"uuid","repository link","title","author","contributor","publication year","abstract","subject topic","language","publication type","publisher","isbn","issn","patent","patent status","bibliographic note","access restriction","embargo date","faculty","department","research group","programme","project","coordinates"
"uuid:f6a54572-b462-4df9-8a57-5a4645ad5b3c","http://resolver.tudelft.nl/uuid:f6a54572-b462-4df9-8a57-5a4645ad5b3c","Vanadium-Containing Chloroperoxidase-Catalyzed Versatile Valorization of Phenols and Phenolic Acids","Li, Huanhuan (Xi’an Jiaotong University); Duan, Peigao (Xi’an Jiaotong University); Huang, Yawen (Chinese Academy of Sciences); Cui, Chengsen (Chinese Academy of Sciences); Hollmann, F. (TU Delft BT/Biocatalysis); Ma, Yunjian (South China University of Technology); Wang, Yonghua (South China University of Technology); Zhang, Jie (Chinese Academy of Sciences); Liu, Weidong (Chinese Academy of Sciences); Zhang, Wuyuan (Chinese Academy of Sciences)","","2024","The downstream product transformation of lignin depolymerization is of great interest in the production of high-value aromatic chemicals. However, this transformation is often impeded by chemical oxidation under harsh reaction conditions. In this study, we demonstrate that hypohalites generated in situ by the vanadium-containing chloroperoxidase from Curvularia inaequalis (CiVCPO) can halogenate various electron-rich and electron-poor phenol and phenolic acid substrates. Specifically, CiVCPO enabled decarboxylative halogenation, deformylative halogenation, halogenation, and direct oxidation reactions. The versatile transformation routes for the valorization of phenolic compounds showed up to 99% conversion and 99% selectivity, with a turnover number of 60,700 and a turnover frequency of 60 s-1 for CiVCPO. This study potentially expands the biocatalytic toolbox for lignin valorization.","biocatalysis; decarboxylation; halogenation; lignin valorization; vanadium-containing chloroperoxidase","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2024-07-18","","","BT/Biocatalysis","","",""
"uuid:bcd4947a-a3b4-4e2a-837e-01237bd73c7e","http://resolver.tudelft.nl/uuid:bcd4947a-a3b4-4e2a-837e-01237bd73c7e","Bienzymatic Cascade Combining a Peroxygenase with an Oxidase for the Synthesis of Aromatic Aldehydes from Benzyl Alcohols","Ma, Yunjian (South China University of Technology; Macau University of Science and Technology); Li, Zongquan (South China University of Technology); Zhang, Hao (South China University of Technology); Wong, Vincent Kam Wai (Macau University of Science and Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology; Guangdong Youmei Institute of Intelligent Bio-manufacturing Co, Foshan)","","2023","Aromatic aldehydes are important aromatic compounds for the flavour and fragrance industry. In this study, a parallel cascade combining aryl alcohol oxidase from Pleurotus eryngii (PeAAOx) and unspecific peroxygenase from the basidiomycete Agrocybe aegerita (AaeUPO) to convert aromatic primary alcohols into high-value aromatic aldehydes is proposed. Key influencing factors in the process of enzyme cascade catalysis, such as enzyme dosage, pH and temperature, were investigated. The universality of PeAAOx coupled with AaeUPO cascade catalysis for the synthesis of aromatic aldehyde flavour compounds from aromatic primary alcohols was evaluated. In a partially optimised system (comprising 30 μM PeAAOx, 2 μM AaeUPO at pH 7 and 40 °C) up to 84% conversion of 50 mM veratryl alcohol into veratryl aldehyde was achieved in a self-sufficient aerobic reaction. Promising turnover numbers of 2800 and 21,000 for PeAAOx and AaeUPO, respectively, point towards practical applicability.","AaeUPO; aromatic aldehydes; cascade catalysis; flavour compounds; PeAAOx","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:fc787c51-4285-4312-ae30-e6e33ec1d94a","http://resolver.tudelft.nl/uuid:fc787c51-4285-4312-ae30-e6e33ec1d94a","A photodecarboxylase from Micractinium conductrix active on medium and short-chain fatty acids","Ma, Yunjian (South China University of Technology; Macau University of Science and Technology); Zhong, Xuanru (South China University of Technology); Wu, Bin (South China University of Technology); Lan, Dongming (South China University of Technology); Zhang, Hao (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology; Guangdong Youmei Institute of Intelligent Bio-manufacturing Co, Foshan)","","2023","Hydrocarbons are essential base chemicals as energy carriers and starting materials for chemical manufacture. So-called fatty acid photodecarboxylases (FAPs) represent interesting catalysts for the conversion of natural fatty acids into hydrocarbons thereby giving access to alkanes from renewable feedstock. Today, however, only few FAPs are known. In the current study we report a new FAP from the marine organism Micractinium conductrix (McFAP). In contrast to currently known FAPs McFAP exhibits high catalytic activity towards short and medium fatty acids. Recombinant expression and basic biochemical characterisation of this new member of the FAP family is reported.","Fatty acids; Heterologous expression; Hydrocarbon biofuel; McFAP; Photodecarboxylase","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2023-06-10","","","BT/Biocatalysis","","",""
"uuid:d1f9bdaa-c33a-419c-833b-26659a40968b","http://resolver.tudelft.nl/uuid:d1f9bdaa-c33a-419c-833b-26659a40968b","Structure-Based Redesign of a Methanol Oxidase into an “Aryl Alcohol Oxidase” for Enzymatic Synthesis of Aromatic Flavor Compounds","Wu, Bin (South China University of Technology); Wang, S. (Chinese Academy of Sciences; University of Chinese Academy of Sciences); Ma, Yunjian (South China University of Technology); Yuan, Shuguang (Chinese Academy of Sciences); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2023","Alcohol oxidases (AOxs) catalyze the aerobic oxidation of alcohols to the corresponding carbonyl products (aldehydes or ketones), producing only H2O2 as the byproduct. The majority of known AOxs, however, have a strong preference for small, primary alcohols, limiting their broad applicability, e.g., in the food industry. To broaden the product scope of AOxs, we performed structure-guided enzyme engineering of a methanol oxidase from Phanerochaete chrysosporium (PcAOx). The substrate preference was extended from methanol to a broad range of benzylic alcohols by modifying the substrate binding pocket. A mutant (PcAOx-EFMH) with four substitutions exhibited improved catalytic activity toward benzyl alcohols with increased conversion and kcat toward the benzyl alcohol from 11.3 to 88.9% and from 0.5 to 2.6 s-1, respectively. The molecular basis for the change of substrate selectivity was analyzed by molecular simulation.","alcohol oxidase; flavor compounds; molecular modification; substrate selectivity","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2023-10-11","","","BT/Biocatalysis","","",""
"uuid:90f1dd5c-15b1-48f2-924e-bb7b86c422f8","http://resolver.tudelft.nl/uuid:90f1dd5c-15b1-48f2-924e-bb7b86c422f8","Continuous Fatty Acid Decarboxylation using an Immobilized Photodecarboxylase in a Membrane Reactor","Zhou, Jianle (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); He, Qi (South China University of Technology); Chen, Wen (South China University of Technology); Ma, Yunjian (South China University of Technology); Wang, Yonghua (South China University of Technology; GuangdongYoumei Institute of Intelligent Bio-manufacturing Co. Ltd., v)","","2023","The realm of photobiocatalytic alkane biofuel synthesis has burgeoned recently; however, the current dearth of well-established and scalable production methodologies in this domain remains conspicuous. In this investigation, we engineered a modified form of membrane-associated fatty acid photodecarboxylase sourced from Micractinium conductrix (McFAP). This endeavour resulted in creating an innovative assembled photoenzyme-membrane (protein load 5 mg cm−2), subsequently integrated into an illuminated flow apparatus to achieve uninterrupted generation of alkane biofuels. Through batch experiments, the photoenzyme-membrane exhibited its prowess in converting fatty acids spanning varying chain lengths (C6–C18). Following this, the membrane-flow mesoscale reactor attained a maximum space-time yield of 1.2 mmol L−1 h−1 (C8) and demonstrated commendable catalytic proficiency across eight consecutive cycles, culminating in a cumulative runtime of eight hours. These findings collectively underscored the photoenzyme-membrane's capability to facilitate the biotransformation of diverse fatty acids, furnishing valuable benchmarks for the conversion of biomass via photobiocatalysis.","alkane biofuel; continuous photocatalysis; decarboxylation; photoenzyme-membrane; self-assembly","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2024-06-15","","","BT/Biocatalysis","","",""
"uuid:ab9002c8-475b-43a9-9455-b92727e8f965","http://resolver.tudelft.nl/uuid:ab9002c8-475b-43a9-9455-b92727e8f965","Selective Peroxygenase-Catalysed Oxidation of Toluene Derivates to Benzaldehydes","Wang, Y. (TU Delft BT/Biocatalysis; Tianjin University); Teetz, Niklas (University of Applied Sciences Mittelhessen); Holtmann, Dirk (University of Applied Sciences Mittelhessen); Alcalde, Miguel (Institute of Catalysis, CSIC, Madrid); van Hengst, J.M.A. (TU Delft BT/Biocatalysis); Liu, Xiaoxiao (Chinese Academy of Sciences); Wang, Mengfan (Tianjin University); Qi, Wei (Tianjin University); Zhang, Wuyuan (Chinese Academy of Sciences); Hollmann, F. (TU Delft BT/Biocatalysis)","","2023","Biocatalytic oxidation reactions of toluene derivates to the corresponding aldehydes are typically challenged by regio- and chemoselectivity issues. In this contribution we address both challenges by a combined reactant- and reaction engineering approach. We demonstrate that the peroxygenase-catalysed transformation of ring-substituted toluenes proceeds highly regioselectively in benzylic position. Furthermore, neat reaction conditions not only enable attractive product concentrations (up to 185 mM) but also result in highly chemoselective oxidations to the aldehyde level.","Benzaldehydes; Biocatalytic oxidation; Peroxygenase; Selective oxyfunctionalisation; Solvent-free biocatalysis","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:af4301b8-c203-41db-9b9c-04c1c4e85028","http://resolver.tudelft.nl/uuid:af4301b8-c203-41db-9b9c-04c1c4e85028","A novel unspecific peroxygenase from Agaricus bisporus var. bisporus for biocatalytic oxyfunctionalisation reactions","Li, Tiantian (South China University of Technology); Liang, Hongjing (South China University of Technology); Wu, Bin (South China University of Technology); Lan, Dongming (South China University of Technology); Ma, Yunjian (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2023","Unspecific peroxygenases (UPOs) represent an emerging class of catalysts for the selective oxyfunctionalisation of C–H- and C = C groups. Until now, only a few UPOs have been characterised. In this study, we report a new peroxygenase identified from the Unspecific Peroxygenase Database. The UPO from Agaricus bisporus var. bisporus (AbvbUPO) has been heterologously expressed in Aspergillus niger and initially characterised with respect to its basic biochemical features. Furthermore, its catalytic properties were evaluated with enzymatic cascade reactions of choline oxidase (AnChOx) and AbvbUPO, which the AnChOx provided H2O2 necessary via reductive activation of oxygen in situ. Three types of oxyfunctionalizations, such as hydroxylation of ethylbenzene, epoxidations of styrene and cyclohexene, sulfoxidations of methyl phenyl sulfide and phenyl vinyl sulfide, were successfully achieved. We also investigated the activity of AbvbUPO on fatty acids in some more detail. The experimental results show that Under the above conditions, AbvbUPO had the higher activity for cyclohexene epoxidation and sulfonation of sulfide substrates. The concentration of epoxy cyclohexane was 2.91 mM, and the concentration of methyl phenyl sulfoxide was 3.69 mM. The regioselectivity of AbvbUPO was ω-1 bonds position of linear saturated fatty acid. All in all, AbvbUPO exhibits some interesting differences which may put the basis for further understanding of the factors determining peroxygenase selectivity.","Agaricus bisporus var. bisporus; Heme-thiolate peroxidase; Heterologous expression; Oxyfunctionalisation; Unspecific peroxygenase","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:dba1bf53-dc4f-490b-8abc-ecc524e821e1","http://resolver.tudelft.nl/uuid:dba1bf53-dc4f-490b-8abc-ecc524e821e1","Biosynthesis of cyclic ketones by a H2O2 self-sufficient cascade reaction","Wu, Bin (South China University of Technology); Wang, Xiangyun (South China University of Technology); Yang, Bo (South China University of Technology); Ma, Yunjian (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology; Guangdong Youmei Institute of Intelligent Bio-manufacturing Co. Ltd.)","","2023","In the present work we propose a bienzymatic cascade for the oxyfunctionalisation of cycloalkanes to cyclic alcohols/cyclic ketones. By combining a H2O2-dependent peroxygenase with a O2-consuming and H2O2-producing alcohol oxidase an overall aerobic oxidation system was established. A convincing proof-of-concept is presented and some current limitations are outlined.","Alcohol oxidase; Cyclohexanone; HO self-cycling; Unspecific peroxygenase","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:69f97604-bdda-466f-8482-91a0884fcfff","http://resolver.tudelft.nl/uuid:69f97604-bdda-466f-8482-91a0884fcfff","Chemoenzymatic intermolecular haloether synthesis","Chen, Shaohang (Wuhan University of Science and Technology); Zhang, Jiaan (Wuhan University of Science and Technology); Zeng, Zhigang (Wuhan University of Science and Technology); Dai, Zongjie (Chinese Academy of Sciences); Wang, Qinhong (Chinese Academy of Sciences); Wever, Ron (Universiteit van Amsterdam); Hollmann, F. (TU Delft BT/Biocatalysis); Zhang, W. (TU Delft BT/Biocatalysis; Chinese Academy of Sciences)","","2022","A chemoenzymatic method for the synthesis of haloethers is presented. A combination of enzymatic hypohalite synthesis with spontaneous oxidation of alkenes and nucleophilic attack by various alcohols enabled the synthesis of a wide range of haloethers. The reaction system has been characterised and current imitations have been worked out. In the present, aqueous reaction system, hydroxyhalide formation represents the main undesired side reaction. Nevertheless, semi-preparative scale synthesis of a range of haloethers is demonstrated.","Chemoenzymatic synthesis; Ether synthesis; Haloetherification; Vanadium chloroperoxidase","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:3bbaa07a-58eb-4443-b5df-f88301aa8ce6","http://resolver.tudelft.nl/uuid:3bbaa07a-58eb-4443-b5df-f88301aa8ce6","More efficient enzymatic cascade reactions by spatially confining enzymes via the SpyTag/SpyCatcher technology","Zhong, Xuanru (South China University of Technology); Ma, Yunjian (South China University of Technology; Macau University of Science and Technology); Zhang, Xizhen (South China University of Technology); Zhang, Jiahui (South China University of Technology); Wu, Bin (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology; Guangdong Youmei Institute of Inteligent Bio-manufacturing Co, Guangdong)","","2022","Hydrocarbon synthesis from (waste)oils enabled by a cascade of lipase-catalysed hydrolysis and decarboxylase-catalysed decarboxylation has become an active area of research en route to alternative, biobased fuels. However, Poor substrate transport efficiency is a major issue causing low reaction rates. This study focused on a protein self-assembly strategy based on SpyTag/SpyCatcher to overcome diffusion limitations. For this, two fusion proteins, TLL-Linker-SpyCatcher based on the lipase from Thermomyces lanuginosus and CvFAP-Linker-SpyTag based on the fatty acid photodecarboxylase from Chlorella variabilis were designed. A covalent multi-enzyme complex (TLL-CvFAP) was formed spontaneously by self-assembly of each enzyme. The effects of temperature, pH and molar ratio of self-assembled components on assembly efficiency were investigated. The results showed that the multi-enzyme complex TLL-CvFAP reached about 60% after 12 h of assembly, and the enzyme activity of the multienzyme complex was increased by about 50% compared to that of the corresponding non-assembled enzymes. Under optimized conditions 10 mM soybean oil were converted into 25 mM of the corresponding hydrocarbons, suggesting a good potential of biofuel synthesis.","CvFAP; Hydrocarbon biofuels; Multienzyme complex; SpyTag/SpyCatcher; TLL","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2022-08-23","","","BT/Biocatalysis","","",""
"uuid:4d977959-be7d-402f-b2ec-776883aca05e","http://resolver.tudelft.nl/uuid:4d977959-be7d-402f-b2ec-776883aca05e","Study on green extraction of limonene from orange peel and cascade catalysis to produce carvol and carvone in deep eutectic solvents","Li, Zongquan (South China University of Technology); Ma, Yunjian (South China University of Technology; Macau University of Science and Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology; Guangdong Youmei Institute of Intelligent Bio-manufacturing Co, Foshan)","","2022","Carvol and carvone are oxidation products from the natural product limonene. They are important raw materials for the flavours and fragrances industry and also act as pharmaceutical active ingredients. Orange waste peels possibly represent an attractive source for limonene, but studies on valorizing orange peel wastes are rare. In this study, we report a new enzymatic cascade system for the in-situ conversion of limonene from orange peel into valued-added carvol and carvone. The use of deep eutectic solvents (DES) allows for efficient in-situ extraction of limonene from waste orange peels. We propose a dual function use of DES as solvent for the extraction and the biocatalytic oxidation of limonene as well as cosubstrate to promote the oxidation reaction. Using ChCl-Pro-H2O DES for the extraction of limonene from waste orange peels, approximately 17 milligrams of limonene per gram of orange peel was achieved at 40°C for 24 h. Then, with ChCl-Pro-H2O DES as the extractant and reaction medium, a cascade reaction system of choline oxidase (ChOx) and unspecific peroxygenase (UPO) was established to catalyse the conversion of limonene into carvol and carvone. The concentration of the final products was up to about 1.6 mmol L−1. This study showed a biocatalytic transformation pathway and provides technical support for the high-value utilization of waste in orange peel.","Carvol; carvone; Cascade reaction; deep eutectic solvents; Orange peel waste","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2022-11-09","","","BT/Biocatalysis","","",""
"uuid:80b324be-727f-4831-8a5e-6a93014fc4f0","http://resolver.tudelft.nl/uuid:80b324be-727f-4831-8a5e-6a93014fc4f0","A Bienzymatic Cascade for the Complete Hydrolysis of Phthalic Acid Esters","Yang, Liu (South China University of Technology); Ma, Yunjian (South China University of Technology; Macau University of Science and Technology); Chen, Yebao (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (GuangdongYoumeiInstituteof IntelligentBio-manufacturing, Guangdong)","","2022","Phthalic acid esters (PAEs) are widely used as plastic additives to increase the flexibility and durability of plastics. Constantly leaching out from plastics, PAEs are ubiquitously found in the environment. As PAEs exhibit biological activities such as being endocrine disruptive, the quest for efficient degradation strategies continues. Here, we report a bienzymatic degradation system for PAEs to phthalic acid (PA) using a cascade comprising two hydrolases, EstJ6 and P8219. The reaction conditions were optimized with respect to concentrations of both enzymes, temperature, and initial pH. Finally, the substrate scope of the new cascade was investigated, revealing that particularly PAEs with relatively small alcohols were degraded to more than 90 %. This present study provides a potential doable biocatalytic strategy for the complete hydrolysis of PAEs.","cascade; degradation; hydrolase; phthalic acid; phthalic acid esters","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2023-02-10","","","BT/Biocatalysis","","",""
"uuid:2b75cc88-a569-4d82-91ba-a62e7669cc25","http://resolver.tudelft.nl/uuid:2b75cc88-a569-4d82-91ba-a62e7669cc25","A Novel Unspecific Peroxygenase from Galatian marginata for Biocatalytic Oxyfunctionalization Reactions","Ma, Yunjian (South China University of Technology; Macau University of Science and Technology); Liang, Hongjing (South China University of Technology); Zhao, Zexin (Hubei University of Technology); Wu, Bin (South China University of Technology); Lan, Dongming (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology; Guangdong Youmei Institute of Inteligent Bio-manufacturing Co, Guangdong)","","2022","Unspecific peroxygenases (UPOs, EC 1.11.2.1) are promising oxyfunctionalization catalysts because of their unique stereoselectivity. However, so far only a few UPOs have been reported. In this study, gene mining was used to identify a gene from Galerina marginata that coded for a novel UPO (GmaUPO). GmaUPO was expressed in Pichia pastoris X-33 by scale-up fermentation (the UPO activity of the culture supernatant was 118 U/L). GmaUPO exhibited a molecular weight of 40 kDa and exhibited highest activity at 35°C and pH 9, respectively. Furthermore, GmaUPO was demonstrated to catalyze the epoxidation, sulfoxidation, and hydroxylation of common substrates, particularly fatty acids such as tridecanoic acid. The molecular basis for GmaUPO regioselectivity for fatty acid hydroxylation was explored by molecular modelling. The regioselectivity was mostly governed by the architecture of the enzyme's active site.","Bioinformatics analysis; Galerina marginata; Heterologous expression; Oxyfunctionalization; Unspecific peroxygenase","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:1d0a18e4-a7eb-46bf-bbf2-5f73d516d441","http://resolver.tudelft.nl/uuid:1d0a18e4-a7eb-46bf-bbf2-5f73d516d441","Production of fatty alcohols from non-edible oils by enzymatic cascade reactions","Ma, Yunjian (South China University of Technology); Zhang, Xizhen (South China University of Technology); Li, Yongru (South China University of Technology); Li, Peilin (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2020","A biocatalytic cascade transforming castor oil into (R,Z)-octadec-9-en-7-ol is presented by combining a lipase catalysed hydrolysis of castor oil into ricinoleic acid followed by a photoenzymatic decarboxylation into (R,Z)-octadec-9-en-7-ol. Conversion of up to 41.7% and overall product concentrations of up to 60 mM, this new bienzymatic and photocatalytic cascade exhibits significant potential for the valorisation of non-edible castor oil. The scope and limitations of the current system are described and discussed.","","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:673b6d1d-be70-49f2-a313-4b7a2f9774e7","http://resolver.tudelft.nl/uuid:673b6d1d-be70-49f2-a313-4b7a2f9774e7","Photoenzymatic Production of Next Generation Biofuels from Natural Triglycerides Combining a Hydrolase and a Photodecarboxylase","Ma, Yunjian (South China University of Technology); Zhang, Xizhen (South China University of Technology); Zhang, W. (TU Delft BT/Biocatalysis); Li, Peilin (South China University of Technology); Li, Yongru (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2020","A photobiocatalytic cascade transforming natural triglycerides into alkanes/alkenes is proposed. Starting from natural triglycerides, free fatty acids have been obtained using lipases. The free fatty acids were then, in a photoenzymatic step, decarboxylated into the C1-shortened alkanes using a recently described photodecarboxylase from Chlorella variabilis NC64A. This cascade produced alkanes from various natural (waste) oils in significant amounts (up to 24 g L−1) and may provide a basis for valorisation of waste oils into a next generation of biodiesel.","biocatalysis; biodiesel; cascade reactions; decarboxylation; photocatalysis","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:b9c412ce-4af0-49c7-9cfe-23892e133859","http://resolver.tudelft.nl/uuid:b9c412ce-4af0-49c7-9cfe-23892e133859","Enantioselective Sulfoxidation of Thioanisole by Cascading a Choline Oxidase and a Peroxygenase in the Presence of Natural Deep Eutectic Solvents","Li, Yongru (South China University of Technology); Ma, Yunjian (South China University of Technology); Li, Peilin (South China University of Technology); Zhang, Xizhen (South China University of Technology); Ribitsch, Doris (acib GmbH); Alcalde, Miguel (Institute of Catalysis, CSIC, Madrid); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2020","A bienzymatic cascade for selective sulfoxidation is presented. The evolved recombinant peroxygenase from Agrocybe aegeritra catalyses the enantioselective sulfoxidation of thioanisole whereas the choline oxidase from Arthrobacter nicotianae provides the H2 O2 necessary via reductive activation of ambient oxygen. The reactions are performed in choline chloride-based deep eutectic solvents serving as co-solvent and stoichiometric reductant at the same time. Very promising product concentrations (up to 15 mM enantiopure sulfoxide) and catalyst performances (turnover numbers of 150,000 and 2100 for the peroxygenase and oxidase, respectively) have been achieved.","biocatalysis; enantioselectivity; natural deep eutectic solvents; peroxygenases; sulfoxidation","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:2a7d5730-b175-43d0-be68-2e5b72464403","http://resolver.tudelft.nl/uuid:2a7d5730-b175-43d0-be68-2e5b72464403","Chemoenzymatic Halocyclization of γ,δ-Unsaturated Carboxylic Acids and Alcohols","Younes, S.H.H. (TU Delft BT/Biocatalysis; Sohag University); Tieves, F. (TU Delft BT/Biocatalysis); Lan, Dongming (South China University of Technology); Wang, Yonghua (South China University of Technology); Süss, Philipp (Enzymicals AG, Greifswald); Brundiek, Henrike (Enzymicals AG, Greifswald); Wever, Ron (Van ’t Hoff Institute of Molecular Sciences); Hollmann, F. (TU Delft BT/Biocatalysis)","","2019","A chemoenzymatic method for the halocyclization of unsaturated alcohols and acids by using the robust V-dependent chloroperoxidase from Curvularia inaequalis (CiVCPO) as catalyst has been developed for the in situ generation of hypohalites. A broad range of halolactones and cyclic haloethers are formed with excellent performance of the biocatalyst.","biocatalysis; enzymes; etherification; haloperoxidases; lactones","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:0475d555-416d-4feb-97fb-066c951c6c5a","http://resolver.tudelft.nl/uuid:0475d555-416d-4feb-97fb-066c951c6c5a","How To Break the Janus Effect of H 2 O 2 in Biocatalysis? Understanding Inactivation Mechanisms To Generate more Robust Enzymes","Zhao, Ze Xin (South China University of Technology); Lan, Dongming (South China University of Technology); Tan, Xiyu (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Bornscheuer, Uwe T. (Greifswald University); Yang, Bo (South China University of Technology); Wang, Yonghua (South China University of Technology)","","2019","H 2 O 2 , is an attractive oxidant for synthetic chemistry, especially if activated as percarboxylic acid. H 2 O 2 , however, is also a potent inactivator of enzymes. Protein engineering efforts to improve enzyme resistance against H 2 O 2 in the past have mostly focused on tedious probabilistic directed evolution approaches. Here we demonstrate that a rational approach combining multiscale MD simulations and Born-Oppenheimer ab initio QM/MM MD simulations is an efficient approach to rapidly identify improved enzyme variants. Thus, the lipase from Penicillium camembertii was redesigned with a single mutation (I260R), leading to drastic improvements in H 2 O 2 resistance while maintaining the catalytic activity. Also the extension of this methodology to other enzymes is demonstrated.","epoxidation; H O; inactivation; lipase; multiscale MD; QM/MM MD","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2019-08-28","","","BT/Biocatalysis","","",""
"uuid:e27fa935-b576-4eec-826f-050499979d79","http://resolver.tudelft.nl/uuid:e27fa935-b576-4eec-826f-050499979d79","An Efficient Strategy for the Production of Epoxidized Oils: Natural Deep Eutectic Solvent-Based Enzymatic Epoxidation","Zhang, Tianyu (South China University of Technology); Ma, Yunjian (South China University of Technology); Tan, Chin Ping (Universiti Putra Malaysia); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Jianrong (South China University of Technology); Yang, Bo (South China University of Technology); Wang, Yonghua (South China University of Technology)","","2019","Poor H 2 O 2 -resistance by enzymes is a key bottleneck in the epoxidation process of oil by enzymatic methods. In this study, the stability of three lipases, from Aspergillus oryzae lipase (AOL), Aspergillus fumigatus lipase B (AflB), and marine Janibacter (MAJ1), in the presence of H 2 O 2 was evaluated in different types of natural deep eutectic solvents (NADES). This stability was strengthened significantly in the NADES compared to the buffer. Specifically, AOL retained 84.7% of its initial activity in the presence of choline chloride/sorbitol (1:1 M ratio) and 3 mol L −1 H 2 O 2 after 24 h incubation at 40°C. In addition, the two-phase epoxidation process was optimized with AOL in ChCl/sorbitol to reach up to 96.8% conversion under the optimized conditions (molar ratio of octanoic acid/H 2 O 2 /C=C-bonds = 0.3:1.5:1, enzyme loading of 15 U g −1 of soybean oil, ChCl/sorbitol content of 70.0% of the weight of hydrophilic phase, and reaction temperature of 50°C). Moreover, the lipase dispersed in NADES retained approximately 66% of its initial activity after being used for seven batch cycles. Overall, NADES-based enzymatic epoxidation is a feasible and promising strategy for the synthesis of epoxidized oils.","Enzyme catalysis; Epoxidation; Lipase; Natural deep eutectic solvent; Soybean oil","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2019-09-20","","","BT/Biocatalysis","","",""
"uuid:09808c27-e933-4cf3-8629-a0bd66f404ea","http://resolver.tudelft.nl/uuid:09808c27-e933-4cf3-8629-a0bd66f404ea","Biocatalytic Oxidation Reactions: A Chemist's Perspective","Dong, J. (TU Delft BT/Biocatalysis); Fernandez Fueyo, E. (TU Delft BN/Greg Bokinsky Lab); Hollmann, F. (TU Delft BT/Biocatalysis); Paul, C.E. (TU Delft BT/Biocatalysis); Pesic, M. (TU Delft BT/Biocatalysis); Schmidt, S. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology); Younes, S.H.H. (TU Delft BT/Biocatalysis); Zhang, W. (TU Delft BT/Biocatalysis)","","2018","Oxidation chemistry using enzymes is approaching maturity and practical applicability in organic synthesis. Oxidoreductases (enzymes catalysing redox reactions) enable chemists to perform highly selective and efficient transformations ranging from simple alcohol oxidations to stereoselective halogenations of non‐activated C−H bonds. For many of these reactions, no “classical” chemical counterpart is known. Hence oxidoreductases open up shorter synthesis routes based on a more direct access to the target products. The generally very mild reaction conditions may also reduce the environmental impact of biocatalytic reactions compared to classical counterparts. In this Review, we critically summarise the most important recent developments in the field of biocatalytic oxidation chemistry and identify the most pressing bottlenecks as well as promising solutions.","German Edition :D OI:10.1002/ange.201800343 Bioc atalys is International Edition :DOI:10.1002/anie.201800343 Biocatalytic Oxidation Reactions :AChemist s Perspectiv e JiaJia Dong ,Elena Fern μ ndez-Fueyo ,Frank Hollmann,* Caroline E. Paul, Milja Pesic,Sandy Schmidt, Yonghua Wang,Sabry Younes,and Baeyer–Villiger oxidation; biocatalysis; halogenation; oxidation; oxyfunctionalisation","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:9848d77d-a98a-45c5-8077-aa3735d53f04","http://resolver.tudelft.nl/uuid:9848d77d-a98a-45c5-8077-aa3735d53f04","Production and immobilization of lipase PCL and its application in synthesis of α‐linolenic acid‐rich diacylglycerol","Liu, Nan (South China University of Technology); Liu, D. (South China University of Technology); Wang, Weifei (Guangdong Academy of Agricultural Sciences); Hollmann, F. (TU Delft BT/Biocatalysis); Xu, Long (South China University of Technology); Ma, Yunjian (South China University of Technology); Yang, Bo (South China University of Technology); Bai, Weidong (Zhongkai University of Agriculture and Engineering); Sun, Xiaotao (Beijing Technology and Business University); Wang, Yonghua (South China University of Technology)","","2018","α‐Linolenic acid‐rich diacylglycerol has been demonstrated with promising health promotion functions. This study examined the production, immobilization of lipase PCL, and its application in the synthesis of diacylglycerol by esterification of α‐linolenic acid with glycerol. The resin ECR8806 was selected as an effective support for the immobilization of lipase PCL. Fourier transform infrared and Laser scanning confocal microscope analysis proved that the lipase was successfully immobilized on the resin. Compared with the free PCL, the immobilized one exhibited higher temperature tolerance. Under optimized reaction conditions, a DAG content of 54.49% were obtained. After further purified by molecular distillation, the purity of DAG was up to 99.28%. During esterification, the immobilized PCL was quite stable and retained more than 91.60% of its initial activity after 10 cycles. These new findings on the immobilized PCL will make it to be a prospective enzyme in oils and fats industry.","diacylglycerol; esterification; immobilization; reusability; a-Linolenic acid","en","journal article","","","","","","Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.","","2019-01-23","","","BT/Biocatalysis","","",""
"uuid:6c83bfc3-a1b8-4ec2-8274-29ec38853207","http://resolver.tudelft.nl/uuid:6c83bfc3-a1b8-4ec2-8274-29ec38853207","Biocatalytic synthesis of lactones and lactams","Hollmann, F. (TU Delft BT/Biocatalysis); Kara, Selin (Aarhus University); Opperman, Diederik J. (University of the Free State); Wang, Yonghua (South China University of Technology)","","2018","Cyclic esters and amides (lactones and lactams) are important active ingredients and polymer building blocks. In recent years, numerous biocatalytic methods for their preparation have been developed including enzymatic and chemoenzymatic Baeyer–Villiger oxidations, oxidative lactonisation of diols, and reductive lactonisation and lactamisation of ketoesters. The current state of the art of these methods is reviewed.","Baeyer–Villiger oxidation; biocatalysis; lactams; lactones; oxidative Lactonisation","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:a345fd42-53c1-4ff9-a154-f0d08e8fb868","http://resolver.tudelft.nl/uuid:a345fd42-53c1-4ff9-a154-f0d08e8fb868","Peroxygenases en route to becoming dream catalysts. What are the opportunities and challenges?","Wang, Yonghua (South China University of Technology); Lan, Dongming (South China University of Technology); Durrani, Rabia (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis)","","2017","Peroxygenases are promising catalysts for preparative oxyfunctionalization chemistry as they combine the versatility of P450 monooxygenases with simplicity of cofactor-independent enzymes. Though many interesting applications have been reported, today ‘we have only scratched the surface’ and significant efforts are necessary to solve issues related to selectivity of the wild type enzymes and low product titers. For this, further elucidation of the vast natural diversity as well as protein and reaction engineering approaches are discussed.","","en","review","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:48239759-6d0c-4aea-a203-a1313270040c","http://resolver.tudelft.nl/uuid:48239759-6d0c-4aea-a203-a1313270040c","Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity","Wang, Xu Ping (South China University of Technology); Zhou, Peng Fei (South China University of Technology); Li, Zhi Gang (South China University of Technology); Yang, Bo (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yong Hua (South China University of Technology)","","2017","A Ser105Ala mutant of the lipase B from Candida antarctica enables 'perhydrolase-only' reactions. At the example of the chemoenzymatic Baeyer-Villiger oxidation of cyclohexanone, we demonstrate that with this mutant selective oxidation can be achieved in deep eutectic solvent while essentially eliminating the undesired hydrolysis reaction of the product.","","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:c8ac51cf-26b8-4a8f-a48d-dbe419e9f7aa","http://resolver.tudelft.nl/uuid:c8ac51cf-26b8-4a8f-a48d-dbe419e9f7aa","Deep Eutectic Solvents Enable More Robust Chemoenzymatic Epoxidation Reactions","Zhou, Pengfei (South China University of Technology); Wang, Xuping (South China University of Technology); Zeng, Chaoxi (South China University of Technology); Wang, Weifei (South China University of Technology); Yang, Bo (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2017","A chemoenzymatic method for the production of epoxidized vegetable oils was developed. The unique combination of the commercial lipase G from Penicillieum camembertii with certain deep eutectic solvents enabled the efficient production of epoxidized vegetable oils.","chemoenzymatic synthesis; deep eutectic solvents; enzymes; epoxidation; fatty acids","en","journal article","","","","","","Accepted Author Manuscript","","2017-12-25","","","BT/Biocatalysis","","",""
"uuid:a472564f-492d-4094-8de3-fdf53a84d095","http://resolver.tudelft.nl/uuid:a472564f-492d-4094-8de3-fdf53a84d095","Chemoenzymatic epoxidation of alkenes with Candida antarctica lipase B and hydrogen peroxide in deep eutectic solvents","Zhou, Pengfei (South China University of Technology); Wang, Xuping (South China University of Technology); Yang, Bo (South China University of Technology); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2017","Epoxides are important synthetic intermediates for the synthesis of a broad range of industrial products. This study presents a promising solution to the current limitation of enzyme instability. By using simple deep eutectic solvents such as choline chloride/sorbitol, significant stabilization of the biocatalyst has been achieved leading to more robust reactions while using environmentally more acceptable solvents as compared to ionic liquids.","","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""
"uuid:1796eb34-d924-48d8-93b8-3958a223cb99","http://resolver.tudelft.nl/uuid:1796eb34-d924-48d8-93b8-3958a223cb99","Deep eutectic solvents as performance additives in biphasic reactions","Lan, Dongming (South China University of Technology); Wang, Xuping (Guangdong Academy of Agricultural Sciences); Zhou, Pengfei (Guangdong Academy of Agricultural Sciences); Hollmann, F. (TU Delft BT/Biocatalysis); Wang, Yonghua (South China University of Technology)","","2017","Deep eutectic solvents act as surfactants in biphasic (hydrophobic/aqueous) reaction mixtures enabling higher interfacial surface areas at lower mechanical stress as compared to simple emulsions. Exploiting this effect the rate of a chemoenzymatic epoxidation reaction was increased more than six-fold.","","en","journal article","","","","","","","","","","","BT/Biocatalysis","","",""