{"title":"Separation of lactic acid using polymeric membrane containing a mobile carrier","authors":"Michiaki Matsumoto, Toshiyuki Takagi, Kazuo Kondo","doi":"10.1016/S0922-338X(98)80066-4","DOIUrl":"10.1016/S0922-338X(98)80066-4","url":null,"abstract":"<div><p>A cellulose triacetate (CTA) membrane containing trioctylmethyl ammonium chloride (TOMAC) as a carrier and <em>o</em>-nitrophenyloctyl ether (NPOE) as a plasticizer was developed for the <em>in situ</em> separation of fermented lactic acid. The separation characteristics of the CTA-TOMAC-NPOE membrane were investigated. The permeation rate of lactate through the CTA-TOMAC-NPOE membrane was comparable to that through a supported liquid membrane. TOMAC played the role of a mobile carrier in lactate transport. It was found that the CTA-NPOE membrane containing TOMAC has the advantages of allowing a high flux of lactate and having a low solubility of TOMAC in aqueous solution.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 5","pages":"Pages 483-487"},"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)80066-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79228750","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}
{"title":"Cloning and sequence analysis of fumarase and superoxide dismutase genes from an extreme thermophile Thermus thermophilus HB27","authors":"Takehide Kosuge, Kaho Umehara, Takayuki Hoshino","doi":"10.1016/S0922-338X(98)80045-7","DOIUrl":"10.1016/S0922-338X(98)80045-7","url":null,"abstract":"<div><p>Class II fumarase (<em>fumC</em>) and Mn-containing superoxide dismutase (<em>sodA</em>) genes were cloned and sequenced from <em>Thermus thermophilus</em> HB27. The <em>fumC</em> and <em>sodA</em> genes existed in tandem. Comparison of the DNA and amino acid sequences of the <em>funC-sodA</em> regions between <em>T. thermophilus</em> HB27 and <em>Thermus aquaticus</em> YT1 revealed that coding regions showed high homology but noncoding regions were less homologous between the two strains. The deduced amino acid sequences of <em>T. thermophilus fumC</em> and <em>sodA</em> genes showed 58.2% and 53.2% identities to those of the corresponding <em>Escherichia coli</em> genes, respectively. The <em>T. thermophilus fumC</em> gene was expressed in <em>E. coli</em> and the heat-resistant fumarase activity was detected at 70°C.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 1","pages":"Pages 125-129"},"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)80045-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90293763","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}
{"title":"Key word index","authors":"","doi":"10.1016/S0922-338X(98)80127-X","DOIUrl":"https://doi.org/10.1016/S0922-338X(98)80127-X","url":null,"abstract":"","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 2","pages":"Page ii"},"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)80127-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136589226","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}
{"title":"Purification and characterization of an endo-1,4-β-d-galactanase from Aspergillus sojae","authors":"Isao Kimura , Naomi Yoshioka , Shigeyuki Tajima","doi":"10.1016/S0922-338X(97)80352-2","DOIUrl":"10.1016/S0922-338X(97)80352-2","url":null,"abstract":"<div><p>An endo-1,4-β-<span>d</span>-galactanase (EC 3.2.1.89) was purified to homogeneity from a solid-state culture of <em>Aspergillus sojae</em>. The molecular weight of the galactanase was estimated to be 39,700 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Gel filtration chromatography indicated the native enzyme to be a monomer. The isoelectric point of the galactanase was 3.60. The optimum pH and temperature of the enzyme activity were 4.5 and 50°C, respectively. The galactanase was stable from pH 6.0 to 10.0, and up to 35°C. The <em>K</em><sub>m</sub> value for arabinogalactan from soybean was 0.82 mg/ml. The activity of the enzyme was significantly inhibited by Mn<sup>2+</sup>, Hg<sup>2+</sup>, Ag<sup>+</sup>, and Fe<sup>3+</sup>, and no stimulation by metal ions was apparent. After the hydrolysis of arabinogalactan from soybean, the major products were galactobiose and galactose, and no liberation of arabinose was observed in the reaction mixture.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 1","pages":"Pages 48-52"},"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)80352-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91153238","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}
{"title":"Novel anthraquinones from stationary cultures of Fusarium oxysporum","authors":"Robert A. Baker, James H. Tatum","doi":"10.1016/S0922-338X(98)80077-9","DOIUrl":"10.1016/S0922-338X(98)80077-9","url":null,"abstract":"<div><p>Two new anthraquinones are described which were produced by stationary cultures of <em>Fusarium oxysporum</em> isolated from the roots of diseased citrus trees. They are 2-acetyl-3,8-dihydroxy- or 3-acetyl-2,8-dihydroxy-6-methoxy-anthraquinone and 2-(1-hydroxyethyl)-3,8-dihydroxy- or 3-(1-hydroxyethyl)-2,8-dihydroxy-6-methoxy-anthraquinone. These compounds differ from most other microbial anthraquinones in that they lack hydroxyl substituents at the 1,4 positions, and have an acetyl or 1-hydroxyethyl group at the 2 or 3 positions. This is the first report of anthraquinone metabolites produced by <em>F. oxysporum</em>.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 4","pages":"Pages 359-361"},"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)80077-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74748282","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}
{"title":"An ingenious device for better prediction of bio-processes using a multiple regression model: A case study on glucose isomerase production","authors":"Siriluk Teeradakorn , Michimasa Kishimoto , Pairoh Pinphanichakarn , Toshiomi Yoshida","doi":"10.1016/S0922-338X(98)80049-4","DOIUrl":"10.1016/S0922-338X(98)80049-4","url":null,"abstract":"<div><p>An ingenious device in the use of a multiple regression analysis model for better prediction of state variable changes in bio-processes is proposed. A correction factor was introduced in the regression equations for the estimation of specific rate parameters taking into account the data distribution resulting in the improvement of the prediction of glucose isomerase production by a <em>Streptomyces</em> fusant during a batch cultivation with periodical monitoring.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 1","pages":"Pages 141-143"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(98)80049-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86378570","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}
{"title":"Cyclic AMP regulation of the mob operon of the non-self-transmissible plasmid pEC3 isolated from a phytopathogenic bacterium","authors":"Nobuhiko Nomura , Mitsuo Yamashita , Yoshikatsu Murooka","doi":"10.1016/S0922-338X(99)80002-6","DOIUrl":"https://doi.org/10.1016/S0922-338X(99)80002-6","url":null,"abstract":"<div><p>A non-self-transmissible multiple-copy plasmid, pEC3, isolated from the phytopathogenic bacterium, <em>Erwinia carotovora</em> subsp. <em>carotovora</em>, can be mobilized with the help of a self-transmissible plasmid. When donors carrying a <em>cya</em> or a <em>crp</em> mutation were used, the mobilization efficiencies of pEC3 were markedly decreased. The covalently closed circular conformation of plasmid DNA containing both <em>oriT</em> and <em>mob</em> genes of pEC3 was found to be relaxed after the addition of cyclic AMP (cAMP). The relaxed DNA contained a specific single-strand DNA nick within the <em>oriT</em> region. RNA transcription of the <em>mob</em> operon was also increased by the addition of cAMP. These results indicate that the expression of the <em>mob</em> operon of pEC3 is positively regulated by cAMP and that the <em>mob</em> gene products are involved in nicking within the <em>oriT</em> region.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 6","pages":"Pages 534-538"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(99)80002-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90005981","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}
{"title":"Molecular cloning and expression of a polygalacturonase gene in Saccharomyces cerevisiae","authors":"Naoto Hirose , Masao Kishida , Haruhiko Kawasaki , Takuo Sakai","doi":"10.1016/S0922-338X(98)80139-6","DOIUrl":"10.1016/S0922-338X(98)80139-6","url":null,"abstract":"<div><p>An endo-polygalacturonase gene was cloned from a mutant of <em>Saccharomyces cerevisiae</em> that can produce a polygalacturonase, and the nucleotide sequence was identified. The polygalacturonase gene consists of 1086 bp. When the polygalacturonase gene was introduced into a strain of <em>S. cerevisiae</em> that cannot produce a polygalacturonase, the transformant secreted a polygalacturonase identical to that produced by the polygalacturonase-producing mutant.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 3","pages":"Pages 332-334"},"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)80139-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75794363","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}
Jun Sawai , Shinobu Shoji , Hideo Igarashi , Atsushi Hashimoto , Takao Kokugan , Masaru Shimizu , Hiromitsu Kojima
{"title":"Hydrogen peroxide as an antibacterial factor in zinc oxide powder slurry","authors":"Jun Sawai , Shinobu Shoji , Hideo Igarashi , Atsushi Hashimoto , Takao Kokugan , Masaru Shimizu , Hiromitsu Kojima","doi":"10.1016/S0922-338X(98)80165-7","DOIUrl":"10.1016/S0922-338X(98)80165-7","url":null,"abstract":"<div><p>Using four kinds of antibiotics, an investigation was made to determine whether or not H<sub>2</sub>O<sub>2</sub> generated from a ZnO powder slurry was related to its antibacterial activity. Changes in the sensitivity of <em>Escherichia coli</em> to the antibiotics suggested that H<sub>2</sub>O<sub>2</sub> was one of the primary factors concerned in the antibacterial activity of the ZnO powder slurry.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 5","pages":"Pages 521-522"},"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)80165-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82975964","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}
{"title":"Papain-catalyzed synthesis of aspartame precursor: A comparison with thermolysin","authors":"H. Nakaoka, Y. Miyajima, K. Morihara","doi":"10.1016/S0922-338X(97)80351-0","DOIUrl":"https://doi.org/10.1016/S0922-338X(97)80351-0","url":null,"abstract":"","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"1 1","pages":"43-47"},"PeriodicalIF":0.0,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77919582","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}