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1.
BackgroundXylanase from bacteria finds use in prebleaching process and bioconversion of lignocelluloses into feedstocks. The xylanolytic enzyme brings about the hydrolysis of complex biomolecules into simple monomer units. This study aims to optimize the cellulase-free xylanase production and cell biomass of Bacillus tequilensis strain ARMATI using response surface methodology (RSM).ResultsStatistical screening of medium constituents and the physical factors affecting xylanase and biomass yield of the isolate were optimized by RSM using central composite design at N = 30, namely 30 experimental runs with 4 independent variables. The central composite design showed 3.7 fold and 1.5 fold increased xylanase production and biomass yield of the isolate respectively compared to ‘one factor at a time approach’, in the presence of the basal medium containing birchwood xylan (1.5% w/v) and yeast extract (1% w/v), incubated at 40°C for 24 h. Analysis of variance (ANOVA) revealed high coefficient of determination (R2) of 0.9978 and 0.9906 for the respective responses at significant level (p < 0.05). The crude xylanase obtained from the isolate showed stability at high temperature (60°C) and alkaline condition (pH 9) up to 4 h of incubation.ConclusionsThe cellulase-free xylanase showed an alkali-tolerant and thermo-stable property with potentially applicable nature at industrial scale. This statistical approach established a major contribution in enzyme production from the isolate by optimizing independent factors and represents a first reference on the enhanced production of thermo-alkali stable cellulase-free xylanase from B. tequilensis. 相似文献
2.
BackgroundLarge amounts of β-alanine are required in fine chemical and pharmaceutical synthesis and other fields. Profitable and green methods are required for the industrial production of β-alanine.ResultsReplacing endogenous panD of Escherichia coli with heterologous CgpanD from Corynebacterium glutamicum enabled β-alanine synthesis of 0.67 g/L by strain B0016-082BB. Overexpressing CgpanD on both plasmids and chromosomes to enhance the rate-limiting step improved the β-alanine titer to 4.25 g/L in strain B0016-083BB/pPL451-panD with a slighter metabolic burden. Growth factors were introduced by addition of yeast extract, and 6.65 g/L of β-alanine was synthesized by strain B0016-083BB/pPL451-panD in the M9-3Y medium.ConclusionsEnhancement of the rate-limiting steps in the β-alanine biosynthetic pathway, recruitment of the temperature-sensitive inducible pL promoter, and optimization of the fermentation process could efficiently increase β-alanine production in E. coli.How to cite: Xua J, Zhua Y, Zhou Z. Systematic engineering of the rate-limiting step of β-alanine biosynthesis in Escherichia col. Electron J Biotechnol 2021;51. https://doi.org/10.1016/j.ejbt.2021.03.002. 相似文献
3.
BackgroundPhospholipase D (PLD) is used as the biocatalyst for phosphatidylserine (PS) production. In general, PLD was expressed in insoluble form in Escherichia coli. High-level soluble expression of PLD with high activity in E. coli is very important for industrial production of PLD.ResultsStreptomyces chromofuscus PLD coding gene was codon-optimized, cloned without signal peptide, and expressed in E. coli. The optimal recombinant E. coli pET-28a+PLD/BL21(DE3) was constructed with pET-28a without His-tag. The highest PLD activity reached 104.28 ± 2.67 U/mL in a 250-mL shake flask after systematical optimization. The highest PLD activity elevated to 122.94 ± 1.49 U/mL by feeding lactose and inducing at 20°C after scaling up to a 5.0-L fermenter. Substituting the mixed carbon source with 1.0 % (w/v) of cheap dextrin and adding a feeding medium could still attain a PLD activity of 105.81 ± 2.72 U/mL in a 5.0-L fermenter. Fish peptone from the waste of fish processing and dextrin from the starch are both very cheap, which were found to benefit the soluble PLD expression.ConclusionsAfter combinatorial optimization, the high-level soluble expression of PLD was fulfilled in E. coli. The high PLD activity along with cheap medium obtained at the fermenter level can completely meet the requirements of industrial production of PLD.How to cite: Wu R, Cao J, Liu F, et al. High-level soluble expression of phospholipase D from Streptomyces chromofuscus in Escherichia coli by combinatorial optimization. Electron J Biotechnol 2021;50.https://doi.org/10.1016/j.ejbt.2020.12.002 相似文献
4.
BackgroundThere is a large amount of industrial wastewater produced by the mushroom industry during the canning processing each year, which could provide abundant carbon, nitrogen and inorganic salts for microbial growth. The aim of this study was to optimize the culture conditions for Bacillus licheniformis cultured in the Agaricus bisporus industrial wastewater to produce the agricultural microbial fertilizer.ResultsIn this work, the maximal biomass of B. licheniformis could be obtained under the following culture conditions: 33.7°C, pH 7.0, 221 rpm shaking speed, 0.5% wastewater, 2 (v:v, %) inoculum dose, loading liquid of 60 mL/250 mL and a culture time of 24 h, and the average experimental value obtained was 1.35 ± 0.04 × 109 Obj/mL, which was within the 95% confidence interval of the predicted model (1.29–1.38 × 109 Obj/mL), and met the national microbial fertilizers' standard in China. Furthermore, the field experiment results showed that the fermentation broth of B. licheniformis could significantly improve the yield of Anoectochilus roxburghii.ConclusionsAgaricus bisporus industrial wastewater can be used to produce agricultural microbial fertilizer.How to cite: Huang J, Huang A, Lu L, et al. Improving the yield of Anoectochilus roxburghii by Bacillus licheniformis cultured in Agaricus bisporus industrial wastewater. Electron J Biotechnol 2020;48. https://doi.org/10.1016/j.ejbt.2020.08.002. 相似文献
5.
BackgroundCurrently, microbial fermentation method has become the research hotspot for acetoin production. In our previous work, an acetoin-producing strain, Bacillus subtilis SF4-3, was isolated from Japanese traditional fermented food natto. However, its conversion of glucose to acetoin was relatively low. In order to achieve a high-efficient accumulation of acetoin in B. subtilis SF4-3, main medium components and fermentation conditions were evaluated in this work.ResultsThe by-products analysis showed that there existed reversible transformation between acetoin and 2,3-butanediol that was strictly responsible for acetoin production in B. subtilis SF4-3. The carbon sources, nitrogen sources and agitation speed were determined to play crucial role in the acetoin production. The optimal media (glucose·H2O 150 g/L, yeast extract 10 g/L, corn steep dry 5 g/L, urea 2 g/L, K2HPO4 0.5 g/L, MgSO4 0.5 g/L) were obtained. Furthermore, the low agitation speed of 300 r/min was found to be beneficial to the reversible transformation of 2,3-butanediol for acetoin production in B. subtilis SF4-3. Eventually, 48.9 g/L of acetoin and 5.5 g/L of 2,3-butanediol were obtained in a 5-L fermenter, and the specific production of acetoin was 39.12% (g/g), which accounted for 79.90% of the theoretical conversion.ConclusionsThe results indicated acetoin production of B. subtilis SF4-3 was closely related to the medium components and dissolved oxygen concentrations. It also provided a method for acetoin production via the reversible transformation of acetoin and 2,3-butanediol. 相似文献
6.
BackgroundThis work studied how the exposure to an unusual substrate forced a change in microbial populations during anaerobic fermentation of crude glycerol, a by-product of biodiesel production, with freshwater sediment used as an inoculum.ResultsThe microbial associations almost completely (99.9%) utilized the glycerol contained in crude glycerol 6 g L−1 within four days, releasing gases, organic acids (acetic, butyric) and alcohols (ethanol, n-butanol) under anaerobic conditions. In comparison with control medium without glycerol, adding crude glycerol to the medium increased the amount of ethanol and n-butanol production and it was not significantly affected by incubation temperature (28 °C or 37 °C), nor incubation time (4 or 8 d), but it resulted in reduced amount of butyric acid. Higher volume of gas was produced at 37 °C despite the fact that the overall bacterial count was smaller than the one measured at 20 °C. Main microbial phyla of the inoculum were Actinobacteria, Proteobacteria and Firmicutes. During fermentation, significant changes were observed and Firmicutes, especially Clostridium spp., began to dominate, and the number of Actinobacteria and Gammaproteobacteria decreased accordingly. Concentration of Archaea decreased, especially in medium with crude glycerol. These changes were confirmed both by culturing and culture-independent (concentration of 16S rDNA) methods.ConclusionsCrude glycerol led to the adaptation of freshwater sediment microbial populations to this substrate. Changes of microbial community were a result of a community adaptation to a new source of carbon.How to cite: Paiders M, Nikolajeva V, Makarenkova G, et al. Changes in freshwater sediment microbial populations during fermentation of crude glycerol. Electron J Biotechnol 2021;49. https://doi.org/10.1016/j.ejbt.2020.10.007 相似文献
7.
BackgroundEndoglucanase plays a major role in initiating cellulose hydrolysis. Various wild-type strains were searched to produce this enzyme, but mostly low extracellular enzyme activities were obtained. To improve extracellular enzyme production for potential industrial applications, the endoglucanase gene of Bacillus subtilis M015, isolated from Thai higher termite, was expressed in a periplasmic-leaky Escherichia coli. Then, the crude recombinant endoglucanase (EglS) along with a commercial cellulase (Cel) was used for hydrolyzing celluloses and microbial hydrolysis using whole bacterial cells.ResultsE. coli Glu5 expressing endoglucanase at high levels was successfully constructed. It produced EglS (55 kDa) with extracellular activity of 18.56 U/mg total protein at optimal hydrolytic conditions (pH 4.8 and 50°C). EglS was highly stable (over 80% activity retained) at 40–50°C after 100 h. The addition of EglS significantly improved the initial sugar production rates of Cel on the hydrolysis of carboxymethyl cellulose (CMC), microcrystalline cellulose, and corncob about 5.2-, 1.7-, and 4.0-folds, respectively, compared to those with Cel alone. E. coli Glu5 could secrete EglS with high activity in the presence of glucose (1% w/v) and Tween 80 (5% w/v) with low glucose consumption. Microbial hydrolysis of CMC using E. coli Glu5 yielded 26 mg reducing sugar/g CMC at pH 7.0 and 37°C after 48 h.ConclusionsThe recombinant endoglucanase activity improved by 17 times compared with that of the native strain and could greatly enhance the enzymatic hydrolysis of all studied celluloses when combined with a commercial cellulase. 相似文献
8.
BackgroundJuvenile Yoshitomi tilapia is often infected by pathogens and results in low-level survival rate. Bacillus subtilis, as a probiotic, may have beneficial effects on Y. tilapia with compound 1-deoxynojirimycin (DNJ), which has antibacterial activities. The effects of dietary probiotic supplementation on Y. tilapias were evaluated.ResultsJuvenile Y. tilapia was fed with B. subtilis for 56 d. Y. tilapia was infected by Aeromonas hydrophila and survival rate was compared. Dietary B. subtilis increased weight gain rate, specific growth, food conversion ratios and food intake rate of Y. tilapia. The diet improved the cumulative survival rate (CSR) of juvenile Y. tilapia when the concentration of B. subtilis was more than 2.05 × 1010 cfu/kg and CSR reached a maximum rate when the concentration of bacillus was 4.23 × 1010 (P < 0.05). Meanwhile, B. subtilis improved total antioxidant capacity (TAC), spleen index, the activities of serum lysozyme, alkaline phosphatase (ALP), superoxide dismutase (SOD) and catalase (CAT) (P < 0.05). In contrast, B. subtilis reduced serum aspartate aminotransferase (AST), alanine aminotransferase (ALT), malondialdehyde (MDA) and C3 complement (P < 0.05). DNJ was isolated from secondary metabolisms and proved to increase the levels of SOD, CAT and reduce the levels of AST, ALT and MDA at cell levels. After A. hydrophila infection, DNJ prevented the reduction in survival rate of Y. tilapia (P < 0.05).Conclusions1-Deoxynojirimycin from Bacillus subtilis can be used to improve the growth performance of juvenile Y. tilapia by affecting its antioxidant and antibacterial activities. 相似文献
9.
BackgroundCatalase (CAT) is an important enzyme that degrades H2O2 into H2O and O2. To obtain an efficient catalase, in this study, a new strain of high catalase-producing Serratia marcescens, named FZSF01, was screened and its catalase was purified and characterized.ResultsAfter optimization of fermentation conditions, the yield of catalase produced by this strain was as high as 51,468 U/ml. This catalase was further purified using two steps: DEAE-fast flow and Sephedex-G150. The purified catalase showed a specific activity of 197,575 U/mg with a molecular mass of 58 kDa. This catalase exhibited high activity at 20–70°C and pH 5.0–11.0. Km of the catalase was approximately 68 mM, and Vmax was 1886.8 mol/min mg. This catalase was further identified by LC–MS/MS, and the encoding gene was cloned and expressed in Escherichia coli BL21 (DE3) with a production of 17,267 ± 2037 U/ml.ConclusionsTo our knowledge, these results represent one of the highest fermentation levels reported among current catalase-producing strains. This FZSF01 catalase may be suitable for several industrial applications that comprise exposure to alkaline conditions and under a wide range of temperatures. 相似文献
10.
《Electronic Journal of Biotechnology》2014,17(2):89-94
BackgroundAspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, especially in the food processing industry. Here we describe a novel aspartic protease that was purified from Peptidase R, a commercial protease preparation derived from Rhizopus oryzae.ResultsAn aspartic protease sourced from Peptidase R was purified to homogeneity by anion exchange chromatography followed by polishing with a hydrophobic interaction chromatography column, resulting in a 3.4-fold increase in specific activity (57.5 × 103 U/mg) and 58.8% recovery. The estimated molecular weight of the purified enzyme was 39 kDa. The N-terminal sequence of the purified protein exhibited 63–75% identity to rhizopuspepsins from various Rhizopus species. The enzyme exhibited maximal activity at 75°C in glycine–HCl buffer, pH 3.4 with casein as the substrate. The protease was stable at 35°C for 60 min and had an observed half-life of approximately 30 min at 45°C. Enzyme activity was not significantly inhibited by chelation with ethylenediamine tetraacetic acid (EDTA), and the addition of metal ions to EDTA-treated protease did not significantly change enzyme activity, indicating that proteolysis is not metal ion-dependent. The purified enzyme was completely inactivated by the aspartic protease inhibitor Pepstatin A.ConclusionBased on the observed enzyme activity, inhibition profile with Pepstatin A, and sequence similarity to other rhizopuspepsins, we have classified this enzyme as an aspartic protease. 相似文献
11.
BackgroundMucor indicus is a dimorphic fungus used in the production of ethanol, oil, protein, and glucosamine. It can ferment different pentoses and hexoses; however, the yields of products highly depend on the nutrients and cultivation conditions. In this study, the effects of different morphologic forms, cultivation time and temperature, presence or absence of oxygen, carbon sources, and concentration of nitrogen source on the products of M. indicus were investigated.ResultsThe fungus with all morphologies produced high yields of ethanol, in the range of 0.32–0.43 g/g, on glucose. However, the fungus with filamentous morphology produced higher amounts of oil, protein, phosphate, and glucosamine together with ethanol, compared with other morphologies. A higher amount of oil (0.145 g/g biomass) was produced at 28°C, while the best temperature for protein and glucosamine production was 32 and 37°C, respectively. Although ethanol was produced at a higher yield (0.44 g/g) under anaerobic conditions compared with aerobic conditions (yield of 0.41 g/g), aerobic cultivation resulted in higher yields of protein (0.51 g/g biomass), glucosamine (0.16 g/g alkali insoluble material, AIM), and phosphate (0.11 g/g AIM).ConclusionsIt is not possible to have the maximum amounts of the products simultaneously. The fermentation conditions and composition of culture media determine the product yields. Carbon source type and the addition of nitrogen source are among the most influencing factors on the product yields. Moreover, all measured products were made with higher yields in cultivation on glucose, except glucosamine, which was produced with higher yields on xylose. 相似文献
12.
BackgroundSalep is obtained by grinding dried orchid tubers and used as a valuable ingredient in the food industry. Because of the glucomannan content of salep, it is thought to have prebiotic potential. However, there is little information in studies concerning the fermentation characteristics and potential prebiotic properties of salep. The objective of this study was to investigate the effect of salep on bifidobacterial growth by measuring the highest optical density (OD), calculating the specific growth rates, and determining the production of lactic acid and short-chain fatty acids (acetic, propionic, and butyric acid) as a result of bacterial fermentation.ResultThe OD and pH values obtained in this study showed that salep was utilized as a source of assimilable carbon and energy by the Bifidobacterium species (BS). All Bifidobacterium strains produced lactic, acetic, propionic, and butyric acid, indicating that salep is readily fermented by these bacteria. Salep at 1% (w/v) showed a similar effect on bifidobacterial growth as that promoted by 1% (w/v) glucose used as a traditional carbon source.ConclusionsBifidobacterium species can develop in media containing salep as well as in glucose and exhibit the potential to be used as new sources of prebiotics.How to cite: Usta-Gorgun B, Yilmaz-Ersan L. Short-chain fatty acid production by the Bifidobacterium species in the presence of salep. Electron J Biotechnol 2020;47. https://doi.org/10.1016/j.ejbt.2020.06.004. 相似文献
13.
BackgroundSulphur-oxidizing microorganisms are widely used in the biofiltration of total reduced sulphur compounds (odorous and neurotoxic) produced by industries such as the cellulose and petrochemical industries, which include high-temperature process steps. Some hyperthermophilic microorganisms have the capability to oxidize these compounds at high temperatures (> 60°C), and archaea of this group, for example, Sulfolobus metallicus, are commonly used in biofiltration technology.ResultsIn this study, a hyperthermophilic sulphur-oxidizing strain of archaea was isolated from a hot spring (Chillán, Chile) and designated as M1. It was identified as archaea of the genus Sulfolobus (99% homology with S. solfataricus 16S rDNA). Biofilms of this culture grown on polyethylene rings showed an elemental sulphur oxidation rate of 95.15 ± 15.39 mg S l-1 d-1, higher than the rate exhibited by the biofilm of the sulphur-oxidizing archaea S. metallicus (56.8 ± 10.91 mg l-1 d-1).ConclusionsThe results suggest that the culture M1 is useful for the biofiltration of total reduced sulphur gases at high temperatures and for other biotechnological applications. 相似文献
14.
BackgroundEndoglucanase, one of three type cellulases, can randomly cleave internal β-1,4-linkages in cellulose polymers. Thus, it could be applied in agricultural and industrial processes.ResultsA novel endoglucanase gene (JqCel5A) was cloned from Jonesia quinghaiensis and functionally expressed in Escherichia coli Rosetta (DE3). It contained 1722 bp and encoded a 573-residue polypeptide consisting of a catalytic domain of glycoside hydrolase family 5 (GH5) and a type 2 carbohydrate-binding module (CBM2), together with a predicted molecular mass of 61.79 kD. The purified JqCel5A displayed maximum activity at 55°C and pH 7.0, with 21.7 U/mg, 26.19 U/mg and 4.81 U/mg towards the substrate carboxymethyl cellulose, barley glucan and filter paper, respectively. Interestingly, JqCel5A exhibited high pH stability over a broad pH range of pH (3–11), and had good tolerance to a wide variety of deleterious chemicals including heavy metals and detergent. The catalytic mechanism of JqCel5A was also investigated by site mutagenesis and homology-modeling in this study.ConclusionsIt was believed that these properties might make JqCel5A to be potentially used in the suitable industrial catalytic condition, which has a broad pH fluctuation and/or chemical disturbance. 相似文献
15.
BackgroundPlanctomycetes is a phylum of biofilm-forming bacteria with numerous biosynthetic gene clusters, offering a promising source of new bioactive secondary metabolites. However, the current generation of chemically defined media achieves only low biomass yields, hindering research on these species. We therefore developed a chemically defined medium for the model organism Planctopirus limnophila to increase biomass production.ResultsWe found that P. limnophila grows best with a 10 mM sodium phosphate buffer. The replacement of complex nitrogen sources with defined amino acid solutions did not inhibit growth. Screening for vitamin requirements revealed that only cyanocobalamin (B12) is needed for growth. We used response surface methodology to optimize the medium, resulting in concentrations of 10 g/L glucose, 34 mL/L Hutner’s basal salts, 23.18 mM KNO3, 2.318 mM NH4Cl and 0.02 mg/L cyanocobalamin. The analysis of amino acid consumption allowed us to develop a customized amino acid solution lacking six of the amino acids present in Aminoplasmal 10%. Fed-batch cultivation in a bioreactor using the optimized medium achieved a final ΔOD600 of 46.8 ± 0.5 after 108 h, corresponding to a cell dry weight of 13.6 ± 0.7 g/L.ConclusionsThe optimized chemically defined medium allowed us to produce larger amounts of biomass more quickly than reported in earlier studies. Further research should focus on triggering P. limnophila biofilm formation to activate the gene clusters responsible for secondary metabolism.How to cite: Kruppa OC, Gerlach D, Fan R, et al. Development of a chemically defined medium for Planctopirus limnophila to increase biomass production. Electron J Biotechnol 2021;54. https://doi.org/10.1016/j.ejbt.2021.09.002. 相似文献
16.
BackgroundPoly(dl-lactic acid), or PDLLA, is a biodegradable polymer that can be hydrolyzed by various types of enzymes. The protease produced by Actinomadura keratinilytica strain T16-1 was previously reported to have PDLLA depolymerase activity. However, few studies have reported on PDLLA-degrading enzyme production by bacteria. Therefore, the aims of this study were to determine a suitable immobilization material for PDLLA-degrading enzyme production and optimize PDLLA-degrading enzyme production by using immobilized A. keratinilytica strain T16-1 under various fermentation process conditions in a stirrer fermenter.ResultsAmong the tested immobilization materials, a scrub pad was the best immobilizer, giving an enzyme activity of 30.03 U/mL in a shake-flask scale. The maximum enzyme activity was obtained at aeration 0.25 vvm, agitation 170 rpm, 45°C, and 48 h of cultivation time. Under these conditions, a PDLLA-degrading enzyme production of 766.33 U/mL with 15.97 U/mL·h productivity was observed using batch fermentation in a 5-L stirrer fermenter. Increased enzyme activity and productivity were observed in repeated-batch (942.67 U/mL and 19.64 U/mL·h) and continuous fermentation (796.43 U/mL and 16.58 U/mL·h) at a dilution rate of 0.013/h. Scaled-up production of the enzyme in a 10-L stirrer bioreactor using the optimized conditions showed a maximum enzyme activity of 578.67 U/mL and a productivity of 12.06 U/mL·h.ConclusionsThis research successfully scaled-up the enzyme production to 5 and 10 L in a stirrer fermenter and is helpful for many applications of poly(lactic acid). 相似文献
17.
BackgroundAt present, cellulases are the most important enzymes worldwide, and their demand has been increasing in the industrial sector owing to their notable hydrolysis capability.ResultsIn the present study, contrary to conventional techniques, three physical parameters were statistically optimized for the production of cellulase by thermophilic fungi by using response surface methodology (RSM). Among all the tested thermophilic strains, the best cellulase producing fungus was identified as Talaromyces thermophilus – both morphologically and molecularly through 5.8S/ITS rDNA sequencing. The central composite design (CCD) was used to evaluate the interactive effect of the significant factors. The CCD was applied by considering incubation period, pH, and temperature as the model factors for the present investigation. A second-order quadratic model and response surface method revealed that the independent variables including pH 6, temperature 50 °C, and incubation period 72 h significantly influenced the production of cellulases. The analysis of variance (ANOVA) indicated that the established model was significant (P ≤ 0.05) and showed the high adequacy of the model. The actual and predicted values of CMCase and FPase activity showed good agreement with each other and also confirmed the validity of the designed model.ConclusionsWe believe the present findings to be the first report on cellulase production by exploiting Kans grass (Saccharum spontaneum) as a substrate through response surface methodology by using thermophilic fungus, Talaromyces thermophilus.How to cite: Abdullah R, Tahseen M, Nisar K et al. Statistical optimization of cellulases by Talaromyces thermophilus utilizing Saccharum spontaneum, a novel substrate. Electron J Biotechnol 2021;51. https://doi.org/10.1016/j.ejbt.2021.03.007. 相似文献
18.
BackgroundThe effect of diverse oxygen transfer coefficient on the l-erythrulose production from meso-erythritol by a newly isolated strain, Gluconobacter kondonii CGMCC8391 was investigated. In order to elucidate the effects of volumetric mass transfer coefficient (kLa) on the fermentations, baffled and unbaffled flask cultures, and fed-batch cultures were developed in present work.ResultsWith the increase of the kLa value in the fed-batch culture, l-erythrulose concentration, productivity and yield were significantly improved, while cell growth was not the best in the high kLa. Thus, a two-stage oxygen supply control strategy was proposed, aimed at achieving high concentration and high productivity of l-erythrulose. During the first 12 h, kLa was controlled at 40.28 h-1 to obtain high value for cell growth, subsequently kLa was controlled at 86.31 h-1 to allow for high l-erythrulose accumulation.ConclusionsUnder optimal conditions, the l-erythrulose concentration, productivity, yield and DCW reached 207.9 ± 7.78 g/L, 6.50 g/L/h, 0.94 g/g, 2.68 ± 0.17 g/L, respectively. At the end of fermentation, the l-erythrulose concentration and productivity were higher than those in the previous similar reports. 相似文献
19.
BackgroundCecropin P1, acting as an antimicrobial, has a broad-spectrum antibacterial activity with some antiviral and antifungal properties. It is a promising natural alternative to antibiotics which is originally isolated from the pig intestinal parasitic nematode Ascaris suum. Many studies have shown that Cecropin P1 is helpful for the prevention or treatment of clinical diseases. Therefore, it is very necessary to establish a safe, nontoxic, and efficient expression method of Cecropin P1.ResultsThe results indicated that the recombinant protein was about 5.5 kDa showed by Tricine–SDS–PAGE and Western blot. And Cecropin P1 was efficiently secreted and expressed after 12 h of induction, with an increasing yield over the course of the induction. Its maximum concentration was 7.83 mg/L after concentration and purification. In addition, in vitro experiments demonstrated that Cecropin P1 not only exerted a strong inhibitory effect on Escherichia coli, Salmonella sp., Shigella sp., and Pasteurella sp., but also displayed an antiviral activity against PRRSV NADC30-Like strain.ConclusionsCollectively, the strategy of expressing Cecropin P1 in Saccharomyces cerevisiae is harmless, efficient, and safe for cells. In addition, the expressed Cecropin P1 has antiviral and antibacterial properties concurrently.How to cite: Jiang R, Zhang P, Wu X, et al., Expression of antimicrobial peptide Cecropin P1 in Saccharomyces cerevisiae and its antibacterial and antiviral activity in vitro. Electron J Biotechnol 2021;50. https://doi.org/10.1016/j.ejbt.2020.12.006 相似文献