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At least 19 recordsLinked to original sources
PubMed1977

Isolation and characterization of a polynucleotide phosphorylase from Bacillus amyloliquefaciens.

Bacillus amyloliquefaciens BaM-2 produces large amounts of extracellular enzymes, and the synthesis of these proteins appears to be dependent upon abnormal ribonucleic acid metabolism. A polynucleotide phosphorylase (nucleoside diphosphate:polynucleotide nucleotidyl transferase) was identified, purified, and characterized from this strain. The purification scheme involved cell disruption, phase partitioning, differential (NH4)2SO4 solubilities, agarose gel filtration, and diethylaminoethyl-Sephadex chromatography. The purified enzyme demonstrated the reactions characteristic of polynucleotide phosphorylase: polymerization, phosphorolysis, and inorganic phosphate exchange with the beta-phosphate of a nucleotide diphosphate. The enzyme was apparently primer independent and required a divalent cation. The reactions for the synthesis of the homopolyribonucleotides, (A)n and (G)n, were optimized with respect to pH and divalent cation concentration. The enzyme is sensitive to inhibition by phosphate ion and heparin and is partially inhibited by rifamycin SV and synthetic polynucleotides.

Adenosine Diphosphate↗
PubMed1975

Release of extracellular enzymes from Bacillus amyloliquefaciens.

Washed-cell suspensions of Bacillus amyloliquefaciens secrete significant amounts of the extracellular enzymes alpha-amylase and protease for about 15 min in the almost complete absence of protein synthesis. This apparently represents release of preformed enzyme en route to secretion. The release was independent of energy but was affected by temperature. Pulse-labeling experiments showed that newly synthesized enzyme molecules are either immediately released into the external medium or equilibrate with the preformed enzyme prior to eventual secretion. The results are compatible with a model of secretion whereby enzyme molecules emerging from the cell membrane become temporarily restricted by the cell wall so that a small pool of active enzyme accumulates in this region.

Amino Acids↗
PubMed1978

alpha-Glucosidase, a membrane-bound enzyme of alpha-glucan metabolism in Bacillus amyloliquefaciens. Purification and partial characterization.

The organism Bacillus amyloliquefaciens is capable of producing alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) and isoamylase (glycogen 6-glucanohydrolase, EC 3.2.1.68) extracellurlarly and a membrane-bound, intracellular alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20). The amounts of alpha-glucosidase in cells of B. amyloliquefaciens grown on amylaceous polysaccharides were significantly higher then in cells grown on non-carbohydrate carbon sources. alpha-Glucosidase was exclusively found associated with membranes from ruptured spheroplasts by subcellular fractionation and solubilization studies. Salt solutions and chelating agents alone did not dislodge alpha-glucosidase from membranes, but in combination with detergents were most effective in solubilizing active enzyme (0.1% sodium cholate (pH 8.0)/0.4 M sodium chloride). Purified alpha-glucosidase very rapidly hydrolized p-nitrophenyl alpha-D-glucopyranoside and sucrose. Maltose, maltotriose, isomaltose and isomaltotriose were hydrolized at slower rates, whereas beta-glucosides and polymeric alpha-glucans were not attacked. Other properties of the purified enzyme were as follows: Temperature optimum for catalysis = 39 +/- 1 degrees C; pH optimum = 6.8; molecular weight = 27,000 +/- 1000. alpha-Glucosidase is proposed to function in the endogenous metabolism of alpha-glucans provided extracellularly as carbon sources for growth of B. amyloliquefaciens.

Bacillus↗
PubMed1978

Membrane phospholipid asymmetry in Bacillus amyloliquefaciens.

The phospholipid distribution in the membrane of Bacillus amyloliquefaciens was studied by using phospholipase C (B. cereus), phospholipase A2 (Crotalus), and the nonpenetrating chemical probe trinitrobenzenesulfonic acid. After treatment of intact protoplasts of B. amyloliquefaciens with either phospholipase, about 70% of total membrane phospholipid was hydrolyzed; specifically, about 90, 90, and 30% of phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin, respectively. Under these conditions, protoplasts remained intact and sealed. However, when protoplasts that were permeabilized by cold-shock treatment were incubated with either of the phospholipases, up to 80% of cardiolipin was hydrolyzed and phosphatidylglycerol and phosphatidylethanolamine were hydrolyzed virtually to completion. In intact cells, 92% of the phosphatidylethanolamine could be labeled with trinitrobenzenesulfonic acid under conditions in which the reagent did not penetrate the membrane to any significant extent. These results indicate that 70% of total phospholipid of this bacillus exists in the outer half of the bilayer. The distribution of phosphatidylethanolamine in this bilayer is highly asymmetric with it being located predominantly in the outer half. The results with phospholipases suggest that the distributions of cardiolipin and phosphatidylglycerol are also asymmetric but independent confirmation of this is required.

Bacillus↗
PubMed2025

Identification of an antifungal lipopeptide from Bacillus amyloliquefaciens HAU3 inhibiting the growth of Fusarium graminearum using preparative chromatography and 2D-NMR.

UNLABELLED: The presence of fungal contamination and its mycotoxins in animal feed is pervasive, posing a significant threat to the well-being and performance of animals, as well as the safety of animal-derived food products. In this work, we screened a strain of Bacillus amyloliquefaciens (B. amyloliquefaciens) HAU3 that exhibits efficient antifungal activity against the growth of Fusarium graminearum (F. graminearum). The antifungal activity was detected in the supernatant, with 20% sterile supernatant demonstrating an impressive antifungal rate of 98.46% against F. graminearum. The antifungal activity of the strain was evaluated through spectrum analysis and silage trials, revealing its effective antifungal activity against multiple fungal species. Furthermore, the strain is capable of degrading ZEN and its derivatives. The targeted disruption of fungal mycelial membrane was observed using scanning electron microscopy and transmission electron microscopy. Additionally, staining with the reactive oxygen species (ROS)-sensitive fluorogenic dye DCFH-DA and propidium iodide (PI) revealed that the strain induces accumulation of ROS in fungal mycelia. The active compounds underwent further separation, purification, and detection. The prominent active peak was identified through mass spectrometry and magnetic resonance spectroscopy. The molecular structure of the active compounds was predicted to be lipopeptides composed of 8 amino acids known as fengycin. The whole genome sequencing and informatics analysis unveiled a total of 13 gene clusters responsible for the synthesis of secondary metabolites. The antifungal effects of B. amyloliquefaciens HAU3 are exerted through the synthesis of fengycin, which selectively targets and compromises the integrity of fungal mycelia membranes, thereby making it a potential biocontrol agent for mitigating mycotoxin contamination in feed. IMPORTANCE: Mycotoxin contamination in animal feed, predominantly driven by Fusarium graminearum, represents a persistent threat to livestock health and food chain integrity. Here, we report the isolation of a soil-derived Bacillus amyloliquefaciens HAU3, exhibiting potent and broad-spectrum antifungal activity alongside efficient biodegradation of zearalenone and its derivatives. Mechanistic dissection reveals that fengycin, the principal bioactive metabolite, compromises fungal membrane integrity and elicits intracellular oxidative stress, culminating in hyphal collapse. Genomic profiling uncovers a diverse repertoire of biosynthetic gene clusters underpinning secondary metabolite production. These findings establish strain HAU3 as a promising microbial chassis for the development of next-generation biocontrol strategies aimed at mitigating mycotoxin burden in agroecosystems.

Bacillus amyloliquefaciens↗
PubMed2026

Integrated Genome Mining and Bioactivity-Guided Isolation of Antimicrobial Peptides from Bacillus amyloliquefaciens BS4.

Bacterial resistance remains a critical global health challenge, driving the continuous search for novel antimicrobial agents. Bacillus amyloliquefaciens is a recognized repository of bioactive metabolites; however, its full biosynthetic potential requires integrated genomic and experimental validation. This study characterized the antimicrobial profile of B. amyloliquefaciens BS4 through a hybrid pipeline. Genome sequencing and de novo assembly revealed a 3.9 Mb chromosome with a G + C content of 46.14%. Functional annotation identified 3,887 coding sequences, including pathways for siderophore biosynthesis and a complete bacilysin biosynthetic cluster. BGC analysis using antiSMASH v7.1.0 and BAGEL4 identified 18 biosynthetic gene clusters, while similarity network analysis via BiG-SCAPE highlighted unique singleton BGCs, indicating untapped biosynthetic diversity. Although in silico screening via Macrel predicted two putative cationic antimicrobial peptides (AMPs), bioactivity-guided purification utilizing sequential RP-HPLC, and de novo sequencing revealed a distinct set of four active peptides. Notably, three of these sequences were identified as fragments derived from the BclA exosporium protein family, highlighting the structural proteome as a non-canonical source of antimicrobials. The purified fractions exhibited activity against M. luteus and E. coli, while displaying no significant hemolytic activity or cytotoxicity, even above the MIC values. Molecular docking further supported the interaction of these candidates with bacterial targets. Overall, this hybrid strategy effectively uncovers the antimicrobial complexity of BS4, revealing 'cryptic' peptide candidates with therapeutic potential.

Bacillus amyloliquefaciens BS4↗
PubMed1978

Effect of growth temperature on membrane fatty acid composition and susceptibility to cold shock of Bacillus amyloliquefaciens.

We investigated the fatty acid composition of the membrane of Bacillus amyloliquefaciens grown at different temperatures. A decrease in growth temperature was accompanied by an increase in the ratio of branched- to straight-chain fatty acids and a marked increase in the level of unsaturation of branched-chain fatty acids. When cells of this organism grown at 30 degrees C were cold shocked, viability and ability to secrete extracellular protease were lost. Growth of this organism at lower temperatures or addition of Tween 80 to cells caused the critical temperature zone for cold shocking to be lowered significantly. These results suggest a direct correlation between membrane fluidity and the susceptibility to cold shock.

Bacillus↗
PubMed1978

alpha-amylase from five strains of Bacillus amyloliquefaciens: evidence for identical primary structures.

The alpha-amylases from five strains of Bacillus amyloliquefaciens were compared to determine whether differences in primary structure are responsible for variations in catalytic properties previously reported among the enzymes. Amino acid analysis established virtually identical compositions for the proteins. Reaction with dimethylaminoaphthylene sulfonylchloride indicated the amino-terminal amino acid of each amylase to be valine. Carboxyl termini of the enzymes have been determined by digestion with carboxypeptidase A. The resulting kinetic data indicate tyrosine as the carboxyl terminus and leucine as the penultimate residue for all five proteins. Isoelectric focusing of the enzymes yielded isoelectric points in the pH range of 5.09 to 5.18. Tryptic digests of the enzymes chromatographed on a cation-exchange column showed identical elution patterns. It is concluded that the primary structure of the amylase from the five strains is identical or exhibits only conservative substitutions.

Amino Acids↗
PubMed1978

[Isolation and some properties of restriction endonuclease from Bacillus amyloliquefaciens].

A partially purified preparation of restriction endonuclease Bam I was isolated from the cells of Bacillus amyloliquefaciens. The purification procedure was a modification of a method described by Wilson and Young. Isolation and purification of the enzyme involved disruption of the cells by ultrasonication, treatment with streptomycin sulfate, fractionation by ammonium sulfate, chromatography on DEAE-cellulose and hydroxylapatite and rechromatography on DEAE-cellulose. Restrictase Bam I splits the linear double-chain DNA molecule of phage gamma into six fragments. The enzyme retained its stability under storage on the ice for 1,5--2 months in a Na- or K-phosphate buffer with beta-mercaptoethanol (10 mM).

Bacillus↗
PubMed1976

The restriction endonucleases in Bacillus amyloliquefaciens N strain. Substrate specificities.

Two species of restriction endonuclease were isolated by gel filtration and DEAE-cellulose chromatography from a cell-free extract of Bacillus amyloliquefaciens (B. subtilits) N strain; a lower molecular weight endonuclease (endonuclease R.BamNI) and a higher molecular-weight one (endonuclease R.BamNx). Both of them required only Mg2+ for their activities. Endonuclease R.BamNx introduced a larger number of site-specific scissions in Excherchia coli phage lambda DNA that endonuclease R.BamNI did. Endonuclease R.BamNx cleaved Bacillus phage phi 105C DNA at the specific sites which are classified into two groups: one type of sites is modified by B. amyloliquefaciens H strain in vivo while the other is not affected. It was also active on DNA'S OF E. coli phage T7, lambdadvl, Simian virus 40 (SV40) and colicinogenic factor ColEI and was inactive on DNAs of Bacillus phages phi 29 and M2. Endonuclease R.BamHI isolated from H strain by Wilson and Young. This endonuclease was active on DNAs of phage lambda, lambdadvl and SV40, adn was inactive on DNAs of phages phi 105C, phi 29, M2 and T7, and ColEI DNA.

Adenosine Triphosphate↗
PubMed1977

[Physicochemical properties of an extracellular polysaccharide isolated from culture media of Bacillus amyloliquefaciens].

A new extracellular polysaccharide has been isolated by chromatography on anion exchanger of a fraction obtained from highly viscous culture media of Bacillus amyloliquefaciens. This polysaccharide is characterised by high molecular weight (1,000,000 dalton) and intrinsic viscosity (323 ml/g). It contains 24% neutral sugar (galactose and mannose 5:1), 35% glucuronic acid and 51.5% N-acetylhexosamines (N-actylglucosamine, N-acetylgalactosamine and N-acetylbacillosamine 6:9:1).

Bacillus↗
PubMed1977

Human papillomavirus DNA: physical mapping of the cleavage sites of Bacillus amyloliquefaciens (BamI) and Haemophilus parainfluenzae (HpaII) endonucleases and evidence for partial heterogeneity.

The DNA of human papillomavirus (HPV) obtained from a pool of plantar warts is cleaved by bacillus amyloliquefaciens (BamI) and Haemophilus parainfluenzae (HpaII) restriction endonucleases at one and four specific sites, respectively. These sites were localized on the previously established cleavage map of HPV DNA, using the Hind, HindIII, HpaI, and EcoRI endonuclease restriction sites as reference. The four HpaII sites were mapped, clockwise, at 1.4, 41.1, 44.3, and 52.8% of the genome length from the unique BamI cleavage site taken as point zero. The HpaII site mapped at 1.4% of the genome length was absent in 40 to 50% of the molecules, thus showing a genetic heterogeneity of HPV DNA.

Bacillus↗
PubMedDate not supplied

[Effect of different carbon, nitrogen and phosphorus sources on the biosynthesis of proteases with coagulase activity by Bacillus subtilis var, amyloliquefaciens].

Proteolytic enzymes with coagulase activity were found in the cultural broth of Bacillus subtilis var. amyloliquefaciens 759 grown on chemically defined and natural media. The effect of various sources of carbon, nitrogen and phosphorus on biosynthesis of proteases with coagulase activity was studied; mineral and organic nitrogen sources were equally favourable for the growth and protease biosynthesis. The best sources of carbon for biosynthesis of the enzymes were glucose, sucrose, maltose, fructose, and sorbitol. Potassium salts of ortho-phosphoric acid were assimilated as a source of phosphorus.

Bacillus subtilis↗
PubMed1978

New chromogenic and fluorogenic substrates for pyrrolidonyl peptidase.

L-Pyroglutamyl derivatives of p-nitroaniline and 7-amino-4-methylcoumarin were synthesized as new sensitive substrates for pyrrolidonyl peptidase (pyrrolidonecarboxylyl peptidase) from Bacillus amyloliquefaciens. Their hydrolyses could be followed by conventional colorimetric and fluorometric procedures; i.e., in terms of the increase in absorbance at 410 nm caused by the liberation of p-nitroaniline and the emission at 440 nm after excitation at 370 nm depending on the liberation of 7-amino-4-methylcoumarin. Values of Km were estimated to be 0.69 mM for anilide substrate and 0.33 mM for methylcoumarin substrate in the pyrrolidonyl peptidase reaction at pH 8.0. The methylcoumarin compound was about one thousand fold more sensitive than the anilide substrate.

Aminopeptidases↗
PubMed1978

Purification and characterization of L-pyrrolidonecarboxylate peptidase from Bacillus amyloiliquefaciens.

Microorganisms capable of producing L-pyrrolidonecarboxylate peptidase [L-pyrrolidonyl peptidase, EC 3.4.11.8] were screened and a strain of Bacillus amyloliquefaciens was chosen as one of the most potent producers of the enzyme. The enzyme was purified from lysozyme-lysate of the bacterial cells by salting out with ammonium sulfate, adsorption on DEAE-cellulose, covalent chromatography on PCMB-Sepharose and by gel filtration on Sephadex G-150. By these procedures, the enzyme was purified about 800-fold with an activity recovery of 9%, and the preparation was electrophoretically homogenous. The enzyme was most active and stable at pH 7-8. The presence of 2-mercaptoethanol and EDTA was effective for stabilizing the enzyme. The molecular weight was estimated to be 72,000 by the gel filtration method and to be 24,000 by SDS-polyacrylamide gel electrophoresis, suggesting that the enzyme is a subunit oligomer, presumably trimer. The enzyme was inactivated by the addition of PCMB, sodium tetrathionate, Hg2+ and Cu2+, but the activity lost was restored by the addition of 2-mercaptoethanol and EDTA. The purified enzyme split amide and ester linkages in L-pyroglutamyl derivatives of L-alanine, beta-naphthylamine, alpha-naphthol, and 4-methylumbelliferone, but was completely inert towards various peptides and esters used as substrates for usual amino- and carboxy-peptidases, and for endopeptidases such as trypsin, subtilisin and alpha-chymotrypsin.

Aminopeptidases↗