Simultaneous bioelectricity generation and pollutants removal of sediment microbial fuel cell combined with submerged macrophyte

A submerged macrophyte sediment microbial fuel cell (SP-SMFC) was constructed in this study. Ceratophyllum demersum L., Vallisneria natans, Hydrilla verticillate were chosen as the submerged plants to form cer-SMFC, val-SMFC, hyd-SMFC systems. Plant groups showed the advantage of bioelectricity generation and pollutants removal compared with the unplanted system. The cer-SMFC group stood out with the maximum power density as 24.56 mW m^?2 and the average pollutants removal in overlying water (COD: 81.16%, TN: 65.27%, TP: 79.10%) and in sediments (TN: 26.40%, TP: 21.79%). The determination of root exudates and radial oxygen loss (ROL) demonstrated that C. demersum L. was superior to other studied submerged macrophytes. More root exudates may contribute to an increase in available substrates for electrochemically active bacteria and other microorganisms. Higher enzyme activities were obtained in three SP-SMFCs (especially in cer-SMFC). ATPase and APA activities in cer-SMFC group were increased by over 40% compared with the control. The results indicated that the presence of plants enhanced the microorganism activities, thereby improving bioelectricity generation and pollutants removal. This study will facilitate the application of SP-SMFC technology as an alternative for in situ remediation of polluted sediments.     

Bio-mediated generation of food flavors – Towards sustainable flavor production inspired by nature

BackgroundThe consumers’ trend toward naturalness and “clean-label” products advocates the development of “bio-mediated” tools including new processes for the generation of flavors. Today, many fundamental studies demonstrate the feasibility of producing individual flavor compounds or more complex flavoring preparations by fermentation or by enzymatic reactions. However, to turn research into industrial applications, the processes have to be simplified and optimized by combining chemistry, biology and process engineering know-how.Scope and approachThis review summarises recent basic research and development on cell and enzyme based formation of volatile flavors with focus on smart combinations of biocatalytic and thermal steps to enrich the natural flavor profile of foods. Ideally, targeted bioconversion of specific raw materials and ingredients will release flavor precursors required to generate the desired flavor profile by appropriate thermal processing.Key findings and conclusionsThe combination of fermentation or enzymatic treatment of raw materials with heat-induced food processes (e.g. drying, extrusion, roasting) represent an elegant approach in industrial food processing to generate flavors under mild conditions. This requires a good control of fermentation or enzymatic reaction steps to produce suitable substrates at the optimal concentrations adapted to the thermal processes. Using traditional cooking and minimal processing conditions (nature-inspired strategies) has become an attractive approach to generate authentic flavor profiles resonating with consumers’ demand for more naturalness.     

Degradation of phenolic compounds with hydrogen peroxide catalyzed by enzyme from Serratia marcescens AB 90027

In this paper, the degradation of phenolic compounds using hydrogen peroxide as oxidizer and the enzyme extract from Serratia marcescens AB 90027 as catalyst was reported. With such an enzyme/H2O2 combination treatment, a high chemical oxygen demand (COD) removal efficiency was achieved, e.g., degradation of hydroquinone exceeded 96%. From UV-visible and IR spectra, the degradation mechanisms were judged as a process of phenyl ring cleavage. HPLC analysis shows that in the degradation p-benzoquinone, maleic acid and oxalic acid were formed as intermediates and that they were ultimately converted to CO2 and H2O. With the enzyme/H2O2 treatment, vanillin, hydroquinone, catechol, o-aminophenol, p-aminophenol, phloroglucinol and p-hydroxybenzaldehyde were readily degraded, whereas the degradation of phenol, salicylic acid, resorcinol, p-cholorophenol and p-nitrophenol were limited. Their degradability was closely related to the properties and positions of their side chain groups. Electron-donating groups, such as -OH, -NH2 and -OCH3 enhanced the degradation, whereas electron-withdrawing groups, such as -NO2, -Cl and -COOH, had a negative effect on the degradation of these compounds in the presence of enzyme/H2O2. Compounds with -OH at ortho and para positions were more readily degraded than those with -OH at meta positions.     

Efficient synthesis of tyrosol from L-tyrosine via heterologous Ehrlich pathway in Escherichia coli

For the efficient conversion of L-tyrosine (L-Tyr) to tyrosol, which is an aromatic compound widely used in the pharmaceutical and chemical industries, a novel four-enzyme cascade pathway based on the Ehrlich pathway of Saccharomyces cerevisiae was designed and reconstructed in Escherichia coli. Then, the expression levels of the relevant enzymes were coordinated using a modular approach and gene duplication after the identification of the pyruvate decarboxylase from Candida tropicalis (CtPDC) as the rate-limiting enzymatic step. In situ product removal (ISPR) strategy with XAD4 resins was explored to avoid product inhibition and further improve tyrosol yield. As a result, the titer and conversion rate of tyrosol obtained were 35.7 g·L^-1 and 93.6%, respectively, in a 3-L bioreactor. Results presented here provide a potential enzymatic process for industrial production of tyrosol from cheap amino acids.     

Incidence of adenoviruses in raw and treated water

Adenoviruses are of major public health importance and are associated with a variety of clinical manifestations, i.e. gastroenteritis, eye infections and respiratory infections. The importance of water in the epidemiology of adenoviruses and the potential health risks constituted by adenoviruses in water sources and supplies are widely recognised. This study was conducted to assess the incidence of human adenoviruses in raw and treated water systems. Various raw and treated water were routinely monitored for the presence of adenoviruses, over a 1-year period (July 2000-June 2001). The supplies were derived from acceptable quality surface water sources using treatment processes, which conform to international standards for the production of safe drinking water. Adenoviruses were detected by firstly amplifying the viruses in cell cultures and then amplifying the extracted nucleic acids of these viruses using molecular techniques (nested PCR). The results indicated human adenoviruses present in 13 (12.75%) of the raw and 9 (4.41%) of the treated water samples tested. The combination of cell culture and nested PCR has proved to be a quick and reliable method for the detection of adenoviruses in water environments.     

Validation of a Method for Quantitation of Soybean Lectin in Commercial Varieties

Soybean agglutinin (SBA) protein, also known as soybean lectin, is regarded as an anti‐nutrient due to its negative effect on the ability of monogastric animals to gain weight following consumption of raw soybean seed. Historically, SBA has been measured using a time‐consuming and cumbersome hemagglutination procedure. The objective of our research was to obtain a validated methodology that is precise and accurate in the measurement of SBA while allowing minimally equipped laboratories to effectively conduct the analysis, thus our focus was on evaluating an existing commercially available ELISA, an enzyme‐linked‐lectin‐assay (ELLA), and a hybrid ELISA/ELLA. A new ELLA technique that can detect and quantify lectins was chosen and modified specifically for the quantitation of SBA in soybean seed. The proposed ELLA methodology is similar to a standard sandwich ELISA, and uses polyacrylamide‐linked N‐acetylgalactosamine (Gal–NAc–PAA) for a capture phase and the biotinylated version (Gal–NAc–PAA–Biotin) for detection. Based upon the validation data, the ELLA method can precisely and accurately determine soybean lectin levels in soybean seed. The validated ELLA method was used to quantify SBA in nine commercial soybean varieties introduced between 1972 and 2008 and demonstrated that the natural variability of SBA is subject to the effects of genotype and environment.     

One‐Pot Lipase Entrapment Within Silica Particles to Prepare a Stable and Reusable Biocatalyst for Transesterification

In order to enhance the reusability, Rhizomucor miehei lipase was entrapped in a single step within silica particles having an oleic acid core (RML@SiO₂). Characterization of RML@SiO₂ by scanning and transmission electron microscopy and Fourier transform infrared studies supported the lipase immobilization within silica particles. The immobilized enzyme was employed for transesterification of cottonseed oil with methanol and ethanol. Under the optimum reaction conditions of a methanol‐to‐oil molar ratio of 12:1 or ethanol‐to‐oil molar ratio of 15:1, stirring speed of 250 revolutions/min (flask radius = 3 cm), reaction temperature of 40 °C, and biocatalyst concentration of 5 wt% (with respect to oil), more than 98 % alkyl ester yield was achieved in 16 and 24 h of reaction duration in case of methanolysis and ethanolysis, respectively. The immobilized enzyme did not require any buffer solution or organic solvent for optimum activity; hence, the produced biodiesel and glycerol were free from metal ion or organic molecule contamination. The activation energies for the immobilized enzyme‐catalyzed ethanolysis and methanolysis were found to be 34.9 ± 1.6 and 19.7 ± 1.8 kJ mol^?1, respectively. The immobilized enzyme was recovered from the reaction mixture and reused in 12 successive runs without significant loss of activity. Additionally, RML@SiO₂ demonstrated better reusability as well as stability in comparison to the native enzyme as the former did not lose the activity even upon storage at room temperature (25–30 °C) over an 8‐month period.     

Enzyme Processing of Soy Flour with Minimized Protein Loss

The enzymatic treatment of defatted soy flour (SF) to reduce indigestible carbohydrates can result in undesirable protein loss. Here protein loss was minimized with quantitation of the effects of ionic strength (IS), protease activity, and SF toasting. At the enzyme processing condition (25% w/v SF, 50 °C, pH 4.8, 48 hours), protein loss increased linearly with the IS in enzyme broths (EB); e.g., contacting untoasted SF with water or heat-deactivated EB showed protein loss of 28% in water but up to 40% when IS was increased in the range of 0.04–0.19 M. Protein loss also increased with protease in EB (nondeactivated): after adjusted for IS-related loss, approximately 10% and 25% additional protein loss occurred in EB of 73 and 490–557 U/(g SF) protease, respectively. SDS-PAGE results showed that proteolysis was not extensive, mainly on β-conglycinin α'/α and glycinin acidic 37-kDa subunits; and most of the proteolytic products could be recovered by heat-induced precipitation. SF toasting effects were studied, particularly at 2-hours 160°C, with material balances, protein distributions, and monosaccharide yields in hydrolysates. Overall, protein loss was minimized to 5.2% and the conversion of carbohydrate to monomeric sugars increased to 89.2%.     

Microenvironmental engineering:An effective strategy for tailoring enzymatic activities

Rationally, engineering a favorable physicochemical microenvironment for enzymes has recently emerged as an effective strategy to improve their catalytic performance. In this review, we discuss four microenvironmental effects according to the mechanism of action: localizing and excluding reactants and regulators, regulating microenvironmental pH, creating a water-like microenvironment, and increasing the local temperature. These mechanisms are enzyme-independent and can in principle be used in combination to tailor enzyme behaviors,offering new approaches to enabling, enhancing, and regulating enzyme catalysis in diverse applications without the need for genetic engineering.