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A protease-resistant α-galactosidase characterized by relatively acid pH tolerance from the Shitake Mushroom Lentinula edodes.

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A monomeric α-galactosidase with a molecular weight of 64 kDa was purified from fresh fruiting bodies of Lentinula edodes. The purification protocol involved ion-exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a final gel-filtration on Superdex 75. The purified

Antimicrobial activity of Bacillus subtilis and Bacillus pumilus during the fermentation of African locust bean (Parkia biglobosa) for Soumbala production.

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OBJECTIVE To examine predominant isolates of Bacillus subtilis and B. pumilus isolated from Soumbala for their antimicrobial activity against indicator microorganisms as Micrococcus luteus, Staphyloccocus aureus, Bacillus cereus, Enterococus facium, Listeria monocytogenes, Escherichia coli,

Genetic and biochemical characterization of a protease-resistant mesophilic β-mannanase from Streptomyces sp. S27.

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A β-mannanase gene, designated as man5S27, was cloned from Streptomyces sp. S27 using the colony polymerase chain reaction (PCR) method and expressed in Escherichia coli BL21 (DE3). The open reading frame consisted of 1,161 bp and encoded a 386-amino-acid polypeptide (Man5S27) with calculated

Novel low-temperature-active, salt-tolerant and proteases-resistant endo-1,4-β-mannanase from a new Sphingomonas strain.

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Sphingomonas sp. JB13, isolated from slag of a >20-year-old phosphate rock-stacking site, showed the highest 16S rDNA (1343bp) identity of 97.2% with Sphingomonas sp. ERB1-3 (FJ948169) and <97% identities with other identified Sphingomonas strains. A mannanase-coding gene (1191bp) was cloned and

Characterization of a Glycoside Hydrolase Family 27 α-Galactosidase from Pontibacter Reveals Its Novel Salt-Protease Tolerance and Transglycosylation Activity.

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α-Galactosidases are of great interest in various applications. A glycoside hydrolase family 27 α-galactosidase was cloned from Pontibacter sp. harbored in a saline soil and expressed in Escherichia coli. The purified recombinant enzyme (rAgaAHJ8) was little or not affected by 3.5-30.0% (w/v) NaCl,

Effect of boiling and roasting on the fermentation of soybeans into dawadawa (soy-dawadawa).

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Soybeans which had initially been dehulled by either boiling (boiled/dehulled) or roasting (roasted/dehulled) before peeling, were cooked and fermented into dawadawa, a traditional food condiment. The micropopulation, enzymatic activities, proximate composition, amino acid, and aroma profiles of the

Antioxidant dressing therapy versus standard wound care in chronic wounds (the REOX study): study protocol for a randomized controlled trial

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Background: A wound that does not heal in the orderly stages of the healing process or does not heal within 3 months is considered a chronic wound. Wound healing is impaired when the wound remains in the inflammatory stage for too long. A range of factors can delay

Evaluation of an endo-beta-mannanase produced by Streptomyces ipomoea CECT 3341 for the biobleaching of pine kraft pulps.

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An endo-beta-mannanase (EC 3.2.1.78) from Streptomyces ipomoea CECT 3341 was purified and applied to the biobleaching of pine kraft pulps. The maximum level of endo-beta-mannanase activity (0.6 units ml(-1)) was achieved after 4 days of growth in a medium containing locust bean gum and yeast

A Novel endo-1,4-β-mannanase from Bispora antennata with good adaptation and stability over a broad pH range.

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An endo-β-1,4-mannanase encoding gene, man5, was cloned from Bispora antennata CBS 126.38, which was isolated from a beech stump. The cDNA of man5 consists of 1,299 base pairs and encodes a 432-amino-acid protein with a theoretical molecular mass of 46.6 kDa. Deduced MAN5 exhibited the highest amino

A multi-tolerant low molecular weight mannanase from Bacillus sp. CSB39 and its compatibility as an industrial biocatalyst.

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Bacillus sp. CSB39, isolated from popular traditional Korean food (Kimchi), produced a low molecular weight, thermostable mannanase (MnCSB39); 571.14U/mL using locust bean gum galactomannan as a major substrate. It was purified to homogeneity using a simple and effective two-step purification

Optimization of Saccharomyces cerevisiae α-galactosidase production and application in the degradation of raffinose family oligosaccharides.

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α-Galactosidases are enzymes that act on galactosides present in many vegetables, mainly legumes and cereals, have growing importance with respect to our diet. For this reason, the use of their catalytic activity is of great interest in numerous biotechnological applications,

Acidic β-mannanase from Penicillium pinophilum C1: Cloning, characterization and assessment of its potential for animal feed application.

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The β-mannanase gene, man5C1, was cloned from Penicillium pinophilum C1, a strain isolated from the acidic wastewater of a tin mine in Yunnan, China, and expressed in Pichia pastoris. The sequence analysis displayed the gene consists of a 1221-bp open reading frame encoding a protein of 406 amino

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