Journal of Molecular Catalysis B-enzymatic最新文献_第10页

Lipase mediated resolution of cis- and trans-linalool oxide (pyranoid) 脂肪酶介导的顺式和反式芳樟醇氧化物(pyranoid)的分解

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2017-03-09 DOI: 10.1016/j.molcatb.2017.03.004

Stefano Serra , Davide De Simeis , Elisabetta Brenna

引用次数: 8

Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications 单脂醇氧化还原酶atbe样蛋白15l182v生物催化应用的表征

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-11-09 DOI: 10.1016/j.molcatb.2016.10.018

Sabine Pils , Kordula Schnabl , Silvia Wallner , Marko Kljajic , Nina Kupresanin , Rolf Breinbauer , Michael Fuchs , Raquel Rocha , Joerg H. Schrittwieser , Wolfgang Kroutil , Bastian Daniel , Peter Macheroux

{"title":"Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications","authors":"Sabine Pils , Kordula Schnabl , Silvia Wallner , Marko Kljajic , Nina Kupresanin , Rolf Breinbauer , Michael Fuchs , Raquel Rocha , Joerg H. Schrittwieser , Wolfgang Kroutil , Bastian Daniel , Peter Macheroux","doi":"10.1016/j.molcatb.2016.10.018","DOIUrl":"10.1016/j.molcatb.2016.10.018","url":null,"abstract":"<div>Monolignol oxidoreductases from the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) catalyze the oxidation of monolignols to the corresponding aldehydes. In this report, we explore the potential of a monolignol oxidoreductase from Arabidopsis thaliana (AtBBE-like protein 15) as biocatalyst for oxidative reactions. For this study we employed a variant with enhanced reactivity towards oxygen, which was obtained by a single amino acid exchange (L182V). The pH and temperature optima of the purified AtBBE-like protein 15 L182V were determined as well as the tolerance toward organic co-solvents; furthermore the substrate scope was characterized. The enzyme has a temperature optimum of 50°C and retains more than 50% activity between pH 5 and pH 10 within 5min. The enzyme shows increased activity in the presence of various co-solvents (10–50% v/v), including acetonitrile, 2-propanol, 1,4-dioxane, and dimethyl sulfoxide. Primary benzylic and primary or secondary allylic alcohols were accepted as substrates. The enantioselectivity E in the oxidation of secondary alcohols was good to excellent (E>34 to >200).</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S6-S14"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.10.018","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89309986","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Characterization of a new lysine decarboxylase from Aliivibrio salmonicida for cadaverine production at alkaline pH 在碱性条件下产尸胺的一种新型赖氨酸脱羧酶的研究

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-11-30 DOI: 10.1016/j.molcatb.2016.11.023

Fengyu Kou , Jing Zhao , Jiao Liu , Jie Shen , Qin Ye , Ping Zheng , Zhimin Li , Jibin Sun , Yanhe Ma

{"title":"Characterization of a new lysine decarboxylase from Aliivibrio salmonicida for cadaverine production at alkaline pH","authors":"Fengyu Kou , Jing Zhao , Jiao Liu , Jie Shen , Qin Ye , Ping Zheng , Zhimin Li , Jibin Sun , Yanhe Ma","doi":"10.1016/j.molcatb.2016.11.023","DOIUrl":"10.1016/j.molcatb.2016.11.023","url":null,"abstract":"<div>Lysine decarboxylases (LDCs) catalyze the conversion of l-lysine to cadaverine, a highly attractive building block for bio-based polyamides. Due to economic and environmental concerns, LDCs active at elevated pH are highly desirable. In this study, a new LDC from Aliivibrio salmonicida (AsLdc) was discovered, expressed, and characterized. Compared to the LDCs from Escherichia coli, LdcC and CadA, the latter was frequently used for cadaverine production, the purified AsLdc showed much higher activities at alkaline pH 7.0–8.5, for instance, 205.1U/mg at pH 7.5 with 10μg/mL enzyme, in comparison to 68.3 and 51.5U/mg for CadA and LdcC, respectively. The activities of AsLdc and CadA correlated well with the proportions of decamers at the pH range of 5.0–8.5. AsLdc with a melting temperature of 79°C was more thermostable than CadA (73.6°C). When used for whole-cell biotransformation of l-lysine to cadaverine at pH 7.5, AsLdc completed the transformation within 7h while the CadA did only 82.8%. These results indicate the high potential of the new AsLdc for the industrial production of cadaverine.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S88-S94"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.11.023","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73458310","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

Bench scale production of nicotinic acid using a newly isolated Stenotrophomonas maltophilia AC21 producing highly-inducible and versatile nitrilase 利用新分离的嗜麦芽寡养单胞菌AC21生产高诱变和多功能硝化酶的实验规模生产烟酸

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-11-21 DOI: 10.1016/j.molcatb.2016.11.019

Arastoo Badoei-Dalfard, Zahra Karami, Narjes Ramezani-pour

{"title":"Bench scale production of nicotinic acid using a newly isolated Stenotrophomonas maltophilia AC21 producing highly-inducible and versatile nitrilase","authors":"Arastoo Badoei-Dalfard, Zahra Karami, Narjes Ramezani-pour","doi":"10.1016/j.molcatb.2016.11.019","DOIUrl":"10.1016/j.molcatb.2016.11.019","url":null,"abstract":"<div>A novel bacterial named AC21 having nitrile-converting activity was gained with acetonitrile as sole source of nitrogen, which was recognized by morphology and 16S rDNA gene sequence as Stenotrophomonas maltophilia. This intracellular nitrilase induced by acetonitrile (0.3%) catalyses the conversion of 3-cyanopyridine to nicotinic acid without noticeable production of nicotinamide. Optimal pH and temperature of Nitrilase AC21 was obtained at pH 8.0 and 45°C. Irreversible thermo-inactivation results showed that, enzyme half-life was 6h at 80°C. Several process factors, including quantity of enzyme and rate of substrate feeding, were considered with the goal of reaching whole substrate transformation. In a fed batch manner at 1l scale using hyper-induced AC21 resting cells equivalent to 10Uml−1 nitrilase activity, a total of 945mM of 3-cyanopyridine was formed at a rate of 3.32g h−1  <!-->dcw−1, which directed AC21 has ability of application in large scale nicotinic acid production.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S552-S559"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.11.019","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74777438","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: 12

Microbial hydroxylation of steroids by Penicillium decumbens 匍匐青霉菌对类固醇的微生物羟基化作用

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2017-02-16 DOI: 10.1016/j.molcatb.2017.02.007

Shuhong Mao , Lixia Zhang , Zhijiang Ge , Xuerong Wang , Yanqing Li , Xiaoguang Liu , Fei Liu , Fuping Lu

{"title":"Microbial hydroxylation of steroids by Penicillium decumbens","authors":"Shuhong Mao , Lixia Zhang , Zhijiang Ge , Xuerong Wang , Yanqing Li , Xiaoguang Liu , Fei Liu , Fuping Lu","doi":"10.1016/j.molcatb.2017.02.007","DOIUrl":"10.1016/j.molcatb.2017.02.007","url":null,"abstract":"<div>Biotransformation of steroid compounds: androst-4-ene-3, 17-dione (1), 19-nor-4-androstene-3, 17-dione (2), 13β-ethyl-4-gonene-3, 17-dione (3) using Penicillium decumbens as biocatalyst was investigated, and selective hydroxylation of 1–3 was observed. Biotransformation of 1 afforded 1α-hydroxy-androst-4-ene-3, 17-dione (4) and 1α, 6β-dihydroxy-androst-4-ene-3, 17-dione (5). Incubation of 19-nor-4-androstene-3, 17-dione (2) with P. decumbens culture resulted in the isolation of compounds 1α-hydroxy-19-nor-4-androstene-3, 17-dione (6) and 1α, 15β-dihydroxy-19-nor-4-androstene-3, 17-dione (7). Biotransformation of 3 gave one product 1α-hydroxy-13β-ethyl-4-gonene-3, 17-dione (8) at the same condition. The four metabolic products 5–8 were reported for the first time and the identified C1-α hydroxylation reaction of steroid by P. decumbens provides an another possibility to perform chemical modifications on C-1.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S346-S351"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.02.007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77253450","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: 9

Production of 5-O-α-glucosylgingerol via glucosylation of 6-gingerol by Ensifer sp. M-26 Ensifer sp. M-26通过6-姜辣素糖基化生产5-O-α-葡萄糖基姜辣素

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2017-01-06 DOI: 10.1016/j.molcatb.2017.01.005

Rika Matsumoto , Hiroshi Satoh , Makoto Ueda

{"title":"Production of 5-O-α-glucosylgingerol via glucosylation of 6-gingerol by Ensifer sp. M-26","authors":"Rika Matsumoto , Hiroshi Satoh , Makoto Ueda","doi":"10.1016/j.molcatb.2017.01.005","DOIUrl":"10.1016/j.molcatb.2017.01.005","url":null,"abstract":"<div>6-Gingerol ((S)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-3-decanone), the major gingerol present in ginger rhizomes, has been found to prevent fat accumulation and improve blood flow. However, its low solubility in water and strong pungent odor often limit its potential applications such as in functional foods. In order to overcome these disadvantages, we investigated microbial glucosylation of 6-gingerol by the soil bacterium Ensifer sp. M-26. 5-O-α-Glucosylgingerol was found to be produced from a mixture of maltose and 6-gingerol by the action of washed cells of Ensifer sp. M-26. The addition of organic solvents, such as hexane, to the reaction mixture enhanced 5-O-α-glucosylgingerol production. When the microbial reaction was carried out with 1.3g/L of 6-gingerol and 100g/L of maltose under optimized conditions, 0.40g/L of 5-O-α-glucosylgingerol was accumulated in 25h. The molar yield of 5-O-α-glucosylgingerol was 19.9mol%.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S200-S203"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.01.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89263248","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: 5

Conjugate addition of malononitrile on chalcone: Biocatalytic CC bond formation 丙二腈在查尔酮上的共轭加成:生物催化的CC键形成

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-08-10 DOI: 10.1016/j.molcatb.2016.08.004

Nitesh D. Punyapreddiwar, Sangesh P. Zodape, Atul V. Wankhade, Umesh R. Pratap

引用次数: 6

In-silico driven engineering of enantioselectivity of a penicillin G acylase towards active pharmaceutical ingredients 青霉素G酰化酶对活性药物成分的对映体选择性的硅驱动工程

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-11-15 DOI: 10.1016/j.molcatb.2016.11.014

Michal Grulich , Jan Brezovský , Václav Štěpánek , Andrea Palyzová , Helena Marešová , Jiří Zahradník , Eva Kyslíková , Pavel Kyslík

{"title":"In-silico driven engineering of enantioselectivity of a penicillin G acylase towards active pharmaceutical ingredients","authors":"Michal Grulich , Jan Brezovský , Václav Štěpánek , Andrea Palyzová , Helena Marešová , Jiří Zahradník , Eva Kyslíková , Pavel Kyslík","doi":"10.1016/j.molcatb.2016.11.014","DOIUrl":"10.1016/j.molcatb.2016.11.014","url":null,"abstract":"<div>Penicillin G acylase is one of the most employed enzymes in the pharmaceutical industry due to its role in the biotransformation of semi-synthetic β-lactam antibiotics. Recently, the enantioselectivity of the penicillin G acylase markedly broadened its application potential. In this study, we have evaluated effects of in-silico replacements of acyl-binding subsite residue Phe24β of the enzyme from Achromobacter sp. CCM 4824 to seven markedly smaller amino acids on its enantioselectivity towards industrially relevant compounds. Models of the two most promising mutants bearing substitutions Pheβ24Ala and Pheβ24Cys were investigated using molecular docking calculations. The Cys substitution revealed much better enantioselectivity traits with a set of seven substrates. To verify the relevance of in-silico predictions, we constructed a PGAA + Phe24βCys mutant towards this substrate was improved by 75% reaching E-value of about 70. Our results suggest the rapid identification of interesting replacements altering enantioselectivity using in-silico approach as the way for further expanding biotechnological application of penicillin G acylase.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S53-S59"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.11.014","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78649797","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

Biosynthesis of oleyl oleate in solvent-free system by Candida rugosa Lipase (CRL) immobilized in macroporous resin with cross-linking of aldehyde-dextran 醛-葡聚糖交联固定化假丝酵母脂肪酶(CRL)在无溶剂体系中合成油酸油酯

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-05-10 DOI: 10.1016/j.molcatb.2016.05.002

Yicheng Bi, Min Yu, Haiyan Zhou, Hua Zhou, Ping Wei

{"title":"Biosynthesis of oleyl oleate in solvent-free system by Candida rugosa Lipase (CRL) immobilized in macroporous resin with cross-linking of aldehyde-dextran","authors":"Yicheng Bi, Min Yu, Haiyan Zhou, Hua Zhou, Ping Wei","doi":"10.1016/j.molcatb.2016.05.002","DOIUrl":"10.1016/j.molcatb.2016.05.002","url":null,"abstract":"<div>In our study, oleyl oleate was synthesized through enzymatic esterification of oleic acid with oleyl alcohol using Candida rugosa lipase (CRL) immobilized on macroporous resin in a solvent-free system. CRL was immobilized flexibly on the support via aldehyde-dextran, and the effectiveness of aldehyde-dextrans, as cross-linking agents with different molecular weights, was compared and discussed. The impact of various factors, such as different molecular weights of dextran, molar ratio between oleic acid and oleyl alcohol, and the temperature and stability of enzymes, on esterification was investigated as well. Our study indicated that lipase immobilized by 20000  <!-->°C, and a 12-h reaction time to reach reaction equilibrium. Under the optimal reaction conditions, a high percentage yield of ester was achieved (92.6%). The immobilized CRL also reached a conversion rate of 86.7% with excellent stability even after 8 cycles.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages 1-5"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.05.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79340993","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: 25

Highly efficient resolution of N-hydroxymethyl vince lactam by solvent stable lipase YCJ01 溶剂稳定型脂肪酶YCJ01高效分解n -羟甲基vince内酰胺

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-11-01 Epub Date: 2016-12-14 DOI: 10.1016/j.molcatb.2016.12.009

Ling Zhu , Fucheng Zhu , Song Qin , Bin Wu , Bingfang He

{"title":"Highly efficient resolution of N-hydroxymethyl vince lactam by solvent stable lipase YCJ01","authors":"Ling Zhu , Fucheng Zhu , Song Qin , Bin Wu , Bingfang He","doi":"10.1016/j.molcatb.2016.12.009","DOIUrl":"10.1016/j.molcatb.2016.12.009","url":null,"abstract":"<div>Both optically pure enantiomers of N-hydroxymethyl vince lactam are the key synthons for some important antiviral drugs. The high enantioselective transesterification of N-hydroxymethyl vince lactam was catalyzed by the lipase from Burkholderia ambifaria YCJ01 using vinyl acetate as the acyl donor. Under the optimized conditions, an efficient resolution of N-hydroxymethyl vince lactam in high substrate concentration (300mM; 41.7g/L) was obtained with nearly theoretical conversion yield of 50.1%, eep of 99% and ees of 99%. Strikingly, the highest enantioselectivity (E>900) and dramatic increase of the lipase activity towards N-hydroxymethyl vince lactam were observed in a binary solvent system with hexane and MTBE (v/v=1:9). The high substrate tolerance and enantioselectivity of lipase YCJ01 showed significant benefit in the practical resolution of racemic N-hydroxymethyl vince lactam. Additionally, the high enantiopreference of lipase YCJ01 towards (−)-N-hydroxymethyl vince lactam was also rationalized through molecular docking.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S150-S156"},"PeriodicalIF":0.0,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.12.009","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76884252","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: 4