Purification and Characterization of Anabaena flos-aquae Phenylalanine Ammonia-Lyase as a Novel Approach for Myristicin Biotransformation

Arafa, Asmaa M.; Abdel-Ghany, Afaf E.; El-Dahmy, S.; Abdelaziz, Sahar; El-Ayouty, Yassin; El-Sayed, Ashraf S. A.

doi:10.4014/jmb.1908.08009

Cited by 9 publications

(4 citation statements)

References 75 publications

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“…The experimental conditions to be evaluated were identified solely by using the automated process provided by the software: no intuition, prior knowledge, or preliminary screening was required. We selected two widely used enzyme catalyzed reactions: (i) a carboxy-lyase reaction, catalyzed by benzoylformate decarboxylase (BFD), − and (ii) the conversion of trans -cinnamic acid and ammonia to phenylalanine, catalyzed by phenylalanine ammonia lyase (PAL). − The optimization was performed with the aim of maximizing the total turnover number (TON), used as the FoM. Five parameters were selected as variables for both the PAL- and the BFD-catalyzed reactions (Scheme ).…”

Section: Resultsmentioning

confidence: 99%

A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions

Tachibana

Zhang

Zou

et al. 2023

ACS Sustainable Chem. Eng.

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Design of experiments (DoE) plays an important role in optimizing the catalytic performance of chemical reactions. The most commonly used DoE relies on the response surface methodology (RSM) to model the variable space of experimental conditions with the fewest number of experiments. However, the RSM leads to an exponential increase in the number of required experiments as the number of variables increases. Herein we describe a Bayesian optimization algorithm (BOA) to optimize the continuous parameters (e.g., temperature, reaction time, reactant and enzyme concentrations, etc.) of enzyme-catalyzed reactions with the aim of maximizing performance. Compared to existing Bayesian optimization methods, we propose an improved algorithm that leads to better results under limited resources and time for experiments. To validate the versatility of the BOA, we benchmarked its performance with biocatalytic C−C bond formation and amination for the optimization of the turnover number. Gratifyingly, up to 80% improvement compared to RSM and up to 360% improvement vs previous Bayesian optimization algorithms were obtained. Importantly, this strategy enabled simultaneous optimization of both the enzyme's activity and selectivity for cross-benzoin condensation.

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Section: Resultsmentioning

confidence: 99%

A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions

Tachibana

Zhang

Zou

et al. 2023

ACS Sustainable Chem. Eng.

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“…Similar screening paradigm for enzymes production by fungi were reported [ 27 , 42 ]. Coincidently, different tyrosinase producing fungal isolates have been documented [ 1 , 2 , 17 ].…”

Section: Resultsmentioning

confidence: 99%

“…Forty fungal isolates were selected from our lab stock culture [13,[16][17][18][19][20][21][22][23][24], and their potency to grow on L-tyrosine as the sole nitrogen source was determined using modified Czapek's-Dox agar media with 0.5% tyrosine. The media was centrally inoculated with the experimented fungal plug of 6 days old grown on potato dextrose agar [25], incubated for 5 days at 30 • C. The developed fungal colonies were selected and screened for tyrosinase production by growing on Czapek's-Dox broth medium of 0.5% tyrosine as the sole nitrogen source.…”

Section: Screening For the Potent Tyrosinase Producing Fungal Isolatesmentioning

confidence: 99%

Biochemical Properties of Tyrosinase from Aspergillus terreus and Penicillium copticola; Undecanoic Acid from Aspergillus flavus, an Endophyte of Moringa oleifera, Is a Novel Potent Tyrosinase Inhibitor

et al. 2021

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Tyrosinase is a copper-containing monooxygenase catalyzing the O-hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine then to dopaquinone that is profoundly involved in melanin synthesis in eukaryotes. Overactivation of tyrosinase is correlated with hyperpigmentation that is metabolically correlated with severe pathological disorders, so, inhibition of this enzyme is the most effective approach in controlling the overproduction of melanin and its hazardous effects. Thus, searching for a powerful, selective inhibitor of human tyrosinase to limit the hyper-synthesis of melanin is a challenge. Unlike the difficulty of overexpression of human tyrosinase, using fungal tyrosinase as a model enzyme to the human one to evaluate the mechanistics of enzyme inhibition in response to various compounds is the most feasible strategy. Thus, the purification of highly catalytic-efficient fungal tyrosinase, exploring a novel inhibitor, and evaluating the mechanistics of enzyme inhibition are the main objectives of this work. Aspergillus terreus and Penicillium copticola were reported as the most potential tyrosinase producers. The biochemical properties suggest that this enzyme displays a higher structural and catalytic proximity to human tyrosinase. Upon nutritional bioprocessing by Plackett–Burman design, the yield of tyrosinase was increased by about 7.5-folds, compared to the control. The purified tyrosinase was strongly inhibited by kojic acid and A. flavus DCM extracts with IC50 values of 15.1 and 12.6 µg/mL, respectively. From the spectroscopic analysis, the main anti-tyrosinase compounds of A. flavus extract was resolved, and verified as undecanoic acid. Further studies are ongoing to unravel the in vivo effect and cytotoxicity of this compound in fungi and human, that could be a novel drug to various diseases associated with hyperpigmentation by melanin.

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“…17 We selected two widely used enzyme catalyzed reactions: i) a carboxy-lyase reaction, catalyzed by benzoylformate decarboxylase (BFD), [35][36][37] and ii) the conversion of trans-cinnamic acid and ammonia to phenylalanine, catalyzed by phenylalanine ammonia-lyase (PAL). [38][39][40][41][42] The optimization was performed with the aim of maximizing the total turnover number (TON), used as the FoM. Five parameters were selected as continuous variables for both the PAL-and BFD-catalyzed reactions (Scheme 1).…”

mentioning

confidence: 99%

A customized Bayesian algorithm to optimize enzyme-catalyzed reactions

Tachibana

Zhang

Zou

et al. 2023

Preprint

View full text Add to dashboard Cite

Design of experiments (DoE) plays an important role in optimizing the catalytic performance of chemical reactions. The most commonly-used DoE relies on the response surface methodology (RSM) to model the variable space of experimental condi-tions with a minimal number of experiments. However, the RSM leads to an exponential increase in the number of required experiments to be evaluated as the number of variables increases. Herein we describe a Bayesian optimization algorithm (BOA) to optimize the continuous parameters (e.g. temperature, reaction time, reactant and enzyme concentrations etc.) of enzyme-catalyzed reactions with the aim of maximizing performance. Compared to existing Bayesian optimization methods, we propose an improved algorithm that leads to better results under limited resources and time for experiments. To validate the versatility of BOA for the optimization of the turnover number in enzyme-catalyzed reactions, we benchmarked its per-formance for a biocatalytic C-C bond-forming reaction as well as an amination reaction. Gratifyingly, up to 80% improvement compared to RSM and up to 360% improvement vs. previous Bayesian optimization algorithms was obtained. Importantly, this strategy enabled the simultaneous optimization of both the enzyme’s activity and chemoselectivity for a cross-benzoin condensation.

show abstract

Purification and Characterization of Anabaena flos-aquae Phenylalanine Ammonia-Lyase as a Novel Approach for Myristicin Biotransformation

Cited by 9 publications

References 75 publications

A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions

A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions

Biochemical Properties of Tyrosinase from Aspergillus terreus and Penicillium copticola; Undecanoic Acid from Aspergillus flavus, an Endophyte of Moringa oleifera, Is a Novel Potent Tyrosinase Inhibitor

A customized Bayesian algorithm to optimize enzyme-catalyzed reactions

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