Biochemical educationPub Date : 2000-01-01Epub Date: 2000-03-13DOI: 10.1016/S0307-4412(99)00102-8
Pedro Chimoy Effio, Enny Fernandes Silva, Manuel Troyano Pueyo
{"title":"A simple and rapid method for screening amylolytic bacteria","authors":"Pedro Chimoy Effio, Enny Fernandes Silva, Manuel Troyano Pueyo","doi":"10.1016/S0307-4412(99)00102-8","DOIUrl":"https://doi.org/10.1016/S0307-4412(99)00102-8","url":null,"abstract":"<div><p>A laboratory class was designed for the study of the ecology of amylolytic bacteria in soil, although other sources may be equally suitable for this purpose. Groups of three students carried out the following: (a) preparation and sterilization of medium and plates, (b) collection and preparation of soil samples, spreading the samples on the plates, (c) incubation of the plates at 37°C overnight, a further 1 h incubation at 60°C to observe amylolytic activity due to thermophilic bacteria, and (d) interpretation and discussion of the results. These tasks are accomplished in two periods of 4<!--> <!-->h on consecutive days. No sophisticated instruments are required for these experiments, which can be carried out in three classes of 4<!--> <!-->h each. On the first day the students prepare culture media, buffers and reagents, as well as collect and grow soil samples. The second day is spent for both taxonomic identification of colonies and the HAI determination.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"Pages 47-49"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00102-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137389666","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":"Calculating apparent equilibrium constants of enzyme-catalyzed reactions at pH 7.","authors":"Alberty","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Apparent equilibrium constants K' of biochemical reactions at pH 7 and standard apparent reduction potentials of half reactions at pH 7 can be calculated using a table of standard transformed Gibbs energies of formation Delta(f)G'(0) at pH 7. A table is provided for 136 reactants at 25 degrees C, pH 7, and ionic strengths of 0, 0.10, and 0.25 M. Examples are given to illustrate the use of the table.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"12-17"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21570537","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":"alpha-Amylase production by solid state fermentation: a new practical approach to biotechnology courses.","authors":"Mulimani, Patil Ramalingam GN","doi":"10.1111/j.1539-3429.2000.tb00056.x","DOIUrl":"https://doi.org/10.1111/j.1539-3429.2000.tb00056.x","url":null,"abstract":"A laboratory practical experiment in Biotechnology involving the investigation of alpha-amylase production by solid state fermentation of Gibberella fujikuroi is described.","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 3 1","pages":"161-163"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1539-3429.2000.tb00056.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"63147733","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}
Biochemical educationPub Date : 2000-01-01Epub Date: 2000-03-13DOI: 10.1016/S0307-4412(99)00123-5
F. Vella, Leopoldo de Meis, Alan H. Mehler, Wilfried Rombauts, Harold B. White III, E.J. Wood
{"title":"Standards for the Ph.D. Degree in the Molecular Biosciences","authors":"F. Vella, Leopoldo de Meis, Alan H. Mehler, Wilfried Rombauts, Harold B. White III, E.J. Wood","doi":"10.1016/S0307-4412(99)00123-5","DOIUrl":"10.1016/S0307-4412(99)00123-5","url":null,"abstract":"","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"Pages 2-11"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00123-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21570536","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":"Understanding ion transport by quantification of mitochondrial swelling.","authors":"Königsberg","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Suspensions of mitochondria are turbid and scatter light. An increase in the matrix volume (swelling) due to the influx of permeable solutes results in a decrease in the amount of light scattered. This property can be used to study solute fluxes across the mitochondrial inner membrane. A rapid method for isolating mitochondria is presented along with three swelling experiments using energized and non-energized mitochondria to illustrate ion transport across energy transducing membranes.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"24-26"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21569895","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":"beta-Galactosidase immobilization for milk lactose hydrolysis: a simple experimental and modelling study of batch and continuous reactors.","authors":"Obón, Castellar, Iborra, Manjón","doi":"10.1111/j.1539-3429.2000.tb00057.x","DOIUrl":"https://doi.org/10.1111/j.1539-3429.2000.tb00057.x","url":null,"abstract":"The experiment described in this paper introduces students to the practical use of an enzyme (beta-galactosidase, or lactase) acting on a natural substrate. The enzyme is immobilized onto a cheap support, and the immobilized derivative is used in a packed-bed reactor for continuous milk lactose hydrolysis. The results are compared to those obtained for discontinuous batch reactors with soluble enzyme. A mathematical model of the two types of reactors is run, and its results are compared with the experimental data obtained.","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 3 1","pages":"164-168"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1539-3429.2000.tb00057.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"63147743","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":"Plant protoplast isolation - a practical approach.","authors":"Prasad, Naik","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A method for the isolation of plant protoplasts is presented that uses inexpensive sources of enzymes. It is suitable for student use in Biotechnology.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"39-40"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21569900","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":"Chemical cross-linking analysis of Ca(2+-)ATPase from rabbit skeletal muscle.","authors":"Murray, Ohlendieck","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A student laboratory experiment is described dealing with chemical cross-linking analysis of Ca(2+-)ATPase from rabbit muscle. The experiment introduces students to a wide range of techniques including subcellular fractionation, chemical cross-linking, polyacrylamide gel electrophoresis, blotting and immunochemical detection of proteins.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"41-46"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21569901","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}