Metabolic engineering of microorganisms for the production of structurally diverse esters

Menendez-Bravo, Simón; Comba, Santiago; Gramajo, Hugo; Arabolaza, Ana

doi:10.1007/s00253-017-8179-7

Cited by 18 publications

(8 citation statements)

References 79 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2). On the other hand, the second important domain that characterizes the enzymes of the BADH family consists of the sequence DFGWG [Menendez-Bravo et al, 2017;Moglia et al, 2016], which is not found in the sequences mentioned above (data not shown). Gethins et al [2015] conducted synteny studies and observed that the KmATF2 gene was an ortholog of ScATF2.…”

Section: Alcohol Acetyl Transferasesmentioning

confidence: 91%

Study of the Enzymatic Capacity of Kluyveromyces marxianus for the Synthesis of Esters

et al. 2019

View full text Add to dashboard Cite

Recently, biotechnological opportunities have been found in non-Saccharomyces yeasts because they possess metabolic characteristics that lead to the production of compounds of interest. It has been observed that Kluyveromyces marxianus has a great potential in the production of esters, which are aromatic compounds of industrial importance. The genetic bases that govern the synthesis of esters include a large group of enzymes, among which the most important are alcohol acetyl transferases (AATases) and esterases (AEATases), and it is known that some are present in K. marxianus, because it has genetic characteristics like S. cerevisiae. It also has a physiology suitable for biotechnological use since it is the eukaryotic microorganism with the fastest growth rate and has a wide range of thermotolerance with respect to other yeasts. In this work, the enzymatic background of K. marxianus involved in the synthesis of esters is analyzed, based on the sequences reported in the NCBI database.

show abstract

Section: Alcohol Acetyl Transferasesmentioning

confidence: 91%

Study of the Enzymatic Capacity of Kluyveromyces marxianus for the Synthesis of Esters

et al. 2019

View full text Add to dashboard Cite

show abstract

“…The α-keto acids produced during the processing of amino acids are transformed into the corresponding alcohols after action of the α-ketoacid decarboxylase and alcohol dehydrogenase enzymes [ 39 , 40 , 41 ]. These “fusel alcohols” can undergo esterification by activity of alcohol acyltransferase enzyme [ 42 , 43 ]. In this sense, esters such as 3-methyl-1-butanol propanoate and ethyl propanoate, may be sourced by this pathway.…”

Section: Resultsmentioning

confidence: 99%

Metabolic Profiling of VOCs Emitted by Bacteria Isolated from Pressure Ulcers and Treated with Different Concentrations of Bio-AgNPs

Monedeiro

Railean-Plugaru

Monedeiro-Milanowski

2021

IJMS

View full text Add to dashboard Cite

Considering the advent of antibiotic resistance, the study of bacterial metabolic behavior stimulated by novel antimicrobial agents becomes a relevant tool to elucidate involved adaptive pathways. Profiling of volatile metabolites was performed to monitor alterations of bacterial metabolism induced by biosynthesized silver nanoparticles (bio-AgNPs). Escherichia coli, Enterococcus faecalis, Klebsiella pneumoniae and Proteus mirabilis were isolated from pressure ulcers, and their cultures were prepared in the presence/absence of bio-AgNPs at 12.5, 25 and 50 µg mL−1. Headspace solid phase microextraction associated to gas chromatography–mass spectrometry was the employed analytical platform. At the lower concentration level, the agent promoted positive modulation of products of fermentation routes and bioactive volatiles, indicating an attempt of bacteria to adapt to an ongoing suppression of cellular respiration. Augmented response of aldehydes and other possible products of lipid oxidative cleavage was noticed for increasing levels of bio-AgNPs. The greatest concentration of agent caused a reduction of 44 to 80% in the variety of compounds found in the control samples. Pathway analysis indicated overall inhibition of amino acids and fatty acids routes. The present assessment may provide a deeper understanding of molecular mechanisms of bio-AgNPs and how the metabolic response of bacteria is untangled.

show abstract

“…An AAT purified from Neurospora sp . ATCC 46892 has also shown activity towards both butanol and octanoyl-CoA in vitro, however, to date no Neurospora AAT coding gene has not been assigned (Yamauchi et al, 1989; Menendez-Bravo et al, 2017). While butyl octanoate is not the preferred end-product for any of these three enzymes, AAT16 from Actinidia chinensis showed the highest activity for its production, and so was chosen as the candidate AAT for this work (Günther et al, 2011).…”

Section: Resultsmentioning

confidence: 99%

EngineeringEscherichia colifor the production of butyl octanoate from endogenous octanoyl-CoA

Chacón¹,

Kendrick²,

Leak³

2019

PeerJ

View full text Add to dashboard Cite

Medium chain esters produced from fruits and flowering plants have a number of commercial applications including use as flavour and fragrance ingredients, biofuels, and in pharmaceutical formulations. These esters are typically made via the activity of an alcohol acyl transferase (AAT) enzyme which catalyses the condensation of an alcohol and an acyl-CoA. Developing a microbial platform for medium chain ester production using AAT activity presents several obstacles, including the low product specificity of these enzymes for the desired ester and/or low endogenous substrate availability. In this study, we engineered Escherichia coli for the production of butyl octanoate from endogenously produced octanoyl-CoA. This was achieved through rational protein engineering of an AAT enzyme from Actinidia chinensis for improved octanoyl-CoA substrate specificity and metabolic engineering of E. coli fatty acid metabolism for increased endogenous octanoyl-CoA availability. This resulted in accumulation of 3.3 + 0.1 mg/L butyl octanoate as the sole product from E. coli after 48 h. This study represents a preliminary examination of the feasibility of developing E. coli platforms for the synthesis single medium chain esters from endogenous fatty acids.

show abstract

Metabolic engineering of microorganisms for the production of structurally diverse esters

Cited by 18 publications

References 79 publications

Study of the Enzymatic Capacity of <b><i>Kluyveromyces marxianus</i></b> for the Synthesis of Esters

Study of the Enzymatic Capacity of <b><i>Kluyveromyces marxianus</i></b> for the Synthesis of Esters

Metabolic Profiling of VOCs Emitted by Bacteria Isolated from Pressure Ulcers and Treated with Different Concentrations of Bio-AgNPs

EngineeringEscherichia colifor the production of butyl octanoate from endogenous octanoyl-CoA

Contact Info

Product

Resources

About