{"title":"Biocatalytic synthesis of dioctyl sebacate in toluene using an immobilised lipase","authors":"Mingxin Zhu, Shuyi Guo, Rongchen Mang, Hua Zhou","doi":"10.1080/10242422.2022.2087512","DOIUrl":"https://doi.org/10.1080/10242422.2022.2087512","url":null,"abstract":"Abstract Sebacic esters have excellent lubricity, thermal stability, and biodegradability and therefore are widely used as aerospace lubricants, metal working oil, or engine oil. They are mainly produced by chemical synthesis which, however, may cause environmental pollution, its enzymatic synthesis represents a more environmentally friendly alternative. A few reports have described the synthesis of sebacic esters employing immobilised lipases, but these biocatalytic reactions were exclusively carried out in solvent-free systems and thus, could have been limited by slow reaction rates and high reaction temperatures due to poor enzyme dispersion, low substrate solubility, and high viscosity of the reaction mixture. The current study investigated the biosynthesis of dioctyl sebacate in toluene by Novozym 435, a commercial immobilised lipase. The reaction parameters were investigated using the single factor approach and an orthogonal array design. The optimal conditions obtained were as follows: 10 mL toluene, sebacic acid,1 mmol (202.25 mg); molar ratio of sebacic acid to 1-octanol, 1:3; Novozym 435, 0.03 g; 4 Å molecular sieves, 1.5 g; reaction temperature, 40 °C; reaction time, 30 h. A dioctyl sebacate conversion rate of 93% was achieved under these optimal conditions. In particular, the addition of molecular sieves to the reaction mixture markedly improved the product yield. The reaction temperature was low enough to make the operation easy and energy-efficient and therefore, well suited for large-scale production.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44827323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova
{"title":"Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium","authors":"O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova","doi":"10.1080/10242422.2022.2085034","DOIUrl":"https://doi.org/10.1080/10242422.2022.2085034","url":null,"abstract":"Abstract A comparative study of the ability of Trametes hirsuta laccase isoenzymes to biotransform 17β-oestradiol (3,17β-dihydroxyestra-1,3,5(10)-triene, E2) was carried out. Native major LacA and recombinant minor isoenzymes (rLacC, rLacD, and rLacF) obtained in Penicillium canescens were used. It was found that all the studied isozymes are capable of catalysing the oxidative coupling of E2 in an aqueous medium (22 ± 2 °C, pH 4.5) with the formation of predominantly dimers and trimers. Other concurrently formed products were detected by high-pressure liquid chromatography – high-resolution mass spectrometry (HPLC–HRMS) and characterized, summarizing the overall condensation pathway of E2 in laccases. The highest catalytic activity was observed for major LacA. For other laccases, the activity decreased in the following sequence rLacF > rLacD > rLacC. Utilization of T. hirsuta enzymatic variety of laccases can be of benefit for detoxification of phenol-like steroid compounds in the environment.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48801490","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Remediation of chlorpyrifos in soil using immobilized bacterial consortium biostimulated with organic amendment","authors":"Elizabeth Mary John, J. Sreekumar, M. S. Jisha","doi":"10.1080/10242422.2022.2085033","DOIUrl":"https://doi.org/10.1080/10242422.2022.2085033","url":null,"abstract":"Pesticides released into the environment have become a danger to the mother earth arousing a worldwide alert to initiate remediation at the point sources of contamination in an ecofriendly way. The...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138515806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A biocatalytic system obtained via immobilization of urease onto magnetic metal/alginate nanocomposite: Improving reusability and enhancing stability","authors":"O. Almaghrabi, Y. Almulaiky","doi":"10.1080/10242422.2022.2082871","DOIUrl":"https://doi.org/10.1080/10242422.2022.2082871","url":null,"abstract":"Abstract Alginate is a biomaterial that is considered suitable for enzyme immobilization. The biocompatibility and characteristics of the immobilized system can be improved by combining alginate with magnetite Fe3O4 nanoparticles. Therefore, the current study investigated the effect of magnetite Fe3O4 NPs on urease immobilization using different concentrations of magnetite Fe3O4 NPs. The morphological features for alginate/magnetite Fe3O4 NPs before and after immobilization were studied using an SEM, TGA, and FTIR. The reusability, half-life, enzymatic kinetics, and storage stability of the enzyme were all enhanced. The immobilization efficiency was determined to be 91% at optimal conditions. The immobilized urease was reused 20 times and a recovery of 59% of the initial activity. The soluble and immobilized urease was stored at 4 °C for 12 weeks and preserved 13% and 49% of the initial activities, respectively. The optimum pH for soluble and immobilized urease activity was estimated to be 7. The optimum temperature for soluble and immobilized urease activity was found to be 35 °C and 40 °C, respectively. The kinetics parameters showed the Vmax of 4.4 and 3.1 μmol/ml·min and the Km of 49.5 and 54.6 mM for the soluble and immobilized urease, respectively. Immobilized urease had a half-life of 11–20 min. The activation energy (Ea) of immobilized urease was determined to be 32 kJ K−1 mol−1, indicating that a small quantity of energy is required to produce the activated complex of substrate hydrolysis.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47825227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Thermo-active and alkaliphilic amalgamated laccase immobilized on sodium alginate for synthetic dye decolourization","authors":"Chiedu E. Edoamodu, Uchechukwu U. Nwodo","doi":"10.1080/10242422.2022.2078661","DOIUrl":"https://doi.org/10.1080/10242422.2022.2078661","url":null,"abstract":"Purified crude laccase of Enterobacter sp. Kamsi and Bacillus sp. NU2 in the hybrid and combined form was immobilized on sodium alginate beads and applied to decolourize various textile dyes throug...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-05-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138515800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Biotransformation of chalcones and flavanones: An update on their bio-based derivatizations","authors":"L. Aguiar, E. Silva, J. David","doi":"10.1080/10242422.2022.2073226","DOIUrl":"https://doi.org/10.1080/10242422.2022.2073226","url":null,"abstract":"Abstract Chalcones and flavanones are both present as secondary metabolites in edible and medicinal plants as isomers. Mostly of them are isolated in low yields from natural sources, along with the difficulties faced by the total synthesis, make them attractive for biotechnological studies in order to obtain new derivatives. Prompted by the enormous pharmacological interest in chalcones and flavanones compounds, their alimentary and chemical applications, this review covers their biotransformation as an alternative way for achieving chemical analogues with high selectivity, using mild and eco-friendly conditions. Stereoselective bioreductions of chalcones were the most reported biotransformation reactions, and they could be performed by bacteria, cyanobacteria, non-conventional yeasts (NCYs), and fungi strains with good yields. Flavanones have also been derivatized under stereochemical control by several microorganisms. All reported biotransformations contribute to increasing the availability of new and valuable leads for the market and industrial fields.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-05-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43957047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
N. Aminudin, Nurul Aqilah Amran, Zaima Azira Zainal Abidin, D. Susanti
{"title":"Biotransformation of curcumin and structure–activity relationship (SAR) of its analogues: A systematic review","authors":"N. Aminudin, Nurul Aqilah Amran, Zaima Azira Zainal Abidin, D. Susanti","doi":"10.1080/10242422.2022.2073227","DOIUrl":"https://doi.org/10.1080/10242422.2022.2073227","url":null,"abstract":"Abstract Curcumin has been widely acclaimed for several pharmacological properties, such as antioxidant, antimicrobial, anticancer, and anti-inflammation. Curcumin’s poor aqueous solubility, bioavailability, and cellular uptake hamper its ability to display maximum pharmacological effect in the human body. Synthesis of curcumin analogues to enhance its properties can be achieved through biotransformation. Greener, simpler, and higher selectivity and specificity make biotransformation an alternative approach when preparing curcumin analogues for the structure–activity relationship (SAR) study intended for drug design. This work systematically reviews the biotransformation of curcumin by utilizing fungi, gut microbiota, and enzymes. The SAR study of curcumin and its analogues for several bioactivities is also highlighted. Graphical Abstract","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49003739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Solís, Abraham Cano, R. M. Martínez-Cásares, M. Solís-Oba, R. Castro-Rivera, Oscar Velázquez Flores
{"title":"Preparation of optically active cyanohydrins from 2-substituted benzaldehydes using a hydroxynitrile lyase from Pouteria sapota seeds immobilized on celite","authors":"A. Solís, Abraham Cano, R. M. Martínez-Cásares, M. Solís-Oba, R. Castro-Rivera, Oscar Velázquez Flores","doi":"10.1080/10242422.2022.2070430","DOIUrl":"https://doi.org/10.1080/10242422.2022.2070430","url":null,"abstract":"Abstract The HNL from the defatted meal of the seeds of Pouteria sapota (PsHNL) was extracted with water, and the aqueous extract was immobilized over celite or lyophilized and used as semi-purified PsHNL. The aqueous extract was mixed with celite, ratios 1:1, 1:2 and 1:4, and lyophilized. The immobilized PsHNLdir-celite catalysed the addition of HCN to 1b in buffer saturated-DIPE (microaqueous system) with high enantioselectivity in the first cycle but diminished in the next two cycles, best results were obtained with the ratio 1:4. The reaction with PsHNLdir-celite in biphasic medium (5% citrates buffer) improved the conversion compared with the microaqueous system, but it was still lower to that obtained with the PsHNL. Other way of immobilization studied was the precipitation of the enzyme with acetone and immobilization on celite, the PsHNLpp-celite catalysed the enantioselective addition of HCN to 2-fluoro (1a), 2-chloro (1b), 2-bromo (1c), 2-methyl (1d) and 2-nitro (1e) benzaldehydes, in the biphasic medium (1:4 ratio, 5% citrates buffer). The enantiomeric excess (ee) of (R)-2a, (R)-2b, (R)-2c and (R)-2d were >98% and remained during the three cycles. The ee of 2-nitromandelonitrile was 82% and was raised to 95% in the third cycle. Compared with the PsHNL, the conversion of 1a and 1b diminished 6% and 40%, respectively, after third cycle; for 2c, conversion was almost 10% higher in the first two cycles and diminished 19% in the third; for 2d and 2e the conversion was between 18–13% and 31–18% higher, respectively.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48062976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. M. Baron, Ricardo de Sousa Rodrigues, Luis Guilherme Giannina Sante, Jocácia Muriele de Miranda Kister, Valéria Marta Gomes do Nascimento, Alesandro Bail
{"title":"Metal-organic framework based on iron and terephthalic acid as a multiporous support for lipase Burkholderia lata LBBIO-BL02 and its potential for biocatalysis","authors":"A. M. Baron, Ricardo de Sousa Rodrigues, Luis Guilherme Giannina Sante, Jocácia Muriele de Miranda Kister, Valéria Marta Gomes do Nascimento, Alesandro Bail","doi":"10.1080/10242422.2022.2068371","DOIUrl":"https://doi.org/10.1080/10242422.2022.2068371","url":null,"abstract":"Abstract Metal-organic frameworks (MOFs) are versatile materials because they have a large internal surface area and tuneable pores, making them suitable for enzyme immobilization. In this study, we prepared a typical microporous Fe-BDC MOF through a thermal treatment to produce additional meso and macropores interconnected to each other, capable of immobilizing the Burkholderia lata LBBIO-BL02 (BLL) lipase by entrapment and physical adsorption. The immobilization efficiency (E) was 90%, and the activity retention (R) was 400% (pNPP hydrolysis). The immobilized lipase (BLL@BDC) also showed excellent activity in the hydrolysis of vegetable oils in aqueous medium, achieving up to 3,200 U g−1 for olive oil, as well as high stability in organic solvents, especially for polar ones, such as iso-propanol (101.5 ± 2.6%), ethanol (103.0 ± 6.0%) and acetone (107.7 ± 8.3%). The results indicate that the multiporous Fe-BDC MOF is a promising support for lipase immobilization and further application in biocatalysis performed in organic media. Graphical Abstract","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48516749","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Protease immobilization on activated chitosan/cellulose acetate electrospun nanofibrous polymers: Biochemical characterization and efficient protein waste digestion","authors":"Arastoo Badoei-dalfard, Mahla Saeed, Z. Karami","doi":"10.1080/10242422.2022.2056450","DOIUrl":"https://doi.org/10.1080/10242422.2022.2056450","url":null,"abstract":"Abstract In this paper, a Serratia marcescens fibrinolytic protease KD was covalently immobilized onto the electrospun prepared glutaraldehyde (GA)-functionalized chitosan/cellulose acetate membrane nanofibres. Enzyme immobilization has been optimized at some conditions such as different GA values, different crosslinking times, different enzyme and pH values, and different times of immobilization. Results exhibited that the optimized immobilization conditions were obtained in 5.0% GA, after 4 h of crosslinking time, after 8 h immobilization time, using 210 mg protein/g support at pH 9.0. Based on these optimal conditions, the best encapsulation yield (EY) and activity recovery (AR) were obtained about 85% and 121.3%, respectively. The immobilized protease showed a 52% enhancement in protease activity than the free protease in pH 10. Furthermore, results displayed that the V max values of free and immobilized enzymes towards casein were gained 0.491 and 0.79 µmol/min, respectively. Moreover, the activity of immobilized protease was retained about 75% after incubation at 60 °C for 180 min at pH 9.0, in which the free protease only preserved about 20% of its primary activity. Results exhibited that the protease-NFs kept nearly 73% of its initial activity after three weeks of storage, while the free protease retained about 20% of its initial activity at the same condition. Results showed that the free protease exhibited 31% clot lysis, whereas the immobilized enzyme exhibited 39% clot lysis. The highest hydrolysis value of both proteases was done 17 and 48% after 4 h at 40 °C, respectively. These results indicated that Chit/CA electrospun nanofibres are excellent membranes for protease immobilization with high application in the digestion of protein waste.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2022-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49096601","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}