Invertase from baker's yeast (Saccharomyces cerevisiae) was covalently bound via glutaraldehyde to a macroporous polystyrene anion-exchanger, silica, and porous glass. The thermal stability of the enzyme-matrix complexes was found to be higher than that of soluble invertase, increasing in the order given above. The immobilization of invertase to the polystyrene anion-exchanger by benzoquinonen and trichlorotriazine provided enzyme derivatives with lower thermal stability compared to the soluble enzyme. The thermal inactivation of all invertase-matrix complexes is characterized by a biphasic course. The inactivation process is well described by a model of ULBRICH and SCHELLENBERGER [1] which is based on the assumption of two differently stable enzyme fractions each of which being inactivated by a first-order reaction. This model proved to be appropriate also for the description of the thermal inactivation in the presence of substrate.
{"title":"Untersuchungen zur Thermostabilität immobilisierter Invertase","authors":"J. Mansfeld, A. Schellenberger","doi":"10.1002/ABIO.370060137","DOIUrl":"https://doi.org/10.1002/ABIO.370060137","url":null,"abstract":"Invertase from baker's yeast (Saccharomyces cerevisiae) was covalently bound via glutaraldehyde to a macroporous polystyrene anion-exchanger, silica, and porous glass. The thermal stability of the enzyme-matrix complexes was found to be higher than that of soluble invertase, increasing in the order given above. \u0000 \u0000 \u0000 \u0000The immobilization of invertase to the polystyrene anion-exchanger by benzoquinonen and trichlorotriazine provided enzyme derivatives with lower thermal stability compared to the soluble enzyme. \u0000 \u0000 \u0000 \u0000The thermal inactivation of all invertase-matrix complexes is characterized by a biphasic course. The inactivation process is well described by a model of ULBRICH and SCHELLENBERGER [1] which is based on the assumption of two differently stable enzyme fractions each of which being inactivated by a first-order reaction. This model proved to be appropriate also for the description of the thermal inactivation in the presence of substrate.","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"25 1","pages":"89-99"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87979395","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 simple medium enhancing the production of thiaminase I (EC 2.5. 1.2) by Bacillus thiaminolyticus was developed. Ca 2+ stimulated the enzyme production. The activity of extracellular thiaminase I ranged between 1.29 and 1.33 U/ml medium
{"title":"Production of thiaminase I for analytical purposes","authors":"T. Ruml, L. Šilhánková","doi":"10.1002/ABIO.370150115","DOIUrl":"https://doi.org/10.1002/ABIO.370150115","url":null,"abstract":"A simple medium enhancing the production of thiaminase I (EC 2.5. 1.2) by Bacillus thiaminolyticus was developed. Ca 2+ stimulated the enzyme production. The activity of extracellular thiaminase I ranged between 1.29 and 1.33 U/ml medium","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"90 1","pages":"117-121"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83924330","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}
Genomic RNA of the Respiratory syntical virus (RS-virus) was used as a template to synthesize calfthymus DNA-primed cDNAs. These cDNAs were subsequently cloned into the E. coli plasmid pBR 322 at the PstI-site. By hybridization 6 recombinants with virusspecific cDNAs representing 10% of the whole genome could be isolated.
{"title":"Klonierung von RSV‐cDNS (Respiratiorisches Syncytial Virus) und erste Charakterisierung der Rekombinanten","authors":"S. Prösch, W. Seidel, L. Döhner, D. Liebscher","doi":"10.1002/ABIO.370060107","DOIUrl":"https://doi.org/10.1002/ABIO.370060107","url":null,"abstract":"Genomic RNA of the Respiratory syntical virus (RS-virus) was used as a template to synthesize calfthymus DNA-primed cDNAs. These cDNAs were subsequently cloned into the E. coli plasmid pBR 322 at the PstI-site. By hybridization 6 recombinants with virusspecific cDNAs representing 10% of the whole genome could be isolated.","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"35 1","pages":"10-13"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83131834","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}
T. Bhalla, M. Aoshima, S. Misawa, R. Muramatsu, K. Furuhashi
The nitrilase of Rhodococcus rhodochrous PA-34 catalyzes the production of optically active amino acids from aminonitriles. The amino acid sequence of the NH 2 terminus of the purified nitrilase was determined for the preparation of a synthetic oligonucleotide as a southern hybridization probe. A 9.5-kbp Pst I-fragment, which hybridized with the oligonucleotide probe, was isolated from R. rhodochrous PA-34 genomic libraries constructed in pUC 19. Nucleotide sequence analysis revealed that the nitrilase gene codes for a putative polypeptide of 380 amino acids which correspond to a relative molecular weight of 41,723.
{"title":"The molecular cloning and sequencing of the nitrilase gene of Rhodococcus rhodochrous PA‐34","authors":"T. Bhalla, M. Aoshima, S. Misawa, R. Muramatsu, K. Furuhashi","doi":"10.1002/ABIO.370150308","DOIUrl":"https://doi.org/10.1002/ABIO.370150308","url":null,"abstract":"The nitrilase of Rhodococcus rhodochrous PA-34 catalyzes the production of optically active amino acids from aminonitriles. The amino acid sequence of the NH 2 terminus of the purified nitrilase was determined for the preparation of a synthetic oligonucleotide as a southern hybridization probe. A 9.5-kbp Pst I-fragment, which hybridized with the oligonucleotide probe, was isolated from R. rhodochrous PA-34 genomic libraries constructed in pUC 19. Nucleotide sequence analysis revealed that the nitrilase gene codes for a putative polypeptide of 380 amino acids which correspond to a relative molecular weight of 41,723.","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"7 1","pages":"297-306"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83512866","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":"Grenzwerte. Kennzahlen zur Umweltbelastung in Deutschland und in der EG. Landsberg: ecomed‐Verlag GmbH & Co., KG 254 Seiten, DM 98,– (Fortsetzungspreis) DM 178,– (Einzelpreis ohne Abonement der Aktualisierungen). ISBN: 3‐609‐75700‐0","authors":"G. Klappach","doi":"10.1002/ABIO.370150204","DOIUrl":"https://doi.org/10.1002/ABIO.370150204","url":null,"abstract":"","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"97 1","pages":"160-160"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89452973","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 determination of oxygen diffusion coefficients was carried out by a modified chronoamperometric method using a stationary platinum electrode. The determined diffusion coefficients are related to approximated η0-values. It was shown a relation of Di and η0 according to the HAYDUK-CHENG-potential equation. That means a strong relative lowering of oxygen diffusion coefficients already by low viscosities, but a little influence at high viscosities. A simple laboratory thin film reactor is described, in which the oxygen supply is maintained by diffusion. This reactor is suitable very well for fermentations of viscous fluids.
{"title":"Untersuchungen zur Sauerstoffdiffusion in wäßrigen Xanthanlösungen","authors":"U. Stottmeister","doi":"10.1002/ABIO.370060133","DOIUrl":"https://doi.org/10.1002/ABIO.370060133","url":null,"abstract":"The determination of oxygen diffusion coefficients was carried out by a modified chronoamperometric method using a stationary platinum electrode. \u0000 \u0000 \u0000 \u0000The determined diffusion coefficients are related to approximated η0-values. \u0000 \u0000 \u0000 \u0000It was shown a relation of Di and η0 according to the HAYDUK-CHENG-potential equation. \u0000 \u0000 \u0000 \u0000That means a strong relative lowering of oxygen diffusion coefficients already by low viscosities, but a little influence at high viscosities. \u0000 \u0000 \u0000 \u0000A simple laboratory thin film reactor is described, in which the oxygen supply is maintained by diffusion. This reactor is suitable very well for fermentations of viscous fluids.","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"22 1","pages":"69-75"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73079473","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":"Vektoren für den Gentransfer in Säugersystemen","authors":"M. Strauss, U. Kiessling, M. Platzer","doi":"10.1002/ABIO.370060121","DOIUrl":"https://doi.org/10.1002/ABIO.370060121","url":null,"abstract":"","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"63 1","pages":"38-39"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75892970","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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