We reported that Neurospora sp. ATCC 46892 produced a fruity odor, for which ethyl caproate may be responsible, I) but few studies have been done on odor production by other Neurospora strains. This study was aimed at examining the production of odors by several Neurospora strains. We examined 12 Neurospora strains, including the ATCC 46892 dscribed previously. I) Neurospora sp. T, which was newly isolated from beiju, a fermented food in Brazil, had been obtained from Dr. Satoh (Universidade Estadual de Campinas, Brazil) and was classified by us from its morphological characteristics. Other strains were purchased from the Institute for Fermentation, Osaka, Japan. These Neurospora strains were inoculated into 5% malt broth and grown aerobically at 30°C for several days in a 500-ml shaking flask. Then each culture was filtered through Miracloth (Calbiochem Corp.) or a microfilter (0.45/lm). Volatiles were extracted and analyzed. Two hundred and fifty ml of the filtrate obtained was saturated with NaCI and then 125 ml of ethyl acetate containing an internal standard, methyl caproate, was added to extract volatiles. After the mixture was shaken vigorously for one minute by a Mini-Beadbeater (Biospec Products), four microliters of the extract was analyzed by GC or GC-MS. GC was done with a Perkin-Elmer 8320B capillary gas chromatograph. The conditions were the same as described elsewhere3) with some modifications: column, a bonded fused silica capillary column, 15 m, 0.53 mm i.d., film thickness = 1.0 /lm; stationary phase, DB-WAX from J and W Scientfic Inc.; carrier gas, helium at 4.6ml/min (split ratio = 1/5); column temperature, kept at 70°C for 3 min, raised from 70°C to lOO°C at the rate of lOoC per min, from lOO°C to 230°C at the rate of 20°C per min and then kept at 230°C for 7.5min; injection port and detector temperature 250°C. GC-MS was done with a Hewlett Packard 5970B GCMS System. The conditions of gas chromatography were Table I. ODOR FORMATION BY VARIOUS Neurospora STRAINS The experimental details are given in the text.
{"title":"Production of Characteristic Odors by Neurospora","authors":"H. Yamauchi, T. Obata, T. Amachi, S. Hara","doi":"10.1271/BBB1961.55.3115","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3115","url":null,"abstract":"We reported that Neurospora sp. ATCC 46892 produced a fruity odor, for which ethyl caproate may be responsible, I) but few studies have been done on odor production by other Neurospora strains. This study was aimed at examining the production of odors by several Neurospora strains. We examined 12 Neurospora strains, including the ATCC 46892 dscribed previously. I) Neurospora sp. T, which was newly isolated from beiju, a fermented food in Brazil, had been obtained from Dr. Satoh (Universidade Estadual de Campinas, Brazil) and was classified by us from its morphological characteristics. Other strains were purchased from the Institute for Fermentation, Osaka, Japan. These Neurospora strains were inoculated into 5% malt broth and grown aerobically at 30°C for several days in a 500-ml shaking flask. Then each culture was filtered through Miracloth (Calbiochem Corp.) or a microfilter (0.45/lm). Volatiles were extracted and analyzed. Two hundred and fifty ml of the filtrate obtained was saturated with NaCI and then 125 ml of ethyl acetate containing an internal standard, methyl caproate, was added to extract volatiles. After the mixture was shaken vigorously for one minute by a Mini-Beadbeater (Biospec Products), four microliters of the extract was analyzed by GC or GC-MS. GC was done with a Perkin-Elmer 8320B capillary gas chromatograph. The conditions were the same as described elsewhere3) with some modifications: column, a bonded fused silica capillary column, 15 m, 0.53 mm i.d., film thickness = 1.0 /lm; stationary phase, DB-WAX from J and W Scientfic Inc.; carrier gas, helium at 4.6ml/min (split ratio = 1/5); column temperature, kept at 70°C for 3 min, raised from 70°C to lOO°C at the rate of lOoC per min, from lOO°C to 230°C at the rate of 20°C per min and then kept at 230°C for 7.5min; injection port and detector temperature 250°C. GC-MS was done with a Hewlett Packard 5970B GCMS System. The conditions of gas chromatography were Table I. ODOR FORMATION BY VARIOUS Neurospora STRAINS The experimental details are given in the text.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"88 1","pages":"3115-3116"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81915304","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}
The xylose isomerase gene from the thermophile Clostridium thermohydrosulfuricum has been cloned into Bacillus brevis. Under control of the strong cell wall protein promoter, the gene was efficiently expressed during the early stationary phase of growth, when cell densities were high. The expressed gene product was a soluble cytoplasmic protein and made up more than 20% of the total cellular protein. A simple heat treatment at 85°C for 10 min gave a virtually pure enzyme. Final isomerase yields were about 0.5 g isomerase per liter culture. The purified isomerase has an optimum temperature at 85°C, and an optimum pH around 7. The isomerase is stable at 85°C for several hours, opening possibilities for new uses.
{"title":"Production of Thermostable Clostridium thermohydrosulfuricum Xylose Isomerase in Bacillus brevis(Microbiology & Fermentation Industry)","authors":"K. Dekker, H. Yamagata, K. Sakaguchi, S. Udaka","doi":"10.1271/BBB1961.55.2993","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2993","url":null,"abstract":"The xylose isomerase gene from the thermophile Clostridium thermohydrosulfuricum has been cloned into Bacillus brevis. Under control of the strong cell wall protein promoter, the gene was efficiently expressed during the early stationary phase of growth, when cell densities were high. The expressed gene product was a soluble cytoplasmic protein and made up more than 20% of the total cellular protein. A simple heat treatment at 85°C for 10 min gave a virtually pure enzyme. Final isomerase yields were about 0.5 g isomerase per liter culture. The purified isomerase has an optimum temperature at 85°C, and an optimum pH around 7. The isomerase is stable at 85°C for several hours, opening possibilities for new uses.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"50 1","pages":"2993-2998"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88835051","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}
Pub Date : 1991-12-23DOI: 10.1080/00021369.1991.10857913
M. Kirihata, T. Kaziwara, Y. Kawashima, I. Ichimoto
{"title":"An Efficient Synthesis of (±)-α-Kainic Acid Using a 3-Hydroxyallylglycine Derivative as a Common Building Block(Organic Chemistry)","authors":"M. Kirihata, T. Kaziwara, Y. Kawashima, I. Ichimoto","doi":"10.1080/00021369.1991.10857913","DOIUrl":"https://doi.org/10.1080/00021369.1991.10857913","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"59 1","pages":"3033-3037"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86403551","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}
M. Ishii, T. Omori, Y. Igarashi, O. Adachi, M. Ameyama, T. Kodama
The hydrogenase reaction in Hydrogenobacter thermophilus strain TK-6, an obligately autotrophic, thermophilic, aerobic hydrogen-oxidizing bacterium, was studied in the membrane fraction, methionaquinone-depleted membrane, and purified membrane-bound hydrogenase. Both b and c type cytochromes were involved in the hydrogen oxidation. Methionaquinone mediated an electron transport between membrane-bound hydrogenase and cytochrome b560. Methionaquinone was reduced directly by purified hydrogenase. From these results, we conclude that methionaquinone is a direct natural electron acceptor for the membrane-bound hydrogenase in the strain.
{"title":"Methionaquinone is a Direct Natural Electron Acceptor for the Membrane-bound Hydrogenase in Hydrogenobacter thermophilus Strain TK-6","authors":"M. Ishii, T. Omori, Y. Igarashi, O. Adachi, M. Ameyama, T. Kodama","doi":"10.1271/BBB1961.55.3011","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3011","url":null,"abstract":"The hydrogenase reaction in Hydrogenobacter thermophilus strain TK-6, an obligately autotrophic, thermophilic, aerobic hydrogen-oxidizing bacterium, was studied in the membrane fraction, methionaquinone-depleted membrane, and purified membrane-bound hydrogenase. Both b and c type cytochromes were involved in the hydrogen oxidation. Methionaquinone mediated an electron transport between membrane-bound hydrogenase and cytochrome b560. Methionaquinone was reduced directly by purified hydrogenase. From these results, we conclude that methionaquinone is a direct natural electron acceptor for the membrane-bound hydrogenase in the strain.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"11 1","pages":"3011-3016"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73663811","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":"Effects on Plant Growth of the HMG-CoA Synthase Inhibitor, 1233A/F-244/L-659,699, Isolated from Scopulariopsis candidus","authors":"J. Jacyno, H. Cutler, R. G. Roberts, R. Waters","doi":"10.1271/BBB1961.55.3129","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3129","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"37 1","pages":"3129-3131"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78887252","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}
Y. Morishita, Mitsuru Takahashi, T. Sano, I. Kawamoto, K. Ando, H. Sano, Y. Saitoh, H. Kase, Y. Matsuda
During the screening program for atrial natriuretic peptide (ANP) receptor ligands of microbial origin, we isolated a novel nonpeptide ANP antagonist, HS-142-1, from a culture broth of Aureo-basidium pullulans var. melanigenum. Structural analysis showed that HS-142-1 was composed of 20–30 kinds of β-1,6-glucan esterified by caproyl groups; each component had an almost equal potency. HS-142-1 inhibited [125I]-rANP binding to its receptor in rabbit kidney cortex membranes with an IC50 of 0.3μg/ml and antagonized ANP-induced cGMP production by bovine lung membranes in a dose-dependent fashion. The discovery of this nonpeptide ANP antagonist, HS-142-1, will provide a useful tool to study the physiological significance of natriuretic peptide system.
在筛选微生物来源的心房利钠肽(ANP)受体配体的过程中，我们从金黄色担子菌(Aureo-basidium pullulans vars . melanigenum)培养液中分离出一种新的非肽类ANP拮抗剂HS-142-1。结构分析表明，HS-142-1由20 ~ 30种经己基酯化的β-1,6-葡聚糖组成;每种成分的效力几乎相等。HS-142-1抑制兔肾皮质膜[125I]-rANP与其受体结合的IC50为0.3μg/ml，并呈剂量依赖性地拮抗anp诱导的牛肺膜cGMP产生。这种非肽类ANP拮抗剂HS-142-1的发现将为研究利钠肽系统的生理意义提供有用的工具。
{"title":"Isolation and Purification of HS-142-1, a Novel Nonpeptide Antagonist for the Atrial Natriuretic Peptide Receptor, from Aureobasidium sp.","authors":"Y. Morishita, Mitsuru Takahashi, T. Sano, I. Kawamoto, K. Ando, H. Sano, Y. Saitoh, H. Kase, Y. Matsuda","doi":"10.1271/BBB1961.55.3017","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3017","url":null,"abstract":"During the screening program for atrial natriuretic peptide (ANP) receptor ligands of microbial origin, we isolated a novel nonpeptide ANP antagonist, HS-142-1, from a culture broth of Aureo-basidium pullulans var. melanigenum. Structural analysis showed that HS-142-1 was composed of 20–30 kinds of β-1,6-glucan esterified by caproyl groups; each component had an almost equal potency. HS-142-1 inhibited [125I]-rANP binding to its receptor in rabbit kidney cortex membranes with an IC50 of 0.3μg/ml and antagonized ANP-induced cGMP production by bovine lung membranes in a dose-dependent fashion. The discovery of this nonpeptide ANP antagonist, HS-142-1, will provide a useful tool to study the physiological significance of natriuretic peptide system.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"38 1","pages":"3017-3025"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90280094","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}
high-performance liquid chromatographic measurements of nicotinamide3' and its major catabolic metabolites such as MNA,4) 2-Py,5) and A^-methyM-pyridone-S-carboxamide (4-Py),6) and have been investigating the effects of nutrients on the metabolic fate of nicotinamide in rats. However, our results did not indicate any evident relationship between the urinary excretion of (2-Py+4Py)/MNAand niacin status. Under speciffed conditions, its excretion ratio reflected an adequacy of amino acid nutrition,7~12) and even when the amino acid nutrition was adequate, an excess administration of tryptophan,13)
高效液相色谱法测定了烟酰胺3′及其主要分解代谢产物如MNA,4) 2-Py,5)和A^-甲基-吡啶酮- s -羧酰胺(4- py)，6)，并研究了营养物质对烟酰胺代谢命运的影响。然而，我们的研究结果并没有显示尿中(2-Py+4Py)/ mna与烟酸状态之间有任何明显的关系。在特定的条件下，它的排泄率反映了氨基酸营养的充足性(7~12)，即使氨基酸营养充足，色氨酸的过量摄入(13)。
{"title":"Effect of Lipid Peroxidation Products on the Catabolic Fate of Nicotinamide in Rats","authors":"K. Shibata, M. Onodera, H. Ashida, K. Kanazawa","doi":"10.1271/BBB1961.55.3113","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3113","url":null,"abstract":"high-performance liquid chromatographic measurements of nicotinamide3' and its major catabolic metabolites such as MNA,4) 2-Py,5) and A^-methyM-pyridone-S-carboxamide (4-Py),6) and have been investigating the effects of nutrients on the metabolic fate of nicotinamide in rats. However, our results did not indicate any evident relationship between the urinary excretion of (2-Py+4Py)/MNAand niacin status. Under speciffed conditions, its excretion ratio reflected an adequacy of amino acid nutrition,7~12) and even when the amino acid nutrition was adequate, an excess administration of tryptophan,13)","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"51 1","pages":"3113-3114"},"PeriodicalIF":0.0,"publicationDate":"1991-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88953098","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}
A transformation system with efficiencies between 6 and 50 stable transformants per micrograms of DNA was developed for Penicillium urticae J1 (ATCC48163) using hygromycin B-resistant plasmids containing or not containing fragments of the P. urticae genome. The tandem repeated integration and/or random integration of vector DNA were observed. Although P. urticae was unable to grow in the presence of 200 micrograms/ml hygromycin B, the transformants were resistant to more than 5 mg/ml of hygromycin B.
{"title":"Transformation of Penicillium urticae with plasmids containing the hygromycin B resistance gene.","authors":"N Kiuchi, A Naruse, H Yamamoto, J Sekiguchi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A transformation system with efficiencies between 6 and 50 stable transformants per micrograms of DNA was developed for Penicillium urticae J1 (ATCC48163) using hygromycin B-resistant plasmids containing or not containing fragments of the P. urticae genome. The tandem repeated integration and/or random integration of vector DNA were observed. Although P. urticae was unable to grow in the presence of 200 micrograms/ml hygromycin B, the transformants were resistant to more than 5 mg/ml of hygromycin B.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","pages":"3053-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12541907","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}
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