Semi-rational engineering of glucosamine-6-phosphate deaminase for catalytic synthesis of glucosamine from D-fructose.

Glucosamine (GlcN), as one of the important derivatives of D-glucose, is formed by the substitution of the hydroxyl group at position 2 of glucose with an amino group. As a bioactive amino monosaccharide, GlcN is known for its various biological effects, including immune enhancement, antioxidant, anti-inflammatory, hepatoprotective, joint pain relief, and alleviation of osteoporosis. These properties highlight the broad applications of GlcN and its derivatives in pharmaceuticals, cosmetics, food production, and other fields, underscoring their promising prospects.

Engineering Glucosamine-6-Phosphate Synthase to Achieve Efficient One-Step Biosynthesis of Glucosamine.

As an important functional monosaccharide, glucosamine (GlcN) is widely used in fields such as medicine, food nutrition, and health care. Here, we report a distinct GlcN biosynthesis method that utilizes engineered glucosamine-6-phosphate synthase (GlmS) to convert D-fructose to directly generate GlcN. The best variant obtained by using a combinatorial active-site saturation test/iterative saturation mutagenesis (CAST/ISM) strategy was a quadruple mutant S596D/V597G/S347H/G299Q (GlmS-BK19), which has a catalytic activity 1736-fold that of the wild type toward D-fructose.

Simultaneous removal of tetracycline and sulfamethoxazole by laccase-mediated oxidation and ferrate(VI) oxidation: the impact of mediators and metal ions.

This study explores the impact of mediators and metal ions of laccase-mediated oxidation and ferrate(VI) oxidation for the simultaneous removal of tetracycline antibiotics (TCs) and sulfonamide antibiotics (SAs) and to effectively remove their antimicrobial activity. The results showed that the antimicrobial activity of tetracycline against Bacillus altitudinis and Escherichia coli was significantly reduced, and the antimicrobial activity of sulfamethoxazole against B. altitudinis disappeared completely after treatment with the laccase-ABTS system.

Improving the decolorization activity of Bacillus pumilus W3 CotA-laccase to Congo Red by rational modification.

Congo Red (CR) is a typical azo dye with highly toxic and carcinogenic properties. This study aimed to improve the decolorization activity of Bacillus pumilus W3 CotA-laccase for azo dye CR. This work analyzed the interaction between CotA-laccase and CR based on homology modeling and molecular docking.

Development and characterization of a halo-thermophilic bacterial consortium for decolorization of azo dye.

Textile wastewater is characterized by high salinity and high temperature, and azo dye decolorization by mixed cultures under extreme salinity and thermophilic environments has received little attention. High salinity and temperature inhibit the biodecolorization efficiency in textile wastewater. In the present study, a halo-thermophilic bacterial consortium (HT1) that can decolorize azo dye at 10% salinity and 50 °C was enriched.

Cold atmospheric plasma increases IBRV titer in MDBK cells by orchestrating the host cell network.

Enhancing virus multiplication could assist in the rapid production of vaccines against viral diseases. Cold atmospheric plasma (CAP), a physical approach relying on reactive oxygen species to achieve the desirable cellular outcome, was shown to be effective in enhancing virus propagation, where bovine rhinotrachieitis virus and Madin-Darby Bovine Kidney cells were used as the modeling virus and cell line, respectively. CAP was shown to create synergies with virus infection in arresting host cells at the G2/M stage, decreasing cell membrane potential, increasing intracellular calcium level, and inducing selective autophagy.

Enhancing the decolorization activity of Bacillus pumilus W3 CotA-laccase to Reactive Black 5 by site-saturation mutagenesis.

Reactive Black 5 (RB5) is a typical refractory azo dye. Widespread utilization of RB5 has caused a variety of environmental and health problems. The enzymatic degradation of RB5 can be a promising solution due to its superiority as an eco-friendly and cost-competitive process.

Decolorization and detoxification of azo dye by halo-alkaliphilic bacterial consortium: Systematic investigations of performance, pathway and metagenome.

The high pH and salinity of textile wastewater is a major hindrance to azo dye decolorization. In this study, a mixed bacterial consortium ZW1 was enriched under saline (10% salinity) and alkaline (pH 10.0) conditions to decolorize Methanil Yellow G (MY-G).

Improving the catalytic thermostability of W3 ω-transaminase by proline substitutions.

As a green biocatalyst, transaminase with high thermostability can be better employed to synthesize many pharmaceutical intermediates in industry. To improve the thermostability of ()-selective amine transaminase from W3, related mutation sites were determined by multiple amino acid sequence alignment between wild-type ω-transaminase and four potential thermophilic ω-transaminases, followed by replacement of the related amino acid residues with proline by site-directed mutagenesis. Three stabilized mutants (D192P, T237P, and D192P/T237P) showing the highest stability were obtained and used for further analysis.

Recombinant Horseradish Peroxidase C1A Immobilized on Hydrogel Matrix for Dye Decolorization and Its Mechanism on Acid Blue 129 Decolorization.

In this study, horseradish peroxidase C1A (HRP C1A) from Armoracia rusticana was expressed in Escherichia coli as an inclusion body. Subsequently, an active recombinant HRP C1A was obtained by refolding gradually using dilution-ultrafiltration. The recombinant HRP C1A was immobilized on agarose-chitosan hydrogel at 86.

Extracellular expression of mutant CotA-laccase SF in Escherichia coli and its degradation of malachite green.

In this study, mutant CotA-laccase SF was successfully expressed in Escherichia coli by co-expression with phospholipase C. The optimized extracellular expression of CotA-laccase SF was 1257.22 U/L.

Gut microbiota of red swamp crayfish Procambarus clarkii in integrated crayfish-rice cultivation model.

Increasing evidences suggest that intestinal microbiota balance closely correlated with host's health status could affected by external environment. Integrated crayfish-rice cultivation model is a highly efficient artificial ecosystem widely practiced in subtropical China. Less information is available to estimate the influence response to the micro-ecology of crayfish intestine and so as to influence the biological processes.

Characterization of a novel carboxylesterase from Bacillus velezensis SYBC H47 and its application in degradation of phthalate esters.

Recently, residual plasticizer phthalate esters (PAEs) in the different environments pose a serious health threat to humans and mammals. Biodegradation has been considered a promising and eco-friendly way to eliminate PAEs. In this study, a gene (baces04) encoding the novel PAEs hydrolase, carboxylesterase (BaCEs04), was screened from the genome of Bacillus velezensis SYBC H47 via bioinformatics analysis.

Mining of alkaline proteases from Bacillus altitudinis W3 for desensitization of milk proteins: Their heterologous expression, purification, and characterization.

In this study, three active alkaline proteases (AprEs) (BaApr1, BaApr2, and BaApr9) from Bacillus altitudinis W3 were obtained through bioinformatics analysis and verification. Multiple sequence alignment showed low identity of 64.60% and suggested that the three AprEs belonged to the S8A subfamily of serine proteases.

Evaluation of the Strain YP6 in Phoxim Degradation via Transcriptomic Data and Product Analysis.

Phoxim, a type of organophosphorus pesticide (OP), is widely used in both agriculture and fisheries. The persistence of phoxim has caused serious environmental pollution problems. In this study, YP6 (YP6), which is capable of promoting plant growth and degrading broad-spectrum OPs, was used to study phoxim degradation.

Enhancement in catalytic activity of CotA-laccase from Bacillus pumilus W3 via site-directed mutagenesis.

CotA-laccases are potential enzymes that are widely used in decolorization of dyes and degradation of toxic substances. In this study, a novel CotA-laccase gene from Bacillus pumilus W3 was applied for rational design. After a series of site-directed genetic mutations, the mutant S208G/F227A showed a 5.

Characterization of a robust cold-adapted and thermostable laccase from Pycnoporus sp. SYBC-L10 with a strong ability for the degradation of tetracycline and oxytetracycline by laccase-mediated oxidation.

A native laccase (Lac-Q) with robust cold-adapted and thermostable characteristics from the white-rot fungus Pycnoporus sp. SYBC-L10 was purified, characterized, and used in antibiotic treatments. Degradation experiments revealed that Lac-Q at 10.

Comparison of aminotransferases of three Bacillus strains Bacillus altitudinis W3, Bacillus velezensis SYBC H47, and Bacillus amyloliquefaciens YP6 via genome analysis and bioinformatics.

Aminotransferases have attracted considerable attention due to their extraordinary potential for the biosynthesis of chiral amines. Research on transaminase genes can facilitate their application to various fields. Herein, 89 putative aminotransferase genes potentially encoding useful biocatalysts were identified in three Bacillus strains genomes by genome annotation.

Effect of residue substitution via site-directed mutagenesis on activity and steroselectivity of transaminase BpTA from Bacillus pumilus W3 for sitafloxacin hydrate intermediate.

Aminotransferases are widely employed as biocatalysts for the asymmetric synthesis of biologically active pharmaceuticals. Transaminase BpTA from Bacillus pumilus W3 can accept a broad spectrum of sterically demanding substrates, but it does not process the key five-membered ring intermediate of sitafloxacin. In the present study, we rationally constructed numerous single-point mutants and six multi-point mutants by combining the structural characteristics of transaminase and its substrates.

The effects of phytoremediation on soil bacterial communities in an abandoned mine site of rare earth elements.

Overexploitation of rare earth elements (REEs) has caused serious desertification and environmental pollution. The ecological restoration of mining areas has attracted increasing attention in China. Soil microbiota is important for successful ecological remediation of abandoned mine land.

An alkaline phosphatase from Bacillus amyloliquefaciens YP6 of new application in biodegradation of five broad-spectrum organophosphorus pesticides.

In recent decades, biodegradation has been considered a promising and eco-friendly way to eliminate organophosphorus pesticides (OPs) from the environment. To enrich current biodegrading-enzyme resources, an alkaline phosphatase (AP3) from Bacillus amyloliquefaciens YP6 was characterized and utilized to test the potential for new applications in the biodegradation of five broad-spectrum OPs. Characterization of AP3 demonstrated that activity was optimal at 40 °C and pH 10.

Mining of aminotransferase gene ota3 from Bacillus pumilus W3 via genome analysis, gene cloning and expressing for compound bioamination.

Aminotransferases are widely employed as biocatalysts to produce chiral amines and biologically active pharmaceuticals via asymmetric synthesis. In this study, transaminase genes in the Bacillus pumilus W3 genome were analysed, and gene ota3 encoding a putative (R)-selective transaminase was identified. The sequence of ota3 shares highest sequence identity (24.

Fe(III)-based immobilized metal-affinity chromatography (IMAC) method for the separation of the catechol siderophore from CD36.

Catechol siderophore plays an important role in microbial ecology, agriculture, and medicine, but its research is often limited by the difficulty in acquisition of it in large quantities. Based on evidence from the coordination chemistry and chemical biology, catechol siderophore could chelate Fe with high affinity. Therefore, Fe(III)-based immobilized metal-affinity chromatography (IMAC) was applied to capture siderophore from the culture filtrate of CD36.

Bacterial laccases: promising biological green tools for industrial applications.

Multicopper oxidases (MCOs) are a pervasive family of enzymes that oxidize a wide range of phenolic and nonphenolic aromatic substrates, concomitantly with the reduction of dioxygen to water. MCOs are usually divided into two functional classes: metalloxidases and laccases. Given their broad substrate specificity and eco-friendliness (molecular oxygen from air as is used as the final electron acceptor and they only release water as byproduct), laccases are regarded as promising biological green tools for an array of applications.

Isolation of β-1,3-Glucanase-Producing Microorganisms from Cultivation Soil via Molecular Biology.

β-1,3-Glucanase is considered as a useful enzymatic tool for β-1,3-glucan degradation to produce (1→3)-linked β-glucan oligosaccharides with pharmacological activity properties. To validly isolate β-1,3-glucanase-producing microorganisms, the soil of considered an environment rich in β-1,3-glucan-degrading microorganisms, was subjected to high throughput sequencing. The results demonstrated that the genera (1.