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박예섭,Nasir Abdul,NGUYEN VO PHU THUAN,류희창,석주연,정규열,박성훈,유태현 한국생물공학회 2023 Biotechnology and Bioprocess Engineering Vol.28 No.6
3-Hydroxypropionic acid (3-HP) is a key building block for value-added chemicals. A biological route for synthesizing this molecule is two-step enzymatic reactions; dehydration of glycerol to 3-hydroxypropanal (3-HPA) by glycerol dehydratase and then oxidation of 3-HPA to 3-HP by aldehyde dehydrogenase. Here, we report an aldehyde dehydrogenase, an engineered α-ketoglutaric semialdehyde dehydrogenase (KGSADH) from Azospirillum brasilense. The variant, named 2C10, was obtained by applying a large KGSADH library to a selection method based on a 3-HP-responsive transcription factor and then a screening method for observing the activities of individual clones. 2C10 exhibited a 4.65-fold higher catalytic activity (kcat/Km: 100 ± 7.1 s−1mM−1) toward 3-HPA than the wild-type enzyme. The flask culture of Pseudomonas denitrificans with 2C10 resulted in an approximately 30% increase in 3-HP titer (43.2 mM) compared with that obtained using wild-type KGSADH (33.1 mM). Molecular dynamics simulations suggested that compared to the wild-type enzyme, 2C10 has a less flexible and smaller binding pocket for aldehyde substrates.
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An engineered aldehyde dehydrogenase for production of 3-hydroxypropionic acid from glycerol
박예섭,유태현 한국공업화학회 2016 한국공업화학회 연구논문 초록집 Vol.2016 No.0
Biological conversion of glycerol into valuable biochemicals has attracted lots of attentions because glycerol is by-product of the biodiesel production. One of these chemicals is 3-hydroxypropionic acid (3-HP) that can be produced from glycerol via two enzymatic reactions: glycerol to 3-hydroxylpropanal (3-HPA) via glycerol dehydratase and 3-HPA to 3-HP via aldehyde dehydrogenase. Biological processes using the two reactions have been developed, and the productivity of more than 0.86g/L/hr was reported. However, improvement in the productivity is needed to move to a next phase of commercialization, and some issues have been raised. One of them is the toxicity of 3-HPA. An approach to solve the problem is to develop a highly active aldehyde dehydrogenase, and the process can be operated at a low concentration of 3-HPA. In this presentation, we report the results of engineering the substrate specific of an aldehyde dehydrogenase, α-ketoglutaric semialdehyde dehydrogenase toward 3-HPA.
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박예섭,유태현,최운종,최상진 한국공업화학회 2017 한국공업화학회 연구논문 초록집 Vol.2017 No.1
3-Hydroxypropionic acid (3-HP) can be produced via two enzymatic reactions: dehydration of glycerol to 3-hydroxypropanal (3-HPA) and oxidation to 3-HP. Commercial production of 3-HP has been beset with several problems; toxicity of 3-HPA and the efficiency of NAD+ regeneration. We engineered α-ketoglutaric semialdehyde dehydrogenase (KGSADH) for the second reaction to address these issues. The residues in the putative binding sites for the substrates, 3-HPA and NAD+, were randomized, and the libraries were screened. Isolated enzymes showed higher substrate specificities for aldehyde and NAD+, less inhibition by NADH, and greater resistance to inactivation by 3-HPA than the wild-type enzyme. A recombinant Pseudomonas denitrificans strain with one of the engineered KGSADH variants exhibited less accumulation of 3-HPA, decreased levels of inactivation of the enzymes involved in the production of 3-HP. These attributes facilitated enhanced the final titer of 3-HP by approximately 40%.
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박예섭,임혜진,김동명,유태현 한국공업화학회 2020 한국공업화학회 연구논문 초록집 Vol.2020 No.-
Methane is a valuable resource in itself. But the resource has some issues hard to use. It exists as a gas making it expensive to transport to remote locations. Another issue is that methane is a potent greenhouse gas. It has global warming potential more than 20 times that of CO<sub>2</sub>. Methane monooxygenases (MMOs) are enzymes that catalyze of methane to methanol in methanotrophic bacteria. Through these enzymes, methane can be selectively converted to methanol in mild condition. But the conversion rate of the enzymes are pretty low. So they should be engineered to satisfy an industrially viable level. The inability to express MMOH (Hydroxylase) in a heterologous host limits their utilization in engineering. In our work, to manipulate sMMOH from Methylosinus trichosporium OB3b in E.coli strains, we chose a method called cell-free protein synthesis. And then we focused on optimizing enzymatic assay for screening to find clones that have higher catalytic acticity than that of Wild type MMOH.
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박예섭,임혜진,김동명,유태현 한국공업화학회 2019 한국공업화학회 연구논문 초록집 Vol.2019 No.1
Methane is a valuable resource in itself. But the resource has some issues hard to use. It exists as a gas making it expensive to transport to remote locations. Another issue is that methane is a potent greenhouse gas. It has global warming potential more than 20 times that of CO<sub>2</sub>. Methane monooxygenases (MMOs) are enzymes that catalyze of methane to methanol in methanotrophic bacteria. Through these enzymes, methane can be selectively converted to methanol in mild condition. But the conversion rate of the enzymes are pretty low. So they should be engineered to satisfy an industrially viable level. The inability to express MMOH (Hydroxylase) in a heterologous host limits their utilization in engineering. In our work, to manipulate sMMOH from Methylosinus trichosporium OB3b in E.coli strains, we chose a method called cell-free protein synthesis. And then we focused on optimizing enzymatic assay for screening to measure concentration of methanol which is converted by sMMO clones.
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Estimation of WorldSID thorax kinematics using multiple 3-axis accelerometers
박예섭,오유근 대한기계학회 2019 JOURNAL OF MECHANICAL SCIENCE AND TECHNOLOGY Vol.33 No.12
It is essential to analyze the kinematics of anthropometry dummy in vehicle’s crash test. In general, it is required to measure the linear and angular components in the three orthogonal directions, respectively, in order to calculate the 3D kinematics of a rigid body. The WorldSID is originally designed to measure the tri-axis linear accelerations at the first (T1), fourth (T4), and twelfth (T12) thoracic vertebrae segments and the angular accelerations in the x and z directions. However, only three tri-axis linear accelerations are often measured for the sake of convenience. The lack of the required information results in the inaccurate calculation of the 3D torso kinematics. In this study, we propose an algorithm to accurately estimate the 3D torso kinematics when only three tri-axis linear accelerations at T1, T4, and T12 are available. Given the fact that the three tri-axis accelerometers are fixed in the torso segment, the mathematical algorithm is developed to estimate the linear acceleration at the location of the center of mass for the torso and the angular acceleration of the torso. The accuracy of the proposed algorithm is validated against the results from a rigid-body model that models the WorldSID’s spine block and tri-axis accelerometers attached to T1, T4, and T12. According to the comparison against the rigid-body model, the estimated values are calculated to be within 1.7 % of the target values. After the validation is achieved, the 3D kinematics of WorldSID’s torso is estimated using a set of actual side impact test data. In conclusion, the proposed algorithm accurately estimates the 3D WorldSID kinematics when at least three sets of tri-axis linear accelerations are available without any measurements of angular components.
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