Journal of Fermentation and Bioengineering最新文献_第2页

Conditions for nitrification and denitrification by an immobilized heterotrophic nitrifying bacterium Alcaligenes faecalis OKK17 固定化异养硝化细菌粪Alcaligenes faecalis OKK17的硝化和反硝化条件

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)89003-5

T. Nishio, T. Yoshikura, H. Mishima, Z. Inouye, H. Itoh

引用次数: 36

Rational Design for Stabilization and Optimum pH Shift of Serine Protease AprN 丝氨酸蛋白酶AprN稳定性及最佳pH位移的合理设计

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80349-2

A. Masui, Nobuaki Fujiwara, Kazuhiko Yamamoto, M. Takagi, T. Imanaka

引用次数: 13

Molecular cloning of xylanase gene xynG1 from Aspergillus oryzae KBN 616, a Shoyu Koji Mold, and analysis of its expression 米曲霉KBN 616木聚糖酶基因xynG1的克隆及表达分析

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80346-7

Tetsuya Kimura, N. Kitamoto, Y. Kito, S. Karita, K. Sakka, K. Ohmiya

引用次数: 26

Inhibitory effects of acetic acid on respiration and growth of Zygosaccharomyces rouxii 醋酸对柔糖酵母菌呼吸和生长的抑制作用

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(97)86770-0

Kazuhiro Kusumegi , Hidetsugu Yoshida , Sachiko Tomiyama

引用次数: 16

Purification and characterization of a novel β-glucosidase from Clavibacter michiganense that hydrolyzes glucosyl ester linkage in steviol glycosides 水解甜菊糖苷中葡萄糖酯链的新型β-葡萄糖苷酶的纯化与表征

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(97)86761-X

Hirofumi Nakano , Katsuyuki Okamoto , Tsuneya Yatake , Taro Kiso , Sumio Kitahata

{"title":"Purification and characterization of a novel β-glucosidase from Clavibacter michiganense that hydrolyzes glucosyl ester linkage in steviol glycosides","authors":"Hirofumi Nakano , Katsuyuki Okamoto , Tsuneya Yatake , Taro Kiso , Sumio Kitahata","doi":"10.1016/S0922-338X(97)86761-X","DOIUrl":"10.1016/S0922-338X(97)86761-X","url":null,"abstract":"<div>Clavibacter michiganense was identified as a microorganism that hydrolyzed the glucosyl ester linkages at site 19 of steviol glycosides. An enzyme that catalyzes the hydrolysis was purified from the cell-free extract using streptomycin treatment, ammonium sulfate fractionation, Q Sepharose anion exchange chromatography, Sephacryl S-100 gel filtration, and Ether Toyopearl hydrophobic chromatography. The purified enzyme migrated as a single protein band in polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate, and isoelectric focusing. The molecular mass was estimated to be approximately 65 kDa, both by gel filtration and sodium dodecyl sulfate/polyacrylamide gel electrophoresis. An isoelectric point, pI, of 4.6, was obtained using isoelectric focusing. The enzyme was most active at around pH 7.5 and at 45°C, and was stable between pH 6–10 and below 40°C. Both Hg2+ and p-chloromercuric benzoate inhibited activity. The enzyme hydrolyzed glucosyl ester linkages at site 19 of rebaudioside A, stevioside, rubusoside, and steviol monoglucosyl ester, although it did not cleave 13-O-linked glucosyl residue of rubusoside and steviol monoside. A transglucosylation product having a cellobiosyl residue at site 19 was formed when rubusoside was used as a glucosyl donor and acceptor. The enzyme hydrolyzed glucosidic linkages in p-nitrophenyl β-glucoside faster than glucosyl ester linkages in the steviol glycosides. It also acted on phenyl β-glucoside and salicin, and faintly on sophorobiose and cellobiose. These results indicate that the enzyme is a novel β-glucosidase that hydrolyzes ester linkages.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 2","pages":"Pages 162-168"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(97)86761-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75809998","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: 33

Performance of photosynthetic electrochemical cells using immobilized Anabaena variabilis M-3 in discharge/culture cycles 固定化变水藻M-3在放电/培养循环中的光合电化学电池性能

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(98)80106-2

Tatsuo Yagishita, Shigeki Sawayama, Ken-Ichiro Tsukahara, Tomoko Ogi

引用次数: 40

SSU1-R, a sulfite resistance gene of wine yeast, is an allele of SSU1 with a different upstream sequence 葡萄酒酵母抗亚硫酸盐基因SSU1- r是SSU1上游序列不同的等位基因

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(98)80146-3

Nami Goto-Yamamoto, Kazuyoshi Kitano , Kunio Shiki , Yuichi Yoshida , Takashi Suzuki , Tomoko Iwata , Yoshiharu Yamane , Shodo Hara

{"title":"SSU1-R, a sulfite resistance gene of wine yeast, is an allele of SSU1 with a different upstream sequence","authors":"Nami Goto-Yamamoto, Kazuyoshi Kitano , Kunio Shiki , Yuichi Yoshida , Takashi Suzuki , Tomoko Iwata , Yoshiharu Yamane , Shodo Hara","doi":"10.1016/S0922-338X(98)80146-3","DOIUrl":"10.1016/S0922-338X(98)80146-3","url":null,"abstract":"<div>A sulfite resistance gene, SSU1-R, was cloned from a highly sulfite-resistant strain of Saccharomyces cerevisiae, Y-9, which was isolated as a contaminant from a wine must. The coding region sequence of SSU1-R was almost identical to that of SSU1, the gene that has been shown to be responsible for sulfite resistance. Although SSU1 is located on chromosome XVI of S. cerevisiae, the upstream region of SSU1-R was homologous with a sequence of chromosome VIII. In our Northern analysis, an intense band was detected in Y-9 and K1-V1116 strains, both of which exhibit strong sulfite resistance, with and without sulfite in the medium. On the other hand, under the same experimental conditions, no band was detected in OC-2, a strain that exhibits weak sulfite resistance. Physical mapping of SSU1/SSU1-R showed that this sequence was on chromosome VIII of Y-9 and the two wine strains, K1-V1116 and WE14. OC-2 and twenty-three other wine, sake, beer, shochu (Japanese distilled liquor), alcohol, bakery, and laboratory strains, had this sequence on chromosome XVI, and four other wine strains had it on both chromosomes. Thus, the difference in the upstream sequence of SSU1/SSU1-R seems to cause differences in the transcription rates and degree of sulfite resistance.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 5","pages":"Pages 427-433"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(98)80146-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81495002","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: 72

Importance of five amino acid residues at C-terminal region for the folding and stability of β-glucosidase of Cellvibrio gilvus gilvus Cellvibrio c端5个氨基酸残基对β-葡萄糖苷酶折叠和稳定性的重要性

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(98)80089-5

Jong Deog Kim , Satya Singh , Sachiko Machida , Young Yu , Chika Aoyagi , Yasushi Kawata , Kiyoshi Hayashi

引用次数: 11

Response of an anaerobic granular sludge to chlorinated aliphatic hydrocarbons in different conditions 厌氧颗粒污泥在不同条件下对氯化脂肪烃的反应

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(98)80118-9

Nuria Rodríguez, JoséL. Sanz

{"title":"Response of an anaerobic granular sludge to chlorinated aliphatic hydrocarbons in different conditions","authors":"Nuria Rodríguez, JoséL. Sanz","doi":"10.1016/S0922-338X(98)80118-9","DOIUrl":"10.1016/S0922-338X(98)80118-9","url":null,"abstract":"<div>In spite of its importance, little attention has been paid thus far to the toxicity of chlorinated aliphatic hydrocarbons under methanogenic conditions. The effect of several parameters which can affect the toxicity of CHCl3, CCl4, C2H2Cl4 and trans-C2H2Cl2 on the acetoclastic methanogenic activity of anaerobic sludge was studied. The following conclusions were derived: (i) The extend of inhibition produced is a function of the toxicant concentration, the type and the amount of the biomass. A lag-period was detected for the inhibition produced by CHCl3 and trans-C2H2Cl2, while for the other compounds the inhibitory effect was instant. (ii) The recovery time for an anaerobic granular sludge exposed to different toxicants was a function of the extent of inhibition and the exposure time, and seemed to be independent of the toxicants used. (iii) The possible acclimatization of an anaerobic sludge to continuous exposure to a toxicant was dependent on the nature of the toxicant. The time required to acquire an activity similar to that of untreated controls was dependent on the concentration of the toxicant used. In our case adaptation was only obtained for CCl4.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 2","pages":"Pages 226-232"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(98)80118-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77963420","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

A novel arylesterase active toward 7-aminocephalosporanic acid from Agrobacterium radiobacter IFO 12607: Nucleotide sequence, gene expression in Escherichia coli, and site-directed mutagenesis 放射农杆菌IFO 12607对7-氨基头孢酸具有活性的新型芳基酯酶:核苷酸序列、基因在大肠杆菌中的表达和位点定向诱变

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(97)86757-8

Yasuyoshi Sakai , Kaoru Ayukawa , Ryoji Mitsui , Hiroya Yurimoto , Keizo Yamamoto , Nobuo Kato

{"title":"A novel arylesterase active toward 7-aminocephalosporanic acid from Agrobacterium radiobacter IFO 12607: Nucleotide sequence, gene expression in Escherichia coli, and site-directed mutagenesis","authors":"Yasuyoshi Sakai , Kaoru Ayukawa , Ryoji Mitsui , Hiroya Yurimoto , Keizo Yamamoto , Nobuo Kato","doi":"10.1016/S0922-338X(97)86757-8","DOIUrl":"10.1016/S0922-338X(97)86757-8","url":null,"abstract":"<div>A novel arylesterase from Agrobacterium radiobacter IFO 12607 catalyzes the deacetylation of 7-aminocephalosporanic acid (7-ACA) to form deacetyl 7-ACA, but is inactive with cephalosporin C. A DNA fragment carrying the gene encoding the 7-ACA-deacetylating enzyme was cloned from the chromosomal DNA of this bacterium. The open reading frame encoding the enzyme was 642 bp long, corresponding to a protein of 214 amino acid residues (molecular mass=23,085). The deduced amino acid sequence did not contain the sequence GXSXG, typical of the many serine esterases including Bacillus cephalosporin C deacetylase, but has the pentapeptide motif sequence GDSLT (amino acid position 9–13) which is also a consensus sequence of some serine esterases. The newly cloned gene was expressed in Escherichia coli under the control of the lac promoter, and the gene product purified from E. coli exhibited the same catalytic properties as the enzyme purified from A. radiobacter. Site-directed mutagenesis of S11A or S11C within the pentapeptide motif sequence led to complete loss of the enzyme activity. Thus, the Ser-11 residue within the GDSLT motif sequence was determined to construct the catalytic center. These results together with those of our previous studies indicated that the 7-ACA-deacetylating enzyme from A. radiobacter IFO 12607 is a new member of the family of lipolytic serine esterases containing the GDSLT sequence as their catalytic center.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 2","pages":"Pages 138-143"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(97)86757-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83540261","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: 2