Journal of Fermentation and Bioengineering最新文献

{"title":"Contents to volume 85","authors":"","doi":"10.1016/S0922-338X(98)90003-4","DOIUrl":"https://doi.org/10.1016/S0922-338X(98)90003-4","url":null,"abstract":"","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 6","pages":"Pages i-viii"},"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)90003-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137378213","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":"Accumulation of yttrium by Variovorax paradoxus","authors":"Manjiroh Kamijo ,&nbsp;Tohru Suzuki ,&nbsp;Keiichi Kawai ,&nbsp;Hironobu Murase","doi":"10.1016/S0922-338X(99)80007-5","DOIUrl":"https://doi.org/10.1016/S0922-338X(99)80007-5","url":null,"abstract":"<div><p>We screened oligotrophic microorganisms for those which were capable of reducing the concentration of yttrium (Y), a representative of the rate-earth elements, in culture medium. From 465 strains of oligotrophic microorganisms (grown on <span><math><mtext>1</mtext><mtext>100</mtext></math></span> diluted nutrient agar) isolated from soil and river water samples, 7 strains capable of reducing the concentration of Y in the diluted nutrient broth containing 5 ppm Y were selected. Three strains capable of reducing the concentration of Y to a great extent were identified as <em>Variovorax paradoxus</em> (strain Y-1) and <em>Comamonas acidovorans</em> (strains Y-2 and Y-3). Energy dispersive X-ray analyses revealed that <em>V. paradoxus</em> Y-1 incorporated Y into both the cell and excreted materials. The three strains tended to reduce the concentrations of mostly light rare-earth elements such as La, Ce, Pr and Nd, and intermediate elements such as Tb, Dy, Ho and Er to some extent, but did not reduce the concentrations of heavy elements such as Tm, Yb and Lu. Although <em>V. paradoxus</em> Y-1 could not reduce the concentration of trivalent metal ions such as Fe³⁺ and Cr³⁺ (5 ppm) which were added individually to the <span><math><mtext>1</mtext><mtext>100</mtext></math></span> diluted nutrient broth, when both Y and Fe³⁺ or Cr³⁺ were added to the broth, the concentration of Fe³⁺ or Cr³⁺ was reduced concomitantly with that of Y. In the case of divalent metal ions such as Mn²⁺, Cu²⁺ and Fe²⁺, such a phenomenon was not observed. Y induced the production of the extracellular materials by <em>V. paradoxus</em> Y-1, suggesting that Y might affect the physiological activity of this strain.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 6","pages":"Pages 564-568"},"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)80007-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91647854","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":"Characterization of a multidomain cellulase from an extremely thermophilic anaerobe strain NA10","authors":"Katsuhide Miyake,&nbsp;Yuichi Machida,&nbsp;Kouji Hattori,&nbsp;Shinji Iijima","doi":"10.1016/S0922-338X(97)85677-2","DOIUrl":"10.1016/S0922-338X(97)85677-2","url":null,"abstract":"<div><p>The nucleotide sequence of a β-glucanase gene from an extremely thermophilic anaerobe NA10 was determined. The open reading frame extended over 3000 bp and encoded a polypeptide with a molecular mass of 113 kDa. The deduced amino acid sequence of this protein exhibited high homology to a bifunctional cellulase CelB of <em>Caldocellum saccharolyticum</em>. Based on the homology to CelB, the NA10 β-glucanase appears to comprise three domains: N-terminal, central, and C-terminal domains. Among these, N- and C-terminal domains apper to be catalytic domains, and the central domain to be a cellulose binding domain. These domains were joined with each other by proline and threonine rich segments (PT box). The GST-fused C-terminal domain showed CMCase and MUCase activities, but the activities of the GST-fused N-terminal domain were very weak. Zymogram analysis revealed that recombinant <em>Escherichia coli</em> containing the β-glucanase gene produced a protein with a molecular mass of approximately 113 kDa, which was in good agreement with that deduced from the DNA sequence. However, Western blot analysis indicated that the amount of this full length protein was very small. Several smaller abundant proteins which exhibited CMCase activity were also detected. Northern blot analysis indicated that there appear to be putative internal transcriptional initiation sites. Generation of small molecular mass species appear to be due to alternative transcription and translation from the initiation sites within the gene, or partial proteolysis.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 3","pages":"Pages 289-296"},"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)85677-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89635948","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 nucleotide sequence of the nitric oxide reductase locus in Paracoccus denitrificans IFO 12442","authors":"Kiyohito Murai,&nbsp;Katsuhide Miyake,&nbsp;Jun Andoh,&nbsp;Shinji Iijima","doi":"10.1016/S0922-338X(98)80158-X","DOIUrl":"10.1016/S0922-338X(98)80158-X","url":null,"abstract":"<div><p>A 5.2-kb DNA fragment containing the upstream region of the nitrite reductase gene (<em>nirS</em>) was cloned from <em>Paracoccus denitrificans</em> IFO 12442 and its DNA sequence was determined. In this fragment, four open reading frames (ORFs) were observed. Among these, two ORFs, located 3 kb upstream of the <em>nirS</em> gene were found to encode nitric oxide reductase (<em>norC, norB</em>) by homology analysis. The <em>norC</em> and <em>norB</em> encoded cytochrome <em>c</em> and <em>b</em> subunits of the enzyme, and the predicted molecular weights of the protein products were 17 kDa (150 amino acid residues) and 52.5 kDa (462 amino acid residues), respectively. The other two open reading frames, designated ORF1 (73 kDa, 681 amino acid residues) and ORF2 (32.5 kDa, 304 amino acid residues), were found between the <em>nir</em> and <em>nor</em> genes. The deduced amino acid sequence of ORF1 showed high similarity (35% identity) to that of NosR which is known to be a transcriptional regulatory protein for the N₂O reductase gene cluster of <em>Pseudomonas stutzeri</em>. Since the ORF1 protein has a well conserved cysteine cluster and 5 hydrophobic transmembrane repeats similar to those of the NosR protein, ORF1 probably functions as a membrane bound sensor for denitrification. Northern blot analysis indicated that the ORF1–2 and <em>norCB</em> regions are probably transcribed as independent operons.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 5","pages":"Pages 494-499"},"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)80158-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81770126","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":"Methane fermentation of pot ale from a whisky distillery after enzymatic or microbial treatment","authors":"Masatsugu Tokuda ,&nbsp;Naotake Ohta ,&nbsp;Shigeru Morimura ,&nbsp;Kenji Kida","doi":"10.1016/S0922-338X(98)80068-8","DOIUrl":"10.1016/S0922-338X(98)80068-8","url":null,"abstract":"<div><p>The pot ales of malt whisky (MW) and grain spirit (GS) were subjected to batchwise methane fermentation. The pot ale of GS could be more easily treated than the pot ale of MW. The substantial difference in performance seemed to be due to the amount of dextrin. Therefore, the pot ale of MW was first hydrolyzed enzymatically and treated using the same method. As a result, the treatment time necessary for methane fermentation was shortened from 15 d to 11–12 d. Koji mould was cultivated aerobically in the pot ale of MW as a substitute for enzymatic hydrolysis. The dextrin content of the MW pot ale subjected to enzymatic hydrolysis was only 40% of that achieved by cultivation of koji mould. The supernatant of the culture broth was then treated continuously by methane fermentation using a novel upflow anaerobic filter process (UAFP) reactor. A maximum loading rate of 10.8 g/<em>l</em>/d was achieved, corresponding to a treatment time of only 18 h. The residual dextrin in the supernatant of the culture broth was completely decomposed by methane fermentation, as deduced from the elution curve after gel-permeation chromatography.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 5","pages":"Pages 495-501"},"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)80068-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76034800","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":"Intructions to authors","authors":"","doi":"10.1016/S0922-338X(98)80051-2","DOIUrl":"https://doi.org/10.1016/S0922-338X(98)80051-2","url":null,"abstract":"","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 1","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)80051-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92137887","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 of xylanase gene xynG1 from Aspergillus oryzae KBN 616, a shoyu koji mold, and analysis of its expression","authors":"Tetsuya Kimura ,&nbsp;Noriyuki Kitamoto ,&nbsp;Yukio Kito ,&nbsp;Shuichi Karita ,&nbsp;Kazuo Sakka ,&nbsp;Kunio Ohmiya","doi":"10.1016/S0922-338X(97)80346-7","DOIUrl":"https://doi.org/10.1016/S0922-338X(97)80346-7","url":null,"abstract":"<div><p>A xylanase gene <em>xynG1</em> was isolated and sequenced from <em>Aspergillus oryzae</em> KBN616 used for making shoyu koji. The structural part of the <em>xynG1</em> gene was found to be 725 bp and was predicted to be interrupted by a single intron which was 62 bp in size. The mature XynG1 was predicted to be 189 amino acids in size and had high amino acid homology to other fungal xylanases classified in family 11 glycosidase. The XynG1 was detected in the culture supernatant of <em>A. oryzae</em> KBN616 grown in xylan medium but was not detected when <em>A. oryzae</em> KBN616 was grown in glucose medium. The <em>xynG1</em> gene was introduced into <em>A. nidulans</em> and was found to be expressed even in the glucose media. This expression pattern was confirmed using a luciferase gene as a reporter in <em>A. nidulans</em>.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 1","pages":"Pages 10-16"},"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)80346-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91704881","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":"Controlled expression of lysis genes encoded in T4 phage for the gentle disruption of Escherichia coli cells","authors":"Yasunori Tanji,&nbsp;Kazuhiro Asami,&nbsp;Xin-Hui Xing,&nbsp;Hajime Unno","doi":"10.1016/S0922-338X(97)80357-1","DOIUrl":"https://doi.org/10.1016/S0922-338X(97)80357-1","url":null,"abstract":"<div><p>Two lysis genes, gene-t and gene-e, encoded in bacteriophage T4 were cloned in vectors pUC118 and pET26b(+), respectively. Immediately after the induction of gene-t expression, growth of <em>Escherichia coli</em> JM 109 cells was halted. Since the expression of gene-t was toxic to the cells, the expressed gene-t product (gp-t) could not be detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). On the other hand, expression of gene-e cloned in vector plasmid pUC118 did not give rise to any detectable change in <em>E. coli</em> JM 109 cells; normal cell growth was observed, and the gene-e product (gp-e) was identified by SDS-PAGE. Lysis genes cloned in vector pET26b(+) were expressed in BL21 (DE3) host cells carrying plasmid pLysS, which encodes T7 lysozyme. It is thought that the expressed protein is translocated into the periplasmic space driven by the signal peptide of the peIB outermembrane protein of <em>E. coli</em> fused in the frame at the N-terminal end of the lysis protein. Immediate cell disruption was observed when the gene-t cloned in pET26b(+) was expressed in the logarithmic growth phase. β-Galactosidase activity was observed in the centrifuged supernatant of the cell culture producing gp-t. Almost 100% of the activity of the β-galactosidase produced in the BL21(DE3)pLysS cells was identified in the supernatant 30 min after the start of the induction period of gene-t, indicating that complete cell disruption had occurred at that time. The production of gp-e with the N-terminal fusion of the signal peptide of pelB did not cause immediate cell lysis, but it did result in a morphological change in the BL21(DE3)pLysS cells, from rod-shaped to elliptical. Resuspension of the gp-e-producing BL21(DE3)pLysS cell nellet with pure water caused cell lysis followed by the release of β-galactosidase into the medium. Almost 100% of the β-galactosidase activity was identified in the resuspended supernatant.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 1","pages":"Pages 74-78"},"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)80357-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91704879","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":"Trehalose metabolism and leavening ability of bakers' yeast grown in the presence of sodium chloride","authors":"Nazneen Bagum,&nbsp;Kumio Yokoigawa,&nbsp;Yuka Isobe,&nbsp;Hiroyasu Kawai","doi":"10.1016/S0922-338X(98)80151-7","DOIUrl":"10.1016/S0922-338X(98)80151-7","url":null,"abstract":"<div><p>We examined the relationship between trehalose metabolism and the leavening ability of bakers' yeast grown in the presence of NaCl. The yeast cells were cultured at 30°C in media (5% glucose, 1% peptone, 0.5% yeast extract, 0.1% KH₂PO₄, and 0.1% MgSO₄) containing 0–3% NaCl. The cells were grown to the stationary phase for 24 h irrespective of the NaCl concentration in the medium, but the cell yield was decreased by addition of NaCl. The presence of 1% NaCl in the medium transiently enhanced the accumulation of intracellular trehalose after 24 h, however, the accumulated trehalose was hydrolyzed during further growth, and 2 or 3% NaCl decreased the intracellular trehalose content. The neutral trehalase activity in yeast cells grown for 24 h increased with increasing NaCl concentration, while the acid trehalase activity decreased. Trehalose-6-phosphate synthase (TPS) activity in cells grown for 24 h increased significantly in the presence of 1 and 2% NaCl, but decreased in the presence of 3% NaCl. When we determined the leavening ability of bakers' yeast cells grown for 24 h in the presence of 0–3% NaCl using dough without addition of NaCl, the leavening ability increased with increasing NaCl concentration in the culture medium. The cells having the highest leavening ability were those that had the lowest amounts of trehalose and the lowest TPS activity among the conditions tested. The leavening ability of bakers' yeast grown in the presence of NaCl appears not to correlate with intracellular trehalose content.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 5","pages":"Pages 457-460"},"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)80151-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82605073","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":"Magnetic field effects on photosynthesis and growth of the cyanobacterium Spirulina platensis","authors":"Morio Hirano,&nbsp;Akira Ohta,&nbsp;Katsuya Abe","doi":"10.1016/S0922-338X(98)80136-0","DOIUrl":"10.1016/S0922-338X(98)80136-0","url":null,"abstract":"<div><p>We investigated the influence of a magnetic field on photosynthesis in, and the growth of <em>Spirulina platensis</em> (<em>S. platensis</em>), under magnetic fields with magnetic flux densities varying from 0.5 gauss (geomagnetic field) to 700 gauss. The specific growth rate of <em>S. platensis</em> was the highest at 100 gauss, being 1.5-fold that at 0.5 gauss, while the growth was obviously inhibited at 700 gauss. The existence of a magnetic field had no effect on the growth when <em>S. platensis</em> was cultured in the dark on a medium containing 0.3% glucose. The oxygen evolution rate during photosynthesis increased with increase in magnetic flux density, and the intracellular concentrations of sugar and phycocyanin, a light-harvesting pigment present in the thylakoid membrane in which reactions of the photosynthetic electron transfer system occur, reached maximal values at 100 gauss. At magnetic flux densities of a over 100 gauss, the phycocyanin content decreased with increase in magnetic flux density. The content of glyceroglycolipid, which exists exclusively in the thylakoid membrane, decreased with increase in magnetic flux density, especially so at 700 gauss, when it became 44% that at 0.5 gauss. From the aforementioned results, it is evident that magnetic fields accelerate the growth of <em>S. platensis</em> associated with activation of light excitation in the photosynthetic electron transfer system and increase in phycocyanin contents, and that these effects are maximal at magnetic flux densities of around 100 gauss. Nevertheless, when a magnetic flux density of over 400 gauss was applied, growth inhibition was observed with decrease in the phycocyanin content, and production of chemical energy necessary for sugar synthesis.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 3","pages":"Pages 313-316"},"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)80136-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77532250","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}