{"title":"Production of raw cassava starch-digestive glucoamylase by Rhizopus sp. in liquid culture","authors":"Hiroshi Nishise , Akira Fuji, Makoto Ueno, Vitchuporn Vongsuvanlert, Yoshiki Tani","doi":"10.1016/0385-6380(88)90005-2","DOIUrl":"10.1016/0385-6380(88)90005-2","url":null,"abstract":"<div><p>Among about 200 <em>Rhizopus</em> strains isolated in Thailand, <em>Rhizopus</em> sp. MB46 was selected as a producer of raw cassava starch-digestive glucoamylase. Rice bran was effective for the enzyme production in a solid culture as well as wheat bran. Addition of turpentine oil into the rice bran solid culture increased the productivity. <em>Rhizopus</em> sp. MB46 was found to produce glucoamylase in a liquid culture containing 1% rice bran but not in one consisting of 10% raw cassava starch of 2% glucose. The productivity per 1 g solids in the medium in liquid culture was finally improved 6-times by utilization of <em>n</em>-hexane-treated rice bran, supplement of 0.1% meat extract and addition of gauze as a support. The activity was superior to that in turpentine oil-supplemented solid culture.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 4","pages":"Pages 397-402"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90005-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85973503","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":"Mirin-making at low alcohol concentration with Koji prepared with a new mutant of Aspergillus usamii","authors":"Haruo Oyashiki , Masahiro Uchida , Akira Obayashi , Satoru Oka","doi":"10.1016/0385-6380(88)90112-4","DOIUrl":"10.1016/0385-6380(88)90112-4","url":null,"abstract":"<div><p>We examined the productivity of <em>mirin</em>-making and the quality if the <em>mirin</em> produced using <em>koji</em> prepared with a new mutant (mutant CA) that originated from <em>Aspergillus usamii</em> mut. <em>shiro-usamii</em>. The <em>koji</em> prepared with the mutant CA contained a large amount of citric acid. Therefore, the concentration of the brewing alcohol added to prevent bacterial contamination of the mash was decreased to 6.0% from the 12.5% needed when the mash was made with <em>koji</em> of the conventional <em>Aspergillus oryzae</em>. A mash containing this low concentration of alcohol was incubated with <em>koji</em> of the mutant CA and enzyme preparations such as α-amylase (6,000 DU/kg mash) from <em>Bacillus subtilis</em> and acidic protease (1,000 PU/kg mash) from <em>Aspergillus niger</em>. The starch and protein in this mash was sufficiently digested. The yield of <em>mirin</em> obtained from this mash was high (96% based on the mash weight), and the resulting <em>mirin</em> contained much citric acid, malic acid, succinic acid, nitrogen compounds, isomaltose, isomaltotriose, and oligosaccarides. The taste of the <em>mirin</em> was refreshingly sour and flavorsome.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 3","pages":"Pages 333-339"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90112-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86729475","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":"Study on the instrumentation and control of the fermentation process","authors":"Akira Nanba","doi":"10.1016/0385-6380(88)90060-X","DOIUrl":"10.1016/0385-6380(88)90060-X","url":null,"abstract":"","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 2","pages":"Page 244"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90060-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79155880","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":"Purification of recombinant α-amylase with immuno-affinity chromatography using monoclonal antibody","authors":"Masamichi Kamihira, Masayuki Taniguchi , Shinji Iijima, Takeshi Kobayashi","doi":"10.1016/0385-6380(88)90066-0","DOIUrl":"10.1016/0385-6380(88)90066-0","url":null,"abstract":"<div><p>A monoclonal antibody against recombinant thermostable α-amylase produced by <em>Escherichia coli</em> was isolated from serum-free medium and immobilized on Sepharose 4B. The adsorption equilibrium between α-amylase and the immobilized immuno-adsorbent showed a Langmuir type isotherm. The breakthrough curve calculated numerically using the averaged volumetric coefficient coincided well with the experimental data. More than 90% of the activity of bound α-amylase could be recovered by eluting with glycine-HCl buffer (pH 2.5). The elution profile at pH 2.5 became sharper with increasing temperature. By using an immuno-affinity column, the recombinant α-amylase produced by <em>E. coli</em> could be purified homogeneously from crude extract enzyme solution with two-step elution.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 6","pages":"Pages 625-631"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90066-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78938469","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":"Production of l-Methionine-enriched cells of a mutant derived from a methylotrophic yeast, Candida boidinii","authors":"Wang-Jin Lim, Yoshiki Tani","doi":"10.1016/0385-6380(88)90068-4","DOIUrl":"10.1016/0385-6380(88)90068-4","url":null,"abstract":"<div><p><span>l</span>-Methionine-enriched cells production of an ethionine-resistant mutant of <em>Candida boidinii</em> no. 2201 was greatly improved by the control of pH and by feeding of methanol and other medium components during cultivation in a jar fermentor. Under the optimal conditions, 38.5 g (as dry weight)_of cells abd 282 mg of pool methionine (intracellular pool of free <span>l</span>-methionine) per <em>l</em> of culture broth were obtained after 11 d of cultivation.</p><p>The culture conditions for production of <span>l</span>-methionine-enriched cells in continuous culture were investigated. With limited methanol in continuous cultivation, pool methionine productivity reached a maximum value of 1.14 mg·<em>l</em><sup>−1</sup>·h<sup>−1</sup> at a dilution rate of 0.05·h<sup>−1</sup>. During methanol-limited growth in continuous cultivation, the pool methionine content of the mutant was about 20–35% higher than that in batch cultivation.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 6","pages":"Pages 643-647"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90068-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85568642","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":"Ethanol production from wheat flour by Zymomonas mobilis","authors":"E. Favela Torres, J. Baratti","doi":"10.1016/0385-6380(88)90043-X","DOIUrl":"10.1016/0385-6380(88)90043-X","url":null,"abstract":"<div><p>Starch from wheat flour was enzymatically hydrolyzed and used for ethanol production by <em>Zymmonas mobilis</em>. The addition of a nitrogen source like ammonium sulfate was sufficient to obtain a complete fermentation of the hdyrolyzed strach. In batch culture a glucose concentration as high as 223 g/<em>l</em> could be fermented (conversion 99.5%) to 105 g/<em>l</em> of ethanol in 70 h with an ethanol yield of 0.47 g/g (92% of theoretical). In continuous culture the use of a flocculent strain and a fermentor with an internal settler resulted (D=1,4 h<sup>−1</sup>) in a high ethanol productivity of 70.7 g/<em>l</em>·h with: ethanol concentration 49.5 g/<em>l</em>, ethanol yield 0.50 g/g (98% of theoretical and substrate conversion 99%.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 2","pages":"Pages 167-172"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90043-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75861855","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":"Purification and properties of glutaminase from Aspergillus oryzae","authors":"Toshihiro Yano, Masae Ito, Kenji Tomita, Hidehiko Kumagai","doi":"10.1016/0385-6380(88)90039-8","DOIUrl":"10.1016/0385-6380(88)90039-8","url":null,"abstract":"<div><p>Glutaminase activity was found in a water extract of a wheat bran <em>koji</em> (extracellular fraction) of <em>Aspergillus oryzae</em> strains Lee-1, H-16 and MA-27-IM isolated from a commercial <em>koji</em> ssed for soy sauce fermentation, as well as in thier mycelia (intracellular fraction). Both the intracellular and the extracellular glutaminases were purified from strain MA-27-IM. Polyacrylamide gel electrophoresis of each purified preparation gave a single band with identical electrophoretic mobility. The molecular weight of the intracellular and the extracellular glutaminases were estimated to be approximately 113, 000. Both preparations hydrolyzed various γ-glutamyl compounds besides <span>l</span>-glutamine but did not exhibit asparaginase activity. Further investigation of these preparations inidicated that these glutaminases possessed almost the same properties, suggesting their similarity.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 2","pages":"Pages 137-143"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90039-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73213166","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":"Fermentation of lactose by Zymomonas mobilis carrying a Lac+ recombinant plasmid","authors":"Hideshi Yanase, Junn Kurii, Kenzo Tonomura","doi":"10.1016/0385-6380(88)90007-6","DOIUrl":"10.1016/0385-6380(88)90007-6","url":null,"abstract":"<div><p>Lac<sup>+</sup> recombinant plasmids encoding a β-galactosidase fused protein and lactose permease of <em>Escherichia coli</em> were introduced <em>Zymomonas mobilis</em>. The fused protein was expressed with 450 to 5,860 Miller units of β-galactosidase activity, and functioned as lactase. Raffinose uptake by <em>Z. mobilis</em> CP4 was enhanced in the plasmid-carrying strain over the plasmid-free strain, suggesting that the lactose permease was functioning in the organism. <em>Z. mobilis</em> carrying the plasmid could produce ethanol from lactose and whey, but could not grow on lactose as the sole carbon source. It was found that the growth of the organism was inhibited by either galactose of the galactose liberated from lactose.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 4","pages":"Pages 409-415"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90007-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75212822","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}