Journal of Fermentation and Bioengineering最新文献_第8页

Analysis of acclimation behavior against nitrification inhibitors in activated sludge processes 活性污泥法对硝化抑制剂的驯化行为分析

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80115-3

Xiaojing Xiong, Makoto Hirata, Hirokazu Takanashi, Min-Gyu Lee , Tadashi Hano

引用次数: 12

Site-directed mutagenesis of histidine residues in the ethylene-forming enzyme from Pseudomonas syringae 丁香假单胞菌乙烯形成酶组氨酸残基的定点突变

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)85671-1

Kazuhiro Nagahama , Kuniaki Yoshino , Masayoshi Matsuoka , Sumio Tanase , Takahira Ogawa , Hideo Fukuda

{"title":"Site-directed mutagenesis of histidine residues in the ethylene-forming enzyme from Pseudomonas syringae","authors":"Kazuhiro Nagahama , Kuniaki Yoshino , Masayoshi Matsuoka , Sumio Tanase , Takahira Ogawa , Hideo Fukuda","doi":"10.1016/S0922-338X(97)85671-1","DOIUrl":"10.1016/S0922-338X(97)85671-1","url":null,"abstract":"<div>The roles of histidine residues in the catalysis of the transformation of 2-oxoglutarate into ethylene via the ethylene-forming enzyme (EFE) from Pseudomonas syringae were studied using site-directed mutagenesis with substitution of glutamine for ten individual histidine residues. The mutant enzymes, which were expressed in Escherichia coli, were purified to homogeneity, and assayed in vitro for Km, kcat and thermostability. The relative kcat of two mutated EFEs, H305Q and H335Q, were 40% and 60%, respectively. However, a mutation at either His-189 or His-233 caused a total loss of activity, implying that these residues play important roles in the binding of iron. The kcat values for other mutant enzymes were 11-to 55-fold less than that for the wild-type enzyme. For six partially inactive mutated EFEs (but not for H305Q or H335Q), the first order rate constants for heat inactivation at 30°C were 11-to 24-fold higher than for the wild-type enzyme. It is noteworthy that the value of the first order rate constant for heat inactivation of H268Q was identical to that of H335Q. The substitution of H268 resulted in a drastic decrease of the kcat value (relative kcat was 1.8%). This suggests that the substitution at His-268 may cause the disruption of the active site of the EFE. Heat inactivation studies with the puridied mutant enzymes revealed that some mutant enzymes, such as H168Q and H116Q, were more thermolabile than the wild-type enzyme.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 3","pages":"Pages 255-258"},"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)85671-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77595666","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: 13

Asymmetric reduction of methyl 3-oxopentanoate by Chlorella 小球藻对3-氧戊酸甲酯的不对称还原

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80091-3

Fumiki Yoshizako, Takayuki Kuramoto, Atsuo Nishimura, Mitsuo Chubachi

引用次数: 9

An approach to high-level production of cephalosporin acylase from Pseudomonas strain N176 in Escherichia coli 假单胞菌N176在大肠杆菌中高效生产头孢菌素酰化酶的途径

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80019-6

Yuji Noguchi, Hisashi Yamada, Michitaka Yamaguchi, Katsuyuki Watanabe, Takao Fujimura, Yoshinori Ishii, Yoshimasa Saito

引用次数: 1

High Production of Pyoluteorin and 2, 4-Diacetylphloroglucinol by Pseudomonas fluorescens S272 Grown on Ethanol as a Sole Carbon Source 以乙醇为唯一碳源培养荧光假单胞菌S272高产吡咯啉和2,4 -二乙酰间苯三酚

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)80006-3

Zhan Yuan, S. Cang, M. Matsufuji, K. Nakata, Y. Nagamatsu, A. Yoshimoto

引用次数: 44

Fatty acid desaturation in methylotrophic yeast Hansenula polymorpha strain CBS 1976 and unsaturated fatty acid auxotrophic mutants 甲基营养酵母菌CBS 1976与不饱和脂肪酸营养缺陷突变体的脂肪酸去饱和

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80065-2

Sarintip Anamnart , Ilya Tolstorukov , Yoshinobu Kaneko , Satoshi Harashima

{"title":"Fatty acid desaturation in methylotrophic yeast Hansenula polymorpha strain CBS 1976 and unsaturated fatty acid auxotrophic mutants","authors":"Sarintip Anamnart , Ilya Tolstorukov , Yoshinobu Kaneko , Satoshi Harashima","doi":"10.1016/S0922-338X(98)80065-2","DOIUrl":"10.1016/S0922-338X(98)80065-2","url":null,"abstract":"<div>Analysis of fatty acid composition in wild-type cells of Hansenula polymorpha strain CBS 1976 revealed the presence of 18 : 1 (Δ9), 18 : 2 (Δ9,12) and 18 : 3 (Δ9,12,15) unsaturated fatty acids (UFAs), indicating that the α-linolenic desaturation pathway operates in this yeast. H. polymorpha cells also showed ability for uptake and incorporation of exogenous UFAs. By ethyl methanesulfonate mutagenesis, nine unsaturated fatty acid auxotrophic mutants of H. polymorpha were isolated. These mutants exhibited the growth arrest phenotype on nutrient medium and on nutrient medium supplemented with saturated fatty acids, but grew on media supplemented with various UFAs. Genetic analysis revealed that single recessive nuclear mutation conferred Ufa auxotrophy on these mutants. Fatty acid analysis by gas chromatography showed the accumulation of 18 : 0 but a decrease in the amount of 18 : 1 and 18 : 2 in mutant cells compared with the wild-type cells. Integrated physiological and genetical data suggested that mutations in all mutants occurred in one gene and probably led to defects in Δ9-desaturation pathway.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 5","pages":"Pages 476-482"},"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)80065-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78874170","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: 20

Effect of hyper-salt stress on the heat resistance of a halotolerant Brevibacterium sp. JCM6894 超盐胁迫对耐盐短杆菌JCM6894耐热性的影响

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)86765-7

Haruo Mimura, Shinichi Nagata

{"title":"Effect of hyper-salt stress on the heat resistance of a halotolerant Brevibacterium sp. JCM6894","authors":"Haruo Mimura, Shinichi Nagata","doi":"10.1016/S0922-338X(97)86765-7","DOIUrl":"10.1016/S0922-338X(97)86765-7","url":null,"abstract":"<div>The heat resistance of Brevibacterium sp. JCM6894 was examined as a function of externally added NaCl concentrations. About a 5-log cycle reduction of the viable cell numbers was observed to result from heat treatment for 30 min at 47°C in the absence of NaCl. When the cells were heated in the buffer containing 2 M NaCl, the viability was maintained within less than 1-log cycle reduction after incubation for 30 min at 56°C. During the heat treatment for 30 min at 47°C in the presence of 2 M NaCl, Na+ and K+ ions in the cells increased and decreased by 13 and 26 μg ions per mg of cell protein, respectively. Under this condition, the amount of free amino acids in the cells changed little except for glutamate and hydroxyproline, which were reduced by 72 and 43 nmol per mg cell protein, respectively. These results indicate that the salt stress itself and Na+ ions existing in the cytoplasm are more important factors than in vivo protein synthesis for preventing the thermal death of the resting cells of this strain.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 2","pages":"Pages 185-189"},"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)86765-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79632731","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: 5

Purification and characterization of β-xylosidase from Thermoascus sp. 热曲霉β-木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(99)89013-8

Masaru Matsuo , Akio Endou , Takahiro Okada , Yuuichi Yamaoka

{"title":"Purification and characterization of β-xylosidase from Thermoascus sp.","authors":"Masaru Matsuo , Akio Endou , Takahiro Okada , Yuuichi Yamaoka","doi":"10.1016/S0922-338X(99)89013-8","DOIUrl":"10.1016/S0922-338X(99)89013-8","url":null,"abstract":"<div>A β-xylosidase was purified from the culture filtrate of the thermophilic fungus Thermoascus sp. by ultrafiltration, ethanol precipitation, and chromatography with DEAE-Toyopearl 650M, Mono Q <math><mtext>HR5</mtext><mtext>5</mtext></math>, and Phenyl Superose <math><mtext>HR5</mtext><mtext>5</mtext></math>. The purified β-xylosidase was found to be homogeneous on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Its molecular weight was estimated to be 107 kDA by gel filtration chromatography (Superdex 200 HR) and 100 kDa by SDS-PAGE. The optimum activity of the enzyme was observed at pH 4.5 and 55°C. The enzyme was stable up to 60°C at pH 4.5 for 1 h. The enzyme exhibited hydrolytic activity on phenyl β-d-xyloside and xylan (birch wood). Fifteen of the amino acid residues in the amino terminal region of the Thermoascus sp. β-xylosidase were homologous with residues in the equivalent region of the maturation protein β-glucosidase from Aspergillus aculeatus.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 4","pages":"Pages 403-405"},"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)89013-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79917910","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: 13

Effect of acetic and butyric acids on the stability of solvent and spore formation by Clostridium acetobutylicum ATCC 824 during repeated subculturing 乙酸和丁酸对醋酸丁酸梭菌ATCC 824反复传代培养过程中溶剂稳定性和孢子形成的影响

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)86769-4

Omar Assobhei , Abdellah El Kanouni , Mohammed Ismaili , Mohammed Loutfi , Henri Petitdemange

引用次数: 28

Removal of mercury ion by the moss Pohlia flexuosa 苔藓对汞离子的去除作用

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80061-5

Mitsuyo Kondoh , Masanori Fukuda , Masayuki Azuma , Hiroshi Ooshima , Jyoji Kato

引用次数: 11