Journal of Fermentation and Bioengineering最新文献_第5页

Purification and characterization of exo-1,4-β-glucosidase from Acetobacter xylinum BPR2001 木醋杆菌BPR2001外链1,4-β-葡萄糖苷酶的纯化及特性研究

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80010-X

Naoki Tahara, Naoto Tonouchi, Hisato Yano, Fumihiro Yoshinaga

{"title":"Purification and characterization of exo-1,4-β-glucosidase from Acetobacter xylinum BPR2001","authors":"Naoki Tahara, Naoto Tonouchi, Hisato Yano, Fumihiro Yoshinaga","doi":"10.1016/S0922-338X(98)80010-X","DOIUrl":"10.1016/S0922-338X(98)80010-X","url":null,"abstract":"<div>An exo-1,4-β-glucosidase (EC 3.2.1.74; G3ase) was obtained from the supernatant of cultured Acetobacter xylinum subsp. sucrofermentans BPR2001 and purified to homogeneity by ammonium sulfate precipitation, cation-exchange, gel-filtration and hydrophobic interaction chromatography. The enzyme migrated to a position corresponding to 81.2 kDa on SDS-polyacrylamide gel electrophoresis under both non-reducing and reducing conditions, suggesting that this enzyme is a monomer polypeptide. The isoelectric point was 6.0. N-Bromosuccinimide inhibited the activity of exo-1,4-β-glucosidase completely, whereas sulfhydryl reagents did not. The Km and Vmax for the hydrolysis of cellotriose as substrate were 3.7 mM and 7.4 μmol/min/mg, respectively. The enzyme specifically cleaved the non-reducing ends of β-glucosyl linkages of cellotriose or larger cello-oligosaccharides, 4-methylumberiferryl- and p-nitrophenyl-β-d-glucosides, but cellobiose was hydrolyzed only slightly and salicin not at all. The enzyme catalyzes the hydrolysis of glucosidic linkages in such a manner that the product retains the anomeric configuration of the substrate.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 6","pages":"Pages 589-594"},"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)80010-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84538591","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: 18

Synthesis of the four possible stereoisomers of 21-methyl-8-pentatriacontene, the female contact sex pheromone of the yellow-spotted longicorn beetle, Psacothea hilaris 黄斑天牛雌性接触性信息素21-甲基-8-五三康内烯四种可能立体异构体的合成

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80366-2

Eiichiro Fukusaki , Shiro Satoda , Hiroyuki Yuasa , Shuji Senda , Tetsuo Omata , Midori Fukaya , Sadao Wakamura

引用次数: 6

Interaction between homoacetogens and methanogens in lake sediments 湖泊沉积物中同质产氧菌与产甲烷菌的相互作用

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80153-0

Jiunn-Jyi Lay , Yu-You Li , Tatsuya Noike

{"title":"Interaction between homoacetogens and methanogens in lake sediments","authors":"Jiunn-Jyi Lay , Yu-You Li , Tatsuya Noike","doi":"10.1016/S0922-338X(98)80153-0","DOIUrl":"10.1016/S0922-338X(98)80153-0","url":null,"abstract":"<div>The interaction between homoacetogens and methanogens in lake sediments was investigated using hydrogen consumption as an indicator. Sediments samples were obtained from Lake Izunuma, Miyagi prefecture, Japan, a wintering place for migratory birds from Siberia. A batch experiment using <math><mtext>H</mtext><msub><mi></mi><mn>2</mn></msub><mtext>CO</mtext><msub><mi></mi><mn>2</mn></msub></math> as a substrate was conducted to determine the acetate generation and methane production potential of the sediments. Incubation for 4 d at 37°C gave the following stoichiometric equation: 88H2 + 39HCO3− + 22H+ → 17CH3COO− + 5CH4 + 83H2O. The activities, νm, of hydrogen-utilizing homoacetogens and methanogens respectively ranged from 3.2 to 48 and from 1.8 to 3.2 mgCOD·gVSS−1·h−1. The population of hydrogen-utilizing homoacetogens was determined to be 2.6 × 108 MPN·gVSS−1, which was approximately two orders of magnitude higher than that of hydrogen-utilizing methanogens. The results suggest that homoacetogens in the sediments functioned not only as hydrogen consumers but also as major degraders of organic matter, forming acetate as the major reduction product.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 5","pages":"Pages 467-471"},"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)80153-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76373597","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: 44

Purification and comparison of phosphoglycerate kinases from nitrifying bacteria 硝化细菌中磷酸甘油酸激酶的纯化与比较

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)89002-3

Y. Mizuno, M. Ohshima, Ya-Feng Yao, R. Shibasaki, R. Takahashi, T. Tokuyama

引用次数: 8

High cell density culture of Rhodococcus rhodochrous by pH-stat feeding and dibenzothiophene degradation ph -稳态饲养和二苯并噻吩降解法培养红红红球菌

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)85685-1

Hiroyuki Honda, Hiroyasu Sugiyama, Ikuo Saito, Takeshi Kobayashi

{"title":"High cell density culture of Rhodococcus rhodochrous by pH-stat feeding and dibenzothiophene degradation","authors":"Hiroyuki Honda, Hiroyasu Sugiyama, Ikuo Saito, Takeshi Kobayashi","doi":"10.1016/S0922-338X(97)85685-1","DOIUrl":"10.1016/S0922-338X(97)85685-1","url":null,"abstract":"<div>A high cell density culture of Rhodococcus rhodochrous IGTS8 was investigated. Acetic acid was one of the most suitable carbon sources for cell growth and sulfate ion was more suitable than dibenzothiophene (DBT) as a sulfur source. Fed-batch culture was conducted in a 1-l jar fermentor with FB medium containing acetic acid and sulfate ion as carbon and sulfur sources. Cell growth was found to be inhibited when the concentrations of acetic acid and ammonium ion were above 3 g/l. To control the concentrations of the two components below 3 g/l, a mixture of acetic acid and ammonium acetate was supplied by means of pH-stat feeding. As a result, a cell concentration of 33 g dry cells/l was obtained after 28-h cultivation. When the cells obtained were incubated in a fresh medium containing DBT as a substrate, hydroxybiphenyl (HBP), which is the end-product of the DBT degradation pathway, was detected and its production rate gradually increased with incubation time. Incubation for 3 to 4 h was enough for the full induction of DBT-degrading enzymes, and the specific production rate of HBP was about 6.1 mmol/kg dry cells/h. A two-phase cultivation (cell growth phase and induction phase) is proposed in order to obtain a high cell density and full induction of DBT-degrading enzymes.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 3","pages":"Pages 334-338"},"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)85685-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81553160","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: 64

Modification of metabolic pathways of Saccharomyces cerevisiae by the expression of lactate dehydrogenase and deletion of pyruvate decarboxylase genes for the lactic acid fermentation at low pH value 低pH条件下乳酸发酵乳酸脱氢酶基因的表达和丙酮酸脱羧酶基因的缺失对酿酒酵母代谢途径的修饰

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80131-1

Eri Adachi, Mikiko Torigoe, Minetaka Sugiyama, Jun-Ichi Nikawa, Kazuyuki Shimizu

{"title":"Modification of metabolic pathways of Saccharomyces cerevisiae by the expression of lactate dehydrogenase and deletion of pyruvate decarboxylase genes for the lactic acid fermentation at low pH value","authors":"Eri Adachi, Mikiko Torigoe, Minetaka Sugiyama, Jun-Ichi Nikawa, Kazuyuki Shimizu","doi":"10.1016/S0922-338X(98)80131-1","DOIUrl":"10.1016/S0922-338X(98)80131-1","url":null,"abstract":"<div>Extractive lactic acid fermentation has recently been paid a great deal of attention. The problem with such a process is, however, that only undissociated lactate can be extracted. Therefore, lactic acid fermentation at low pH values is desirable. In the present study, we modified the metabolism of yeast (not lactic acid producing bacteria often cultivated at pH of 6–7) by expressing the lactate dehydrogenase (LDH) gene for the production of lactate at low pH values. For this purpose, the plasmid pADNS which contains the ADH1 promoter was used as a host vector, and a heterologous gene region, cDNA-LDH-A (encoding bovine lactate dehydrogenase) digested from plasmid pLDH12 was digested and ligated into the aforementioned two host vectors. The resultant plasmids were then transformed into Saccharomyces cerevisiae DS37. Using this recombinant S. cerevisiae strain, several batch and fed-batch fermentations at aerobic, microaerobic, and anaerobic conditions were conducted at several pH values (4.5-3.5). Since the recombinant S. cerevisiae produced a considerable amount of ethanol as well as lactate (about 10 g/l), we disrupted several pyruvate decarboxylase (PDC) genes to suppress the ethanol formation. Among the PDC genes, PDC1, PDC5 and PDC6, PDC1 had the greatest effect on the cell growth and ethanol production. The plasmid which containing the LDH-A structure gene was then transformed into the mutant strain lacking the PDC1 gene. Cultivation of this strain improved the lactate yield from glucose (from 0.155 to 0.20) while suppressing ethanol formation (from 0.35 to 0.20).</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 3","pages":"Pages 284-289"},"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)80131-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80971084","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: 106

Optimizing the culture conditions for higher inulinase production by Kluyveromyces sp. Y-85 and scaling-up fermentation 优化Kluyveromyces sp. Y-85高产菊粉酶的培养条件及扩大发酵规模

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)89011-4

Wenling Wei, Zhonghui Zheng, Yueying Liu, Xinsheng Zhu

引用次数: 38

L(+)-Lactic Acid Production by Repeated Batch Culture of Rhizopus oryzae in Air-Lift Bioreactor 气升式生物反应器中米根霉重复间歇培养L(+)-乳酸的研究

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80361-3

P. Yin, Kazutoyo Yahiro, Tooru Ishigaki, Y. Park, M. Okabe

引用次数: 72

Synthesis of uridine 5′-monophosphate glucose as an inhibitor of UDP-glucose pyrophosphorylase 尿苷5′-单磷酸葡萄糖作为udp -葡萄糖焦磷酸化酶抑制剂的合成

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80052-4

Ken-Ichi Fujita, Teruhiko Tanigawa, Kiyotaka Machida, Toshio Tanaka, Makoto Taniguchi

{"title":"Synthesis of uridine 5′-monophosphate glucose as an inhibitor of UDP-glucose pyrophosphorylase","authors":"Ken-Ichi Fujita, Teruhiko Tanigawa, Kiyotaka Machida, Toshio Tanaka, Makoto Taniguchi","doi":"10.1016/S0922-338X(98)80052-4","DOIUrl":"10.1016/S0922-338X(98)80052-4","url":null,"abstract":"<div>Uridine 5′-monophosphate α-d-glucose (UMPG) was evaluated as a novel and potent inhibitor of the enzymatic reaction involved in sugar nucleotide metabolism. UMPG was synthesized by chemical coupling of 2,3,4,6-tetra-O-acetyl-α-d-glucopyranosyl bromide with uridine 5′-monophosphate (UMP) to give uridine 5′-monophosphate 2″,3″,4″,6″-tetra-O-acetyl-α-d-glucose (UMPTAG), followed by deacetylation of UMPTAG with sodium methoxide. In addition to UMPG, UMPTAG showed potent inhibitory activity toward yeast UDPG pyrophosphorylase (UDPG synthetase). UMPG and UMPTAG were competitive with UDPG in the pyrophosphorolytic reaction, with inhibition constants (Ki) of 4.8 and 20.7 μM, respectively, but non-competitive with inorganic pyrophosphate. UMPG and UMPTAG also inhibited the enzyme non-competitively in the reverse reaction to synthesize UDPG from UTP and glucose 1-phosphate (G1P). The acetyl group of UMPTAG was thought to enhance its hydrophobic interaction, possibly with an active site region of the enzyme functional for binding with UDPG.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 2","pages":"Pages 145-148"},"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)80052-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82831198","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: 3

Production and immobilization of lipase from Aeromonas sobria harboring a heterologous gene 含外源基因的温和气单胞菌脂肪酶的生产与固定化

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80140-2

Saovanee Dharmsthiti, Sudaporn Luchai

引用次数: 3