Biocatalysis最新文献_第2页

Enzymes in Food and Feed Industries: Where Tradition Meets Innovation 食品和饲料工业中的酶:传统与创新的结合

Biocatalysis Pub Date : 2019-01-01 DOI: 10.1007/978-3-030-25023-2_12

P. Fernandes

引用次数: 6

Immobilization of α-amylases and Their Analytical Applications α-淀粉酶的固定化及其分析应用

Biocatalysis Pub Date : 2019-01-01 DOI: 10.1007/978-3-030-25023-2_6

O. Prakash, Saumya Khare

引用次数: 5

Cross-linked Enzyme Aggregates: Current Developments and Applications 交联酶聚集体:目前的发展和应用

Biocatalysis Pub Date : 2019-01-01 DOI: 10.1007/978-3-030-25023-2_5

Rubia Noori, M. Perwez, M. Sardar

引用次数: 6

Screening, Optimization and Assembly of Key Pathway Enzymes in Metabolic Engineering 代谢工程中关键途径酶的筛选、优化与组装

Biocatalysis Pub Date : 2019-01-01 DOI: 10.1007/978-3-030-25023-2_8

Yanfeng Liu, Long Liu

引用次数: 1

Biocatalysis: Enzymatic Basics and Applications 生物催化:酶的基础和应用

Biocatalysis Pub Date : 2019-01-01 DOI: 10.1007/978-3-030-25023-2

Qayyum Husain, Mohammad Fahad Ullah

引用次数: 4

Significance of Enzymes and Their Application in Agriculture 酶的意义及其在农业中的应用

Biocatalysis Pub Date : 2019-01-01 DOI: 10.1007/978-3-030-25023-2_14

A. Piotrowska-Długosz

引用次数: 7

Optimization of enzymatic synthesis of ethyl hexanoate in a solvent free system using response surface methodology (RSM) 响应面法优化无溶剂体系中酶促合成己酸乙酯的工艺

Biocatalysis Pub Date : 2018-05-17 DOI: 10.1515/boca-2018-0002

Sarita D. Gawas, N. Lokanath, V. Rathod

{"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}

引用次数: 15

Novel DyP from the basidiomycete Pleurotus sapidus: substrate screening and kinetics 从担子菌Pleurotus sapidus提取的新型DyP:底物筛选和动力学

Biocatalysis Pub Date : 2018-01-01 DOI: 10.1515/boca-2018-0001

A. Avram, A. Sengupta, P. Pfromm, H. Zorn, P. Lorenz, T. Schwarz, K. Q. Nguyen, P. Czermak

{"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}

引用次数: 8

Communication. Vanillyl alcohol oxidases produced in Komagataella phaffii contain a highly stable noncovalently bound anionic FAD semiquinone 沟通。香草醇氧化酶含有高度稳定的非共价结合阴离子FAD半醌

Biocatalysis Pub Date : 2017-01-01 DOI: 10.1515/boca-2017-0002

G. Gygli, W. Berkel

{"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}

引用次数: 10

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review 纳米材料作为淀粉酶固定化的新型载体及其应用综述

Biocatalysis Pub Date : 2017-01-01 DOI: 10.1515/boca-2017-0004

Q. Husain

引用次数: 51