Pub Date : 2019-01-01DOI: 10.1007/978-3-030-25023-2_12
P. Fernandes
{"title":"Enzymes in Food and Feed Industries: Where Tradition Meets Innovation","authors":"P. Fernandes","doi":"10.1007/978-3-030-25023-2_12","DOIUrl":"https://doi.org/10.1007/978-3-030-25023-2_12","url":null,"abstract":"","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"35 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78603503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1007/978-3-030-25023-2_6
O. Prakash, Saumya Khare
{"title":"Immobilization of α-amylases and Their Analytical Applications","authors":"O. Prakash, Saumya Khare","doi":"10.1007/978-3-030-25023-2_6","DOIUrl":"https://doi.org/10.1007/978-3-030-25023-2_6","url":null,"abstract":"","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"4 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83821097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1007/978-3-030-25023-2_5
Rubia Noori, M. Perwez, M. Sardar
{"title":"Cross-linked Enzyme Aggregates: Current Developments and Applications","authors":"Rubia Noori, M. Perwez, M. Sardar","doi":"10.1007/978-3-030-25023-2_5","DOIUrl":"https://doi.org/10.1007/978-3-030-25023-2_5","url":null,"abstract":"","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"3 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82110551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1007/978-3-030-25023-2_8
Yanfeng Liu, Long Liu
{"title":"Screening, Optimization and Assembly of Key Pathway Enzymes in Metabolic Engineering","authors":"Yanfeng Liu, Long Liu","doi":"10.1007/978-3-030-25023-2_8","DOIUrl":"https://doi.org/10.1007/978-3-030-25023-2_8","url":null,"abstract":"","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"11 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87140976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1007/978-3-030-25023-2_14
A. Piotrowska-Długosz
{"title":"Significance of Enzymes and Their Application in Agriculture","authors":"A. Piotrowska-Długosz","doi":"10.1007/978-3-030-25023-2_14","DOIUrl":"https://doi.org/10.1007/978-3-030-25023-2_14","url":null,"abstract":"","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"43 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85750356","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Abstract The present paper demonstrates application of biocatalysis to the synthesis of ethyl hexanoate, i.e. pineapple flavour ester, in a solvent free system. In order to evaluate the effect of various process parameters on reaction conversion, response surface methodology (RSM) complemented by central composite design (CCD) was employed. A maximum conversion of 88.57% was obtained while changing one factor at a time, at optimum conditions of temperature (50 °C), enzyme dose (2%), molar ratio acid to alcohol (1:3), speed of agitation 250 rpm and reaction time of 120 min. Based on this RSM study, the optimum predicted conditions were: 1:3.39 alcohol to acid ratio, 2.35% enzyme loading and 48.83 oC, for a predicted conversion of 90.99%. The activation energy for the enzymatic esterification was determined and calculated to be 25.76 kJ/mol. The positive values of Gibbs-free energy (ΔG), enthalpy (ΔH) and negative value of entropy (ΔS) revealed that the esterification reaction was non-spontaneous and an endothermic reaction. The reaction seems to follow bi-substrate Ping Pong Bi Bi mechanism with inhibition by both substrates.
{"title":"Optimization of enzymatic synthesis of ethyl hexanoate in a solvent free system using response surface methodology (RSM)","authors":"Sarita D. Gawas, N. Lokanath, V. Rathod","doi":"10.1515/boca-2018-0002","DOIUrl":"https://doi.org/10.1515/boca-2018-0002","url":null,"abstract":"Abstract The present paper demonstrates application of biocatalysis to the synthesis of ethyl hexanoate, i.e. pineapple flavour ester, in a solvent free system. In order to evaluate the effect of various process parameters on reaction conversion, response surface methodology (RSM) complemented by central composite design (CCD) was employed. A maximum conversion of 88.57% was obtained while changing one factor at a time, at optimum conditions of temperature (50 °C), enzyme dose (2%), molar ratio acid to alcohol (1:3), speed of agitation 250 rpm and reaction time of 120 min. Based on this RSM study, the optimum predicted conditions were: 1:3.39 alcohol to acid ratio, 2.35% enzyme loading and 48.83 oC, for a predicted conversion of 90.99%. The activation energy for the enzymatic esterification was determined and calculated to be 25.76 kJ/mol. The positive values of Gibbs-free energy (ΔG), enthalpy (ΔH) and negative value of entropy (ΔS) revealed that the esterification reaction was non-spontaneous and an endothermic reaction. The reaction seems to follow bi-substrate Ping Pong Bi Bi mechanism with inhibition by both substrates.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"1 1","pages":"14 - 26"},"PeriodicalIF":0.0,"publicationDate":"2018-05-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86512991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Avram, A. Sengupta, P. Pfromm, H. Zorn, P. Lorenz, T. Schwarz, K. Q. Nguyen, P. Czermak
Abstract A novel Dye-decolorizing peroxidase from the basidiomycete Pleurotus sapidus was screened for dyedecolorizing peroxidase activity with 2,2‘-azino-bis(3- ethylbenzothiazoline-6-sulfonic acid), Remazol Brilliant Blue R and Guaiacol. Additionally, the catalytic efficiency on degrading β-carotene into volatile products, and the catalyst storage stability with three different additives were also studied. The apparent inhibition constant (KS) was 51.7 μM. Optimal reaction rates (Vmax) and affinity constants (Km) towards the reducing substrates were obtained using Michaelis-Menten kinetic theory. The trend in the calculated Km’s was found to be 7.0 mM > 0.524 mM > 0.051 mM for Guaiacol, 2,2‘-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and Remazol Brilliant Blue R. The storage stability of the catalyst was evaluated with 7.0% w/v PEG400, 7.0% w/v PEG1450 and 0.1% w/v Tween®80 at 5°C over a period of 45 days. The study revealed the longest activity conservation with PEG1450, where rDyP had lost 30% of initial activity. The enzyme solution presented similar pH and temperature dependence to known fungal dye-decolorizing peroxidases with most prolific enzymatic activities registered at pH 4.0 and temperatures below 30°C. An interesting property of the catalyst was oxidation observed in the absence of hydrogen peroxide.
摘要以2,2′-氮基-双(3-乙基苯并噻唑-6-磺酸)、雷马唑亮蓝R和愈创木酚为原料，从担子菌Pleurotus sapidus中筛选了一种新型染料脱色过氧化物酶。此外，还研究了三种不同添加剂对β-胡萝卜素降解为挥发性产物的催化效率以及催化剂的储存稳定性。表观抑制常数(KS)为51.7 μM。利用Michaelis-Menten动力学理论，得到了最佳反应速率(Vmax)和对还原底物的亲和常数(Km)。结果表明，愈创木酚、2,2′-氮基-双(3-乙基苯并噻唑-6-磺酸)和雷马唑亮蓝r的Km值变化趋势为7.0 mM > 0.524 mM > 0.051 mM。以7.0% w/v PEG400、7.0% w/v PEG1450和0.1% w/v Tween®80为催化剂，在5°C条件下保存45天。该研究揭示了PEG1450的活性保存时间最长，rDyP失去了30%的初始活性。该酶溶液具有与已知真菌染料脱色过氧化物酶相似的pH和温度依赖性，在pH 4.0和温度低于30°C时酶活性最高。催化剂的一个有趣的性质是在没有过氧化氢的情况下观察到氧化。
{"title":"Novel DyP from the basidiomycete Pleurotus sapidus: substrate screening and kinetics","authors":"A. Avram, A. Sengupta, P. Pfromm, H. Zorn, P. Lorenz, T. Schwarz, K. Q. Nguyen, P. Czermak","doi":"10.1515/boca-2018-0001","DOIUrl":"https://doi.org/10.1515/boca-2018-0001","url":null,"abstract":"Abstract A novel Dye-decolorizing peroxidase from the basidiomycete Pleurotus sapidus was screened for dyedecolorizing peroxidase activity with 2,2‘-azino-bis(3- ethylbenzothiazoline-6-sulfonic acid), Remazol Brilliant Blue R and Guaiacol. Additionally, the catalytic efficiency on degrading β-carotene into volatile products, and the catalyst storage stability with three different additives were also studied. The apparent inhibition constant (KS) was 51.7 μM. Optimal reaction rates (Vmax) and affinity constants (Km) towards the reducing substrates were obtained using Michaelis-Menten kinetic theory. The trend in the calculated Km’s was found to be 7.0 mM > 0.524 mM > 0.051 mM for Guaiacol, 2,2‘-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and Remazol Brilliant Blue R. The storage stability of the catalyst was evaluated with 7.0% w/v PEG400, 7.0% w/v PEG1450 and 0.1% w/v Tween®80 at 5°C over a period of 45 days. The study revealed the longest activity conservation with PEG1450, where rDyP had lost 30% of initial activity. The enzyme solution presented similar pH and temperature dependence to known fungal dye-decolorizing peroxidases with most prolific enzymatic activities registered at pH 4.0 and temperatures below 30°C. An interesting property of the catalyst was oxidation observed in the absence of hydrogen peroxide.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"19 1","pages":"1 - 13"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79105257","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Abstract Vanillyl alcohol oxidase (VAO) from Penicillium simplicissimum is a covalent flavoprotein that has emerged as a promising biocatalyst for the production of aromatic fine chemicals such as vanillin, coniferyl alcohol and enantiopure 1-(4’-hydroxyphenyl) alcohols. The largescale production of this eukaryotic enzyme in Escherichia coli has remained challenging thus far. For that reason an alternative, eukaryotic expression system, Komagataella phaffii, was tested. Additionally, to produce novel VAO biocatalysts, we screened genomes for VAO homologues. One bacterial and five fungal sequences were selected for expression, using key active site residues as criteria for their selection. Expression of the putative vao genes in K. phaffii was successful, however expression levels were low (1 mg per litre of culture). Surprisingly, all purified enzymes were found to contain a highly stable, non-covalently bound anionic FAD semiquinone that could not be reduced by dithionite or cyanoborohydride. Activity experiments revealed that VAO expressed in K. phaffii does not produce vanillin because the enzyme suffers from oxidative stress.
{"title":"Communication. Vanillyl alcohol oxidases produced in Komagataella phaffii contain a highly stable noncovalently bound anionic FAD semiquinone","authors":"G. Gygli, W. Berkel","doi":"10.1515/boca-2017-0002","DOIUrl":"https://doi.org/10.1515/boca-2017-0002","url":null,"abstract":"Abstract Vanillyl alcohol oxidase (VAO) from Penicillium simplicissimum is a covalent flavoprotein that has emerged as a promising biocatalyst for the production of aromatic fine chemicals such as vanillin, coniferyl alcohol and enantiopure 1-(4’-hydroxyphenyl) alcohols. The largescale production of this eukaryotic enzyme in Escherichia coli has remained challenging thus far. For that reason an alternative, eukaryotic expression system, Komagataella phaffii, was tested. Additionally, to produce novel VAO biocatalysts, we screened genomes for VAO homologues. One bacterial and five fungal sequences were selected for expression, using key active site residues as criteria for their selection. Expression of the putative vao genes in K. phaffii was successful, however expression levels were low (1 mg per litre of culture). Surprisingly, all purified enzymes were found to contain a highly stable, non-covalently bound anionic FAD semiquinone that could not be reduced by dithionite or cyanoborohydride. Activity experiments revealed that VAO expressed in K. phaffii does not produce vanillin because the enzyme suffers from oxidative stress.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"52 1","pages":"17 - 26"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85754854","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Abstract Numerous types of nanoparticles and nanocomposites have successfully been employed for the immobilization and stabilization of amylolytic enzymes; α-amylases, β-amylases, glucoamylases and pullulanases. Nano-support immobilized amylolytic enzymes retained very high activity and yield of immobilization. The immobilization of these enzymes, particularly α-amylases and pullulanases, to the nanosupports is helpful in minimizing the problem of steric hindrances during binding of substrate to the active site of the enzyme. The majority of nano-support immobilized amylolytic enzymes exhibited very high resistance to inactivation induced by different kinds of physical and chemical denaturants and these immobilized enzyme preparations maintained very high activity on their repeated and continuous uses. Amylolytic enzymes immobilized on nano-supports have successfully been applied in food, fuel, textile, paper and pulp, detergent, environmental, medical, and analytical fields.
{"title":"Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review","authors":"Q. Husain","doi":"10.1515/boca-2017-0004","DOIUrl":"https://doi.org/10.1515/boca-2017-0004","url":null,"abstract":"Abstract Numerous types of nanoparticles and nanocomposites have successfully been employed for the immobilization and stabilization of amylolytic enzymes; α-amylases, β-amylases, glucoamylases and pullulanases. Nano-support immobilized amylolytic enzymes retained very high activity and yield of immobilization. The immobilization of these enzymes, particularly α-amylases and pullulanases, to the nanosupports is helpful in minimizing the problem of steric hindrances during binding of substrate to the active site of the enzyme. The majority of nano-support immobilized amylolytic enzymes exhibited very high resistance to inactivation induced by different kinds of physical and chemical denaturants and these immobilized enzyme preparations maintained very high activity on their repeated and continuous uses. Amylolytic enzymes immobilized on nano-supports have successfully been applied in food, fuel, textile, paper and pulp, detergent, environmental, medical, and analytical fields.","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"29 1","pages":"37 - 53"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85968901","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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