Results 181 to 190 of about 12,368,947 (219)
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Production of bacterial α-amylase by B. amyloliquefaciens under solid substrate fermentation

Biochemical Engineering Journal, 2007
Abstract Production of α-amylase by Bacillus amyloliquefaciens, under solid substrate fermentation (SSF) was investigated in shaken-culture. The maximum α-amylase activity was obtained under the following optimized conditions: corn gluten meal (CGM) 30 g/l, yeast extract (YE) 10 g/l, agitation rate 150 rpm and fermentation temperature 33 °C.
Tanyildizi, M. Saban   +2 more
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Extracellular Protease Production by B. Amyloliquefaciens

1987
B. amyloliquefaciens produces large amounts of two major secretory proteases: alkaline protease and neutral protease. Protease production by this organism is very unusual in its response to inhibitors of transcription. Using the antibiotics rifampicin and actinomycin D, which block transcription, we have demonstrated the presence of an apparent mRNA ...
M. J. Bawden   +4 more
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Dual Mode of Action of Amylolysin: A Type-B Lantibiotic Produced by Bacillus amyloliquefaciens GA1

Protein & Peptide Letters, 2014
The partial genome sequencing of Bacillus amyloliquefaciens GA1 led to the identification of the aml gene cluster involved in the synthesis of the novel lantibiotic named amylolysin. Pure amylolysin was shown to have an antibacterial activity toward Gram-positive bacteria including methicillin resistant Staphylococcus aureus.
Arguelles Arias, Anthony   +2 more
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Purification and crystallization of α-amylases from mucoid and non-mucoid B. amyloliquefaciens strains

Journal of Crystal Growth, 2001
Abstract The purified α-amylases from mucoid and non-mucoid B. amyloliquefaciens strains were crystallized in forms suitable for X-ray diffraction analysis. Crystals were grown by the hanging-drop vapor diffusion method. Very thin crystals of α-amylase of non-mucoid strain were obtained in the presence 15% propanol, 12% PEG 6000 and 0.1 M PIPES (pH:
Sarikaya, ELİF, Mikami, B
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SEQUENCE OF CYANOGEN BROMIDE FRAGMENTS D AND E OF B. AMYLOLIQUEFACIENS ALPHA AMYLASE

International Journal of Peptide and Protein Research, 1981
Alpha amylase (Sigma type IIA) was cleaved by cyanogen bromide. The sequences of two fragments, D which contains 88 amino acids and E which contains 56, are presented. By applying the Chou‐Fasman rules, D is predicted to have 32% beta sheet and 37% alpha helix, and E is predicted to exhibit 11% beta sheet and 71% alpha helix.
O, Sachdev, F, Friedberg
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α-Amylase production by Bacillus subtilis and B. amyloliquefaciens in different PEG solutions

World Journal of Microbiology and Biotechnology, 2001
α-Amylase production by Bacillus subtilis and Bacillus amyloliquefaciens was investigated in polyethyleneglycol (PEG)-containing growth medium. Five different molecular weight PEGs (600, 3000, 4000, 8000 and 20,000) were used. Enzyme production with B.
Celal Ülger, Çervin Çirakoğlu
openaire   +1 more source

Derivatives of bacillus amyloliquefaciens ribonuclease (barnase) isolated after limited digestion by carboxypeptidases A and B

Biochemical and Biophysical Research Communications, 1970
Abstract The carboxy-terminal sequence of barnase is -Thr-Thr-Asp-His-Tyr-Gln-ThrPhe-Thr-Lys-Ile-Arg. Derivatives missing one, three, five and eight amino acids (CX-1, CX-3, CX-5 and CX-8) 1 have been produced by digestion with carboxypeptidases A and B, isolated and characterized.
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[Deletion analysis of the structural-functional organization of metalloendopeptidase precursor in B. amyloliquefaciens].

Voprosy meditsinskoi khimii, 2001
Functional destination of propeptides and precursors in bacillar secretory proteases remains uncertain. Formerly deletion assay demonstrated folding and secretion of subtilisin E, chymotrypsin-like protease SGPB from S. griseus and B. cereus metalloprotease to depend on full-length propeptide in the precursors.
S I, Novikova   +5 more
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Unraveling the Bioactivities and Immunomodulatory Potential of Postbiotics Derived from Bacillus subtilis and B. amyloliquefaciens for Aquaculture

Probiotics and Antimicrobial Proteins
Postbiotics are molecules or soluble factors released as a result of a probiotic's metabolic activity. Their use in enhancing the growth, health, and disease resistance of aquatic animals has gained considerable attention in aquaculture. The present investigation was designed to assess the beneficial effects of postbiotic products derived from two ...
Monalisha Kumar   +6 more
openaire   +2 more sources

[Comparison between alpha-amylase from B. amyloliquefaciens and B. licheniformis].

Biomedica biochimica acta, 1991
Two sequence-homologous alpha-amylases from B. amyloliquefaciens and B. licheniformis were studied with respect to their stability against heat denaturation and were compared with respect to common structure-stabilizing principles. The investigated alpha-amylases were isolated from culture broth of B. amyloliquefaciens and B. licheniformis.
openaire   +1 more source

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