AN ASSESSMENT OF USER PREFERENCE IN ARTIFICIAL PATHWAY LIGHTING IN URBAN PARKS; Cases from Greater Colombo region

Urban parks are critical in converting cities to liveable spaces, where artificial lighting directly affects the users’ night-time experience. This study explores the urban park users’ preferences in artificial pathway lighting, through their subjective responses towards Brightness, Correlated Colour Temperature (CCT), and luminaires of the existing lighting design, at four popular urban parks in Colombo. The reasons for the said preferences were investigated under three overarching themes: perceived safety, perceived quality of light, and restorative experience. A mixed methods approach was employed for data collection, where questionnaires were used together with measurements, in-situ observations, and photographic analysis for better understanding. The user preferences were found to be directly associated with their perception of the lit environment. The existing brightness levels are insufficient for majority of the users and has affected their perception of safety. The poor selection and placement of luminaires have negatively affected the lighting quality, while the positive effect on the users’ restorative experience has induced a higher preference towards the CCT of the light sources. The results revealed that the majority of the users opted for changes in the current lighting design, indicating that the user needs and requirements are not effectively addressed in this regard.

Metabolic engineering of Escherichia coli for de novo production of 3-phenylpropanol via retrobiosynthesis approach

Background 3-Phenylpropanol with a pleasant odor is widely used in foods, beverages and cosmetics as a fragrance ingredient. It also acts as the precursor and reactant in pharmaceutical and chemical industries. Currently, petroleum-based manufacturing processes of 3-phenypropanol is environmentally unfriendly and unsustainable. In this study, we aim to engineer Escherichia coli as microbial cell factory for de novo production of 3-phenypropanol via retrobiosynthesis approach. Results Aided by in silico retrobiosynthesis analysis, we designed a novel 3-phenylpropanol biosynthetic pathway extending from l-phenylalanine and comprising the phenylalanine ammonia lyase (PAL), enoate reductase (ER), aryl carboxylic acid reductase (CAR) and phosphopantetheinyl transferase (PPTase). We screened the enzymes from plants and microorganisms and reconstructed the artificial pathway for conversion of 3-phenylpropanol from l-phenylalanine. Then we conducted chromosome engineering to increase the supply of precursor l-phenylalanine and combined the upstream l-phenylalanine pathway and downstream 3-phenylpropanol pathway. Finally, we regulated the metabolic pathway strength and optimized fermentation conditions. As a consequence, metabolically engineered E. coli strain produced 847.97 mg/L of 3-phenypropanol at 24 h using glucose-glycerol mixture as co-carbon source. Conclusions We successfully developed an artificial 3-phenylpropanol pathway based on retrobiosynthesis approach, and highest titer of 3-phenylpropanol was achieved in E. coli via systems metabolic engineering strategies including enzyme sources variety, chromosome engineering, metabolic strength balancing and fermentation optimization. This work provides an engineered strain with industrial potential for production of 3-phenylpropanol, and the strategies applied here could be practical for bioengineers to design and reconstruct the microbial cell factory for high valuable chemicals.

Biotransformation of Benzoate to 2,4,6-Trihydroxybenzophenone by Engineered Escherichia coli

The synthesis of natural products by E. coli is a challenging alternative method of environmentally friendly minimization of hazardous waste. Here, we establish a recombinant E. coli capable of transforming sodium benzoate into 2,4,6-trihydroxybenzophenone (2,4,6-TriHB), the intermediate of benzophenones and xanthones derivatives, based on the coexpression of benzoate-CoA ligase from Rhodopseudomonas palustris (BadA) and benzophenone synthase from Garcinia mangostana (GmBPS). It was found that the engineered E. coli accepted benzoate as the leading substrate for the formation of benzoyl CoA by the function of BadA and subsequently condensed, with the endogenous malonyl CoA by the catalytic function of BPS, into 2,4,6-TriHB. This metabolite was excreted into the culture medium and was detected by the high-resolution LC-ESI-QTOF-MS/MS. The structure was elucidated by in silico tools: Sirius 4.5 combined with CSI FingerID web service. The results suggested the potential of the new artificial pathway in E. coli to successfully catalyze the transformation of sodium benzoate into 2,4,6-TriHB. This system will lead to further syntheses of other benzophenone derivatives via the addition of various genes to catalyze for functional groups.

Anatomical considerations for obturator nerve block with fascia iliaca compartment block

This report reviews the topographical and functional anatomy relevant for assessing whether or not the obturator nerve (ON) can be anesthetized using a fascia iliaca compartment (FIC) block. The ON does not cross the FIC. This means that the ON would only be blocked by an FIC block if the injectate spreads to the ON outside of the FIC. Such a phenomena would require the creation of one or more artificial passageways to the ON in the retro-psoas compartment or the retroperitoneal compartment by disrupting the normal anatomical integrity of the FI. Due to this requirement for an artificial pathway, an FIC block probably does not block the ON.

A High-Efficiency Artificial Synthetic Pathway for 5-Aminovalerate Production From Biobased L-Lysine in Escherichia coli

Bioproduction of 5-aminovalerate (5AVA) from renewable feedstock can support a sustainable biorefinery process to produce bioplastics, such as nylon 5 and nylon 56. In order to achieve the biobased production of 5AVA, a 2-keto-6-aminocaproate-mediated synthetic pathway was established. Combination of L-Lysine α-oxidase from Scomber japonicus, α-ketoacid decarboxylase from Lactococcus lactis and aldehyde dehydrogenase from Escherichia coli could achieve the biosynthesis of 5AVA from biobased L-Lysine in E. coli. The H2O2 produced by L-Lysine α-oxidase was decomposed by the expression of catalase KatE. Finally, 52.24 g/L of 5AVA were obtained through fed-batch biotransformation. Moreover, homology modeling, molecular docking and molecular dynamic simulation analyses were used to identify mutation sites and propose a possible trait-improvement strategy: the expanded catalytic channel of mutant and more hydrogen bonds formed might be beneficial for the substrates stretch. In summary, we have developed a promising artificial pathway for efficient 5AVA synthesis.

De novo biosynthesis of sex pheromone components of Helicoverpa armigera through an artificial pathway in yeast

The cotton bollworm, Helicoverpa armigera, causes severe damage to the yields of cotton and other crops. (Z)-11-hexadecenal (Z11–16:Ald) and (Z)-9-hexadecenal (Z9–16:Ald), as the main components of H. armigera sex pheromones,...