Journal of Fermentation and Bioengineering最新文献_第10页

Purification and identification of the promoter of sediment formation from raw soy sauce by heating 生酱油热沉促进剂的纯化与鉴定

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)89007-2

Masahiro Tomita , Yoshie Motomura , Haruo Kitahara , Yumiko Yoshiki , Kazuyoshi Okubo

{"title":"Purification and identification of the promoter of sediment formation from raw soy sauce by heating","authors":"Masahiro Tomita , Yoshie Motomura , Haruo Kitahara , Yumiko Yoshiki , Kazuyoshi Okubo","doi":"10.1016/S0922-338X(99)89007-2","DOIUrl":"https://doi.org/10.1016/S0922-338X(99)89007-2","url":null,"abstract":"<div>Soy sauce contains promoters of sediment formation at 60°C. These promoters were extracted with 1-butanol from raw soy sauce, followed by acetonitrile extraction. The acetonitrile-soluble fraction was used for further separation of the promoter of sediment formation, as the specific activity of the acetonitrile-soluble fraction was higher than that of the insoluble fraction. The promoter of sediment formation could be separated as a single peak from the main low-molecular weight peak on a Sephadex G-10 column by means of HPLC on a LiChrospher (RP-18) column. The active fraction for sediment forming-activity separated by three columns, namely, a LiChrospher (RP-18) column, an Alltech 700CH carbohydrate column and a Shodex OHpak Q-801 column, was observed as a single peak. 0.08 g of promoter was obtained from 1l of raw soy sauce. The 13C, 1H NMR and 1H-1H COSY spectral data identified the purified promoter as l-glutamic acid 5-n-butyl ester. l-Glutamic acid 5-n-butyl ester was synthesized and identified as a promoter by HPLC and 1H NMR analysis. In addition, the existence of l-glutamic acid 5-n-butyl ester in raw soy sauce was confirmed by HPLC analysis of the extract without 1-butanol extraction from raw soy sauce.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 4","pages":"Pages 373-378"},"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)89007-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91610913","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: 4

Bioconversion of indene to cis (1S,2R) indandiol and trans (1R,2R) indandiol by Rhodococcus species 红球菌将茚二醇转化为顺式(1S,2R)茚二醇和反式(1R,2R)茚二醇

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)80005-1

Michel Chartrain, Barbara Jackey, Colleen Taylor, Vanessa Sandford, Kodzo Gbewonyo, Leonard Lister, Lisa Dimichele, Charles Hirsch, Brian Heimbuch, Carrie Maxwell, Deborah Pascoe, Barry Buckland, Randolph Greasham

{"title":"Bioconversion of indene to cis (1S,2R) indandiol and trans (1R,2R) indandiol by Rhodococcus species","authors":"Michel Chartrain, Barbara Jackey, Colleen Taylor, Vanessa Sandford, Kodzo Gbewonyo, Leonard Lister, Lisa Dimichele, Charles Hirsch, Brian Heimbuch, Carrie Maxwell, Deborah Pascoe, Barry Buckland, Randolph Greasham","doi":"10.1016/S0922-338X(99)80005-1","DOIUrl":"https://doi.org/10.1016/S0922-338X(99)80005-1","url":null,"abstract":"<div>cis (1S,2R) indandiol or trans (1R,2R) indandiol are both potential precursors to (−)-cis (1S,2R)-1-aminoindan-2-ol, a key chiral synthon for Crixivan® (Indinavir), a leading HIV protease inhibitor. Enrichment and isolation studies yielded two Rhodococcus sp. strain B 264-1 (MB 5655) and strain I-24 (MA 7205) capable of biotransforming indene to cis (1S,2R) indandiol and trans (1R,2R) indandiol respectively. Isolate MB 5655 was found to have a toluene dioxygenase, while isolate MA 7205 was found to harbor both toluene and naphthalene dioxygenases as well as a naphthalene monooxygenase. When scaled up in a 14-l bioreactor, MB 5655 produced up to 2.0 g/l of cis (1S,2R) indandiol with an enantiometric excess greater than 99%. MA 7205 cultivated under similar conditions produced up to 1.4 g/l of trans (1R,2R) indandiol with an enantiomeric excess greater than 98%. Process development studies yielded titers greater that 4.0 g/l of cis indandiol for MB 5655. Due to their resistance to indene toxicity and easy cultivation in bioreactors, both Rhodococcus sp. strains appeared as good candidates for future strain engineering and process development work.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 6","pages":"Pages 550-558"},"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)80005-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91647858","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: 61

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

Yuko Shinohara , Hiroo Uchiyama , Osami Yagi , Isao Kusakabe

{"title":"Purification and characterization of component B of a soluble methane monooxygenase from Methylocystis sp. M","authors":"Yuko Shinohara , Hiroo Uchiyama , Osami Yagi , Isao Kusakabe","doi":"10.1016/S0922-338X(97)80350-9","DOIUrl":"https://doi.org/10.1016/S0922-338X(97)80350-9","url":null,"abstract":"<div>Soluble methane monooxygenase (sMMO: EC 1.14.13.25) from Methylocystis sp. M is a multicomponent enzyme consisting of a hydroxylase, a reductase, and component B. The hydroxylase and the reductase have been purified and characterized (Nakajima, Uchiyama, Yagi, and Nakahara, 1992). We describe a purification protocol for the uncharacterized component B. Component B has a molecular mass of approximately 32,000, consisting of 2 subunits, each with a molecular mass of 15,100. It contains neither metals nor prosthetic groups. The protein was gradually truncated from the N-terminal end and lost 30 amino acid residues, forming components B′ or B″ with molecular masses of 11,100 and 10,500, respectively. At the truncation site, the secondary structure of component B changed from α-helix to β-sheet. Component B appeared to have a higher affinity for the hydroxylase than the reductase. It also increased the heat stability of the hydroxylase and retarded separation of iron from the active center of the hydroxylase. From these results, it is suggested that the role of component B in the sMMO system is the stabilization of the hydroxylase structure rather than electron transfer from reductase to hydroxylase.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 1","pages":"Pages 37-42"},"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)80350-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91704876","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: 14

Characterization of the ATF1 and Lg-ATF1 genes encoding alcohol acetyltransferases in the bottom fermenting yeast Saccharomyces pastorianus 底发酵酵母醇乙酰转移酶ATF1和Lg-ATF1基因的研究

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80027-5

Hiroyuki Yoshimoto , Daisuke Fujiwara , Takayuki Momma , Chiori Ito , Hidetaka Sone , Yoshinobu Kaneko , Yukio Tamai

{"title":"Characterization of the ATF1 and Lg-ATF1 genes encoding alcohol acetyltransferases in the bottom fermenting yeast Saccharomyces pastorianus","authors":"Hiroyuki Yoshimoto , Daisuke Fujiwara , Takayuki Momma , Chiori Ito , Hidetaka Sone , Yoshinobu Kaneko , Yukio Tamai","doi":"10.1016/S0922-338X(98)80027-5","DOIUrl":"10.1016/S0922-338X(98)80027-5","url":null,"abstract":"<div>The bottom fermenting yeast Saccharomyces pastorianus (formerly Saccharomyces carlsbergensis) has one ATF1 gene and a homologous gene called Lg-ATF1 which encode alcohol acetyltransferases. Southern blot analysis of chromosomes separated by pulsed-field gel electrophoresis in a variety of bottom fermenting yeasts showed that in most of the yeasts analyzed, the ATF1 gene is located on the 1000- and 1050-kb chromosomes or only on the 1050-kb chromosome, while the Lg-ATF1 gene is located on the 850-kb chromosome. Acetate ester synthesis in a bottom fermenting yeast was found to be reduced by aeration or the addition of an unsaturated fatty acid. The enzyme activities involved in the synthesis of acetate esters decreased under these conditions. Experiments using ATF-lacZ fusion genes showed that the transcription of the ATF1 and Lg-ATF1 genes is co-regulated and is repressed by aeration or the addition of an unsaturated fatty acid. These findings suggest that the reduction in acetate ester synthesis observed in the bottom fermenting yeast was due to a reduction in enzyme synthesis resulting from transcriptional repression of the ATF1 and Lg-ATF1 genes.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 1","pages":"Pages 15-20"},"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)80027-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84678257","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: 67

Screening and fermentation of endo-α-N-acetylgalactosaminidase S, a mucin-hydrolyzing enzyme from Streptomyces acting on the GalNAc-O-Ser (Thr) linkage 链霉菌中作用于GalNAc-O-Ser (Thr)键的黏液水解酶内切-α- n-乙酰半乳糖氨基酶S的筛选和发酵

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80081-0

Yoshitake Tanaka , Yoko Takahashi , Mayumi Shinose , Satoshi Ōmura , Ikuko I. -Karakasa , Hitoo Iwase , Kyoko Hotta

{"title":"Screening and fermentation of endo-α-N-acetylgalactosaminidase S, a mucin-hydrolyzing enzyme from Streptomyces acting on the GalNAc-O-Ser (Thr) linkage","authors":"Yoshitake Tanaka , Yoko Takahashi , Mayumi Shinose , Satoshi Ōmura , Ikuko I. -Karakasa , Hitoo Iwase , Kyoko Hotta","doi":"10.1016/S0922-338X(98)80081-0","DOIUrl":"10.1016/S0922-338X(98)80081-0","url":null,"abstract":"<div>Soil microorganisms were examined for their ability to grow on porcine gastric mucin as a sole source of carbon and energy. Streptomyces sp. OH-11242 thus selected was found to produce endo-α-N-acetylgalactosaminidase (endo-GalNAc-ase S), together with several mucin-degrading glycosidases. Endo-GalNAc-ase S is a new enzyme capable of hydrolyzing the innermost GalNAc-O-Ser (Thr) linkage of the mucin molecule. Studies on the fermentation conditions necessary for its production revealed that the enzyme was induced by mucin but the induction was inhibited by glucose and other easily assimilable carbon sources, as well as by complex nitrogen sources. Addition of palmitate, λ-carrageenan, or crude mucin to a mucin-based production medium enhanced enzyme production and mycelial growth. When the initial mucin concentration of the production medium was increased, the maximum titer of endo-GalNAc-ase S produced in the culture both also increased, while the cultivation time giving the peak enzyme titer was prolonged. As a result of the studies, increased and reproducible production of endo-GalNAc-ase S was achieved, reaching 42 units/ml in a 100-ml culture and 31 units/ml in an 800-ml culture with 2 and 1.5% purified mucin, respectively, as the major carbon source.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 4","pages":"Pages 381-387"},"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)80081-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87310278","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: 8

Permeability barrier of the yeast plasma membrane induced by ethanol 乙醇诱导酵母质膜的通透性屏障

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)80348-0

H. Mizoguchi, S. Hara

引用次数: 24

Exogenous gene transfection into quail embryo using cationic lipid vesicles 利用阳离子脂质囊转染外源基因到鹌鹑胚胎

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80043-3

Satoshi Oguchi, Masamichi Kamihira, Jun You, Ayuko Tachibana, Shinji Iijima

{"title":"Exogenous gene transfection into quail embryo using cationic lipid vesicles","authors":"Satoshi Oguchi, Masamichi Kamihira, Jun You, Ayuko Tachibana, Shinji Iijima","doi":"10.1016/S0922-338X(98)80043-3","DOIUrl":"10.1016/S0922-338X(98)80043-3","url":null,"abstract":"<div>We have previously reported a simple procedure for gene transfection mediated by cationic lipid vesicles for animal cells, in which a commercially available synthetic cationic surfactant, dimethyldioctadecyl ammonium bromide (DDAB), was used for making lipid vesicles. The transfection method was associated with low cytotoxicity and high transfection efficiency. In the present study, the method was applied for gene transfection into quail embryos. The complex solution of lipid vesicles and pmiwZ plasmid, a β-galactosidase expression vector under the control of β-actin promoter as a reporter, was injected into quail embryos at various developmental stages using a glass micropipette. After incubation at 37.7°C for 3–4 d, the embryos were fixed and stained with X-gal solution. Under optimal conditions, about 80% of quail embryos expressed β-galactosidase in limited regions of tissues and organs with high viability. Moreover, 35% of the treated embryos (<math><mtext>15</mtext><mtext>43</mtext></math>) hatched following in vitro embryo culture, using the method developed by us.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 1","pages":"Pages 118-120"},"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)80043-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89229857","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

A comparative study of mannitol production by two lactic acid bacteria 两种乳酸菌生产甘露醇的比较研究

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(97)86768-2

Jong Won Yun, Dong Hyun Kim

{"title":"A comparative study of mannitol production by two lactic acid bacteria","authors":"Jong Won Yun, Dong Hyun Kim","doi":"10.1016/S0922-338X(97)86768-2","DOIUrl":"10.1016/S0922-338X(97)86768-2","url":null,"abstract":"<div>Two different lactic acid bacteria, designated Lactobacillus sp. Y-107 and Leuconostoc sp. Y-002, were isolated during the fermentation of kimchi, a Korean fermented food product, and found to possess the capability of mannitol production. To optimize the culture conditions and compare the mannitol formation characteristics of the two strains, various fermentation conditions were investigated. Of several sugars tested, only fructose and sucrose were utilized as substrates for mannitol formation. With both strains, maximal mannitol production was obtained with fructose as the sole carbon source. Under the optimal culture conditions, the final mannitol concentrations produced by the Lactobacillus and Leuconostoc strains were 73 and 26 g/l from 100 g/l fructose with indicated yields of 86 and 65% based on the fructose consumed, respectively. Neither isolate produced other polyols such as glycerol and sorbitol as by-products. The two organisms exhibited very similar physiological behavior in mannitol biosynthesis apart from their metabolism of some sugars.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"85 2","pages":"Pages 203-208"},"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)86768-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89272295","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: 47

Bioconversion of indene to cis (1S,2R) indandiol and trans (1R,2R) indandiol by Rhodococcus species 红球菌将茚二醇转化为顺式(1S,2R)茚二醇和反式(1R,2R)茚二醇

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(99)80005-1

M. Chartrain, Barbara A. Jackey, C. Taylor, V. Sandford, K. Gbewonyo, Leonard Lister, Lisa Dimichele, C. Hirsch, B. Heimbuch, C. Maxwell, D. Pascoe, B. Buckland, R. Greasham

引用次数: 61

Effects of bacitracin and excess Mg2+ on submerged mycelial growth of Streptomyces azureus 杆菌肽和过量Mg2+对蓝色链霉菌水中菌丝生长的影响

Journal of Fermentation and Bioengineering Pub Date : 1998-01-01 DOI: 10.1016/S0922-338X(98)80029-9

Adel K. Okba, Takahiro Ogata, Hitoshi Matsubara, Shorin Matsuo, Katsumi Doi, Seiya Ogata

{"title":"Effects of bacitracin and excess Mg2+ on submerged mycelial growth of Streptomyces azureus","authors":"Adel K. Okba, Takahiro Ogata, Hitoshi Matsubara, Shorin Matsuo, Katsumi Doi, Seiya Ogata","doi":"10.1016/S0922-338X(98)80029-9","DOIUrl":"10.1016/S0922-338X(98)80029-9","url":null,"abstract":"<div>Effects of bacitracin (BC) and excess Mg2+ on pellet formation and mycelial growth of Streptomyces azureus were studied in a liquid culture using Bennett medium. The addition of Mg2+ at concentrations above 0.2 mM to the medium resulted in the promotion of pellet formation, a distinct inhibition of growth and decrease in cell mass. BC changed the growth type of mycelia from the compact pellet-type to the dispersed-type, and stimulated mycelial growth after a long lag period, accompanied by an increase in cell mass. In the presence of less than 0.2 mM Mg2+, BC completely inhibited mycelial growth. Ca2+ showed an effect similar to Mg2+. EDTA inhibited pellet formation, but never stimulated growth. Furthermore, EDTA suppressed the growth inhibitory and stimulatory actions of BC. From these results, we speculated that: (i) excess Mg2+ induced pellet formation; (ii) BC, similar to EDTA chelated with excess Mg2+ in the medium, leading to the inhibition of pellet formation; and (iii) BC-induced stimulation of growth might be due to its chelating and antimicrobial activities. It was also said that the growth inhibitory action of BC on S. azureus was antagonized by excess Mg2+ or Ca2+ and EDTA.</div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 1","pages":"Pages 28-33"},"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)80029-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82707876","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: 17