M), increasing activity of the enzyme was observed with increasing concentration of these salts. Low concentrations of Ca2+ ion had no activating effect, but high concentrations of the ion (40 - 200 mM) enhanced activity of AmyF. The enzyme activity was increased by increasing concentrations of Mg2+, Zn2+, Hg2+ and Fe3+. However, it was inhibited only at very high concentrations of these metal ions. Cu2+ did not decrease the amylase activity and the highest activity was observed at 100 mM of the ion. These properties indicate wide potential applications of this recombinant enzyme in starch processing industries. This is the first isolation, cloning and characterization of a gene encoding alpha-amylase from Nesternkonia genus.

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