Journal of Fermentation and Bioengineering最新文献_第4页

Supplementation of NaCl to starter culture of the soy yeast Zygosaccharomyces rouxii 添加NaCl对大豆酵母鲁氏酵母发酵剂培养的影响

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(98)80021-4

Makio Kobayashi, Satomi Hayashi

引用次数: 12

Method of Corynebacterium glutamicum fermentation time extension with high lysine production rate by leucine addition 添加亮氨酸延长谷氨酸棒状杆菌发酵时间高产赖氨酸的方法

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(98)80058-5

Noboru Takiguchi, Naoki Fukui, Nobuyuki Shimizu, Hiroshi Shimizu, Suteaki Shioya

{"title":"Method of Corynebacterium glutamicum fermentation time extension with high lysine production rate by leucine addition","authors":"Noboru Takiguchi, Naoki Fukui, Nobuyuki Shimizu, Hiroshi Shimizu, Suteaki Shioya","doi":"10.1016/S0922-338X(98)80058-5","DOIUrl":"10.1016/S0922-338X(98)80058-5","url":null,"abstract":"<div>The effect of leucine addition on the production yield of lysine by Corynebacterium glutamicum AJ-3462 was studied and a method of increasing a fermentation time while maintaining high lysine producing activity was developed. When leucine was not added during the lysine production phase, a high molar production yield of lysine from glucose of 35.6% was obtained. However, lysine production did not continue for a long time and almost stopped at around 90 h. When leucine was added to the medium in the fermentor at 24 h intervals, lysine producing activity was maintained for a long time; however, the production yield of lysine from glucose was reduced to 23.5%. When leucine was added at 30 h intervals, the production yield of lysine from glucose was improved to 32.9%. However, leucine addition did not recover lysine producing activity after 162 h. From these results, in order to extend the fermentation time while maintaining lysine productivity and production yield at high values, a leucine addition strategy was developed as follows. The initial leucine concentration was set as 0.1 g/l. After depletion of leucine, it was added intermittently at 30 h intervals. The interval for intermittent addition was changed to 24 h when a decrease in cellular activity was recognized by on-line monitoring of the lysine production rate based on a metabolic reaction model. As a result, the fermentation time was extended to 174 h, and lysine productivity and total molar production yield of lysine from glucose became 0.104 g/l/h and 29.2%, respectively.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 2","pages":"Pages 180-184"},"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)80058-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86269669","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: 6

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 Epub Date: 2002-02-27 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

Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus aculeatus no. F-50 cellobiohydrolase I (cbhI) gene 刺曲霉的克隆、核苷酸序列及转录分析。F-50纤维生物水解酶I (cbhI)基因

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(97)80345-5

Goro Takada, Takashi Kawaguchi, Jun-Ichi Sumitani, Motoo Arai

{"title":"Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus aculeatus no. F-50 cellobiohydrolase I (cbhI) gene","authors":"Goro Takada, Takashi Kawaguchi, Jun-Ichi Sumitani, Motoo Arai","doi":"10.1016/S0922-338X(97)80345-5","DOIUrl":"https://doi.org/10.1016/S0922-338X(97)80345-5","url":null,"abstract":"<div>The cbhI gene, coding for a major cellobiohydrolase (CBHI) of Aspergillus aculeatus, was cloned and sequenced. The gene consists of 1620-bp and encodes a protein containing 540 amino acids with a calculated molecular mass of 56,723 Da. CBHI, composed of an N-terminal catalytic domain belonging to family 7 of the glycosyl hydrolases, and a C-terminal cellulose-binding domain (CBD) belonging to family I of the CBDs, showed high similarity with other fungal CBHIs, especially with that of Penicillium janthinellum. The cbhI gene transcription start points in A. aculeatus were defined by primer extension, and the putative promoter sequence was analyzed. This sequence was found to be closely related to the consensus sequences of various fungal genes. Transcription analysis by ribonuclease protection assay revealed that the cbhI gene is induced by low-molecular-weight cellooligosaccharide and repressed by glucose. The results emphasize the possibility that in the A. aculeatus cellulase system, cellobiose is the true inducer and the role of the cbhI gene lies within the cascade regulating cellulase induction.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 1","pages":"Pages 1-9"},"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)80345-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91704883","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: 22

Discovery of a new mechanism of 2,3-butanediol stereoisomer formation in Bacillus cereus YUF-4 蜡样芽孢杆菌YUF-4中2,3-丁二醇立体异构体形成新机制的发现

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80358-3

S. Ui, T. Hosaka, Kazuhide Watanabe, A. Mimura

引用次数: 21

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

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

Purification and characterization of α-amylase from hyperthermophilic archaeon Thermococcus profundus, which hydrolyzes both α-1,4 and α-1,6 glucosidic linkages 水解α-1,4和α-1,6糖苷键的超嗜热古细菌深热球菌α-淀粉酶的纯化及特性研究

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)89005-9

Y. Kwak, T. Akiba, T. Kudo

引用次数: 31

Purification and characterization of component B of a soluble methane monooxygenase from Methylocystis sp. M 甲基藻可溶性甲烷单加氧酶B组分的纯化及特性研究

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80350-9

Y. Shinohara, H. Uchiyama, O. Yagi, I. Kusakabe

引用次数: 14

Effect of oxygen on the growth of Clostridium butyricum (type species of the genus Clostridium), and the distribution of enzymes for oxygen and for active oxygen species in Clostridia 氧对丁酸梭菌(梭菌属模式种)生长的影响及梭菌体内氧酶和活性氧酶的分布

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 Epub Date: 2002-02-27 DOI: 10.1016/S0922-338X(99)89006-0

Sinji Kawasaki , Tomoyuki Nakagawa , Yoshitaka Nishiyama , Yoshimi Benno , Tai Uchimura , Kazuo Komagata , Michio Kozaki , Youichi Niimura

{"title":"Effect of oxygen on the growth of Clostridium butyricum (type species of the genus Clostridium), and the distribution of enzymes for oxygen and for active oxygen species in Clostridia","authors":"Sinji Kawasaki , Tomoyuki Nakagawa , Yoshitaka Nishiyama , Yoshimi Benno , Tai Uchimura , Kazuo Komagata , Michio Kozaki , Youichi Niimura","doi":"10.1016/S0922-338X(99)89006-0","DOIUrl":"10.1016/S0922-338X(99)89006-0","url":null,"abstract":"<div>Clostridia are well-known obligatory anaerobic bacteria which cannot utilize oxygen, or otherwise die in oxygenated environments. Clostridium butyricum, the type species of the genus Clostridium, possesses the ability to consume oxygen in amounts proportional to the size of the inoculum. Oxygen consumption was observed when NADH and NADPH were added to the cell extract of this strain. NADH oxidase and NADPH oxidase activities were also detected in all of the tested strains of the genus Clostridium. C. butyricum ceased growing while consuming oxygen in the medium. After consumption of all the dissolved oxygen, C. butyricum resumed growth at a rate equivalent to its anaerobic growth rate, suggesting that no oxidative damage based on oxygen reduction occurs in vivo. As scavengers for active oxygen species, the activities of <math><mtext>NADH</mtext><mtext>NADPH</mtext></math> peroxidase and SOD were detected in C. butyricum. Furthermore, the activities of these enzymes are distributed widely in the genus Clostridium.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 4","pages":"Pages 368-372"},"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)89006-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74888187","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: 56