Characterization of an organic solvent-tolerant polysaccharide lyase from Microbulbifer thermotolerans DAU221.

Alginate and its derivatives are annually produced approximately 30,000 tons or more and are applied to various industries as they are natural polymers. The global market for alginate and its derivatives has been growing steadily. There is little research compared to other enzymes produced through biomass degradation or modification.

Cloning, purification, and characterization of GH3 -glucosidase, MtBgl85, from DAU221.

Background: -Glucosidases have attracted considerable attention due to their important roles in various biotechnological processes such as cellulose degradation to make energy and hydrolysis of isoflavone. () is isolated from deep-sea sediment and has not been researched much yet. As a potential candidate for a variety of biotechnological industries, -glucosidases from the novel bacterial species should be researched extensively.

Cloning, purification, and characterization of an organic solvent-tolerant chitinase, MtCh509, from DAU221.

Background: The ability to use organic solvents in enzyme reactions offers a number of industrially useful advantages. However, most enzymes are almost completely inactive in the presence of organic solvents. Thus, organic solvent-tolerant enzymes have potential applications in industrial processes.

Complete genome sequence and analysis of three kinds of β-agarase of Cellulophaga lytica DAU203 isolated from marine sediment.

Cellulophaga lytica DAU203 (KACC 19187), isolated from the marine sediment in Korea, has a strong ability to degrade agar. The genome of C. lytica DAU203 contains a single chromosome that is 3,952,957bp in length, with 32.

Complete genome sequence of cold-adapted enzyme producing Microbulbifer thermotolerans DAU221.

Microbulbifer thermotolerans DAU221 was preliminary isolated from the marine sediment samples in the Republic of Korea. Here, we present the complete genome sequence of M. thermotolerans DAU221, which consisted of 3,938,396 base pairs with a GC content of 56.

Characterization of maltotriose production by hydrolyzing of soluble starch with α-amylase from Microbulbifer thermotolerans DAU221.

A maltotriose-producing α-amylase, AmyA, from a newly isolated bacterial strain Microbulbifer thermotolerans DAU221 was purified and characterized in the heterologous host, Escherichia coli, using the pCold I vector. The amyA gene encoded a 761-residue protein composed of a 33 amino acid secretion signal peptide. The purified α-amylase with a molecular mass of 80 kDa, approximately, shared a sequence motif characteristic of the glycoside hydrolase family 13.

A cold-adapted carbohydrate esterase from the oil-degrading marine Bacterium Microbulbifer thermotolerans DAU221: gene cloning, purification, and characterization.

A cold-adapted carbohydrate esterase, CEST, belonging to the carbohydrate esterase family 6, was cloned from Microbulbifer thermotolerans DAU221. CEST was composed of 307 amino acids with the first 22 serving as a secretion signal peptide. The calculated molecular mass and isoelectric point of the mature enzyme were 31,244 Da and pH 5.

Characterization of a cold-active β-glucosidase from Paenibacillus xylanilyticus KJ-03 capable of hydrolyzing isoflavones daidzin and genistin.

Paenibacillus xylanilyticus KJ-03 isolated from konjac field, showed β-glucosidase activity on tryptic soy agar plate supplemented with 0.1 % esculin and 0.25 % ferric ammonium citrate.

Hydrolysis of isoflavone glycoside by immobilization of β-glucosidase on a chitosan-carbon in two-phase system.

We explored a method to examine the hydrolysis of isoflavone glycoside by immobilizing β-glucosidase on chitosan-carbon beads in an aqueous-organic two-phase system. The chitosan-carbon beads were cross-linked with glutaraldehyde to immobilize β-glucosidase from Exiguobacterium sp. DAU5.

Cloning and characterization of a new broadspecific β-glucosidase from Lactococcus sp. FSJ4.

A β-glucosidase gene bglX was cloned from Lactococcus sp. FSJ4 by the method of shotgun. The bglX open reading frame consisted of 1,437 bp, encoding 478 amino acids.

An β-1,4-xylanase with exo-enzyme activity produced by Paenibacillus xylanilyticus KJ-03 and its cloning and characterization.

Paenibacillus xylanilyticus KJ-03 was isolated from soil samples obtained from a field with Amorphophallus konjac plants. A gene encoding xylanase was isolated from KJ-03 and cloned using a fosmid library. The xynA gene encodes xylanase; it consists of 1,035 bp and encodes 345 amino acids.

Recombinant expression and characterization of an organic-solvent-tolerant α-amylase from Exiguobacterium sp. DAU5.

The enzyme from halophilic microorganisms often has unique properties such as organic-solvent-tolerance. In this study, a novel organic-solvent-tolerant α-amylase gene was cloned from the mild halophile Exiguobacterium sp. DAU5.

β-cyclodextrin production by the cyclodextrin glucanotransferase from Paenibacillus illinoisensis ZY-08: cloning, purification, and properties.

The gene encoding the cyclodextrin glucanotransferase (CGTase, EC2.4.1.

Gene cloning of endoglucanase Cel5A from cellulose-degrading Paenibacillus xylanilyticus KJ-03 and purification and characterization of the recombinant enzyme.

The bacterial strain Paenibacillus xylanilyticus KJ-03 was isolated from a sample of soil used for cultivating Amorphophallus konjac. The cellulase gene, cel5A was cloned using fosmid library and expressed in Escherichia coli BL21 (trxB). The cel5A gene consists of a 1,743 bp open reading frame and encodes 581 amino acids of a protein.

Cyclodextrin glycosyltransferase encoded by a gene of Paenibacillus azotofixans YUPP-5 exhibited a new function to hydrolyze polysaccharides with β-1,4 linkage.

The bacteria with hydrolysis activity to glucomannan were isolated from the rhizosphere of Amorphophallus konjac through enrichment cultivation. One strain with strong activity in degrading glucomannan was identified preliminarily as Paenibacillus azotofixans YUPP-5 according to the sequence analysis of 16S rDNA. This strain is able to hydrolyze many polysaccharide with β-1,4 linkage, including glucomannan, galactomannan, xylan, carboxymethyl cellulose, and chitin.

Salinomycin-induced apoptosis of human prostate cancer cells due to accumulated reactive oxygen species and mitochondrial membrane depolarization.

The anticancer activity of salinomycin has evoked excitement due to its recent identification as a selective inhibitor of breast cancer stem cells (CSCs) and its ability to reduce tumor growth and metastasis in vivo. In prostate cancer, similar to other cancer types, CSCs and/or progenitor cancer cells are believed to drive tumor recurrence and tumor growth. Thus salinomycin can potentially interfere with the end-stage progression of hormone-indifferent and chemotherapy-resistant prostate cancer.

Molecular cloning, purification and characterization of thermostable beta-1,3-1,4 glucanase from Bacillus subtilis A8-8.

A gene encoding a beta-1,3-1,4-glucanase (CelA) belonging to family 5 of glycoside hydrolases was cloned and sequenced from the Bacillus subtilis A8-8. The open-reading-frame of celA comprised 1499 base pairs and the enzyme was composed of 500 amino acids with a molecular mass of 55 kDa. The recombinant beta-1,3-1,4 glucanase was purified by GST-fusion purification system.

Gene cloning, purification, and characterization of a cold-adapted lipase produced by Acinetobacter baumannii BD5.

Acinetobacter baumannii BD5 was isolated from waters of Baek-du mountain, and the lipase gene was cloned using a PCR technique. The deduced amino acid sequence of the lipase and lipase chaperone were found to encode proteins of 325 aa and 344 aa with a molecular mass of 35 kDa and 37 kDa, respectively. The lipase gene was cloned and expressed in Escherichia coli BL21 (trxB) as an inclusion body, which was subsequently solubilized by urea, and then purified using Ni-affinity chromatography.

Novel roles of Bacillus thuringiensis to control plant diseases.

Bacillus thuringiensis is well known as an effective bio-insecticidal bacterium. However, the roles of B. thuringiensis to control plant diseases are not paid great attention to.

Solubilization of insoluble inorganic phosphate by Burkholderia cepacia DA23 isolated from cultivated soil.

A mineral phosphate solubilizing bacterium, Burkholderia cepacia DA23 has been isolated from cultivated soils. Phosphate-solubilizing activities of the strain against three types of insoluble phosphate were quantitatively determined. When 3% of glucose concentration was used for carbon source, the strain had a marked mineral phosphate-solubilizing activity.

Discovery of three novel lipase ( lipA1 , lipA2 , and lipA3) and lipase-specific chaperone ( lipB) genes present in Acinetobacter sp. DYL129.

A microbe isolated from a soil sample obtained on Deog-yu Mountain in Korea, was found to produce an extracellular lipase. This microbe, which was designated as DYL129, was identified as an Acinetobacter sp. based on phylogenetic analysis of its 16S rDNA.

Characterization of new biosurfactant produced by Klebsiella sp. Y6-1 isolated from waste soybean oil.

To obtain predominant bacteria degrading crude oil, we isolated some bacteria from waste soybean oil. Isolated bacterial strain had a marked tributyrin (C4:0) degrading activity as developed clear zone around the colony after incubation for 24h at 37 degrees C. It was identified as Klebsiella sp.

Isolation and structural analysis of bamylocin A, novel lipopeptide from Bacillus amyloliquefaciens LP03 having antagonistic and crude oil-emulsifying activity.

Bacillus amyloliquefaciens strain LP03 isolated from soil, produced an antagonistic compound that strongly inhibited the growth of plant-pathogenic fungi and a lipopeptide biosurfactant. Also, isolated strain LP03 had a marked crude oil-emulsifying activity as it developed a clear zone around the colony after incubation for 24 h at 37 degrees C. LP03 was identified as Bacillus amyloliquefaciens by analysis of partial 16 S rRNA gene and partial gyrA gene sequence.

Cloning, purification, and characterization of chitinase from Bacillus sp. DAU101.

A chitinase encoding gene from Bacillus sp. DAU101 was cloned in Escherichia coli. The nucleotide sequencing revealed a single open reading frame containing 1781 bp and encoding 597 amino acids with 66 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram.

Overexpression and characterization of a novel chitinase gene from a marine bacterium Pseudomonas sp. BK1.

The chitinase A (ChiA)-coding gene of Pseudomonas sp. BK1, which was isolated from a marine red alga Porphyra dentata, was cloned and expressed in Escherichia coli. The structural gene consists of 1602 bp encoding a protein of 534 amino acids, with a predicted molecular weight of 55,370 Da.