Zeitschriftenartikel zum Thema „Savinase“
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Voisine, R., F. Côté, J. Verreault und A. Porter. „Protein Transfer in Mainstream and Sidestream Cigarette Smoke“. Beiträge zur Tabakforschung International/Contributions to Tobacco Research 21, Nr. 1 (01.03.2004): 9–14. http://dx.doi.org/10.2478/cttr-2013-0766.
Smith, E. M., L. E. Green, D. Mason, T. S. Gunasekera und D. A. Veal. „Savinase Is a Bactericidal Enzyme“. Applied and Environmental Microbiology 69, Nr. 1 (01.01.2003): 719–21. http://dx.doi.org/10.1128/aem.69.1.719-721.2003.
Pedersen, Jan T., Ole H. Olsen, Christian Betzel, Susanne Eschenburg, Sven Branner und Sven Hastrup. „Cavity Mutants of Savinase™“. Journal of Molecular Biology 242, Nr. 3 (September 1994): 193–202. http://dx.doi.org/10.1006/jmbi.1994.1572.
Wu, Shanshan, Tam T. T. N. Nguyen, Olga V. Moroz, Johan P. Turkenburg, Jens E. Nielsen, Keith S. Wilson, Kasper D. Rand und Kaare Teilum. „Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis“. PeerJ 8 (26.06.2020): e9408. http://dx.doi.org/10.7717/peerj.9408.
van Wassenaar, Pieter D. „Substrate specificity of savinase toward β-casein“. Journal of Protein Chemistry 11, Nr. 4 (August 1992): 370. http://dx.doi.org/10.1007/bf01673725.
Kukhtyn, Mykola, Khrystyna Kravcheniuk, Ludmila Beyko, Yulia Horiuk, Oleksandr Skliar und Serhii Kernychnyi. „STUDY OF THE INFLUENCE OF SAVINASE®EVITY16L ENZYME ON BIOFILMS FORMATION OF STAPHYLOCOCCUS AUREUS ON STAINLESS STEEL WITH DIFFERENT ROUGHNESS“. EUREKA: Life Sciences 2 (31.03.2019): 26–32. http://dx.doi.org/10.21303/2504-5695.2019.00858.
N., Wafaa, H. A. Elbarbary, E. M. A. Ibrahim, H. A. Mohamed und H. Jenssen. „EFFECT OF ENZYME TYPE AND HYDROLYSIS TIME ON ANTIBACTERIAL AND ANTIOXIDANT ACTIVITY OF WHEY PROTEIN HYDROLYSATES“. IRAQI JOURNAL OF AGRICULTURAL SCIENCES 53, Nr. 6 (29.12.2022): 1340–57. http://dx.doi.org/10.36103/ijas.v53i6.1650.
Pfeuti, Osborne, Shoveller, Ignatz und Bureau. „Development of a Novel Enzymatic Pretreatment for Improving the Digestibility of Protein in Feather Meal“. AgriEngineering 1, Nr. 4 (07.10.2019): 475–84. http://dx.doi.org/10.3390/agriengineering1040034.
Lin, Hai Tao, Fang Jiang, Hui Su und Jiwei Huang. „Study on Cashmere Fibers Shrink-Proofing by Enzyme Based on Fuzz Mathematics Method“. Advanced Materials Research 236-238 (Mai 2011): 2830–35. http://dx.doi.org/10.4028/www.scientific.net/amr.236-238.2830.
Vinther, Anders, Jørgen Petersen und Henrik Søeberg. „Capillary electrophoretic determination of the protease Savinase in cultivation broth“. Journal of Chromatography A 608, Nr. 1-2 (September 1992): 205–10. http://dx.doi.org/10.1016/0021-9673(92)87125-r.
Lange, Gudrun, Christian Betzel, Sven Branner und Keith S. Wilson. „Crystallographic Studies of Savinase, a Subtilisin-like Proteinase, at pH 10.5“. European Journal of Biochemistry 224, Nr. 2 (September 1994): 507–18. http://dx.doi.org/10.1111/j.1432-1033.1994.00507.x.
Gron, Hanne, Lene M. Bech und Klaus Breddam. „A Salt Dependent Increase in the Catalytic Activity of the Subtilisin Savinase“. Protein & Peptide Letters 1, Nr. 2 (September 1994): 106–13. http://dx.doi.org/10.2174/0929866501666220424134356.
Devita, Liza, Hanifah Nuryani Lioe, Mala Nurilmala und Maggy T. Suhartono. „The Bioactivity Prediction of Peptides from Tuna Skin Collagen Using Integrated Method Combining In Vitro and In Silico“. Foods 10, Nr. 11 (09.11.2021): 2739. http://dx.doi.org/10.3390/foods10112739.
Imai, S. „The effect of the proteolytic enzyme savinase on human plantar skin in vitro“. Archives of Dermatological Research 283, Nr. 6 (September 1991): 377–81. http://dx.doi.org/10.1007/bf00371819.
Remerowski, M. Lyndsay, Henri A. M. Pepermans, Cornelis W. Hilbers und Frank J. M. Ven. „Backbone Dynamics of the 269-residue Protease Savinase Determined from 15N-NMR Relaxation Measurements“. European Journal of Biochemistry 235, Nr. 3 (Februar 1996): 629–40. http://dx.doi.org/10.1111/j.1432-1033.1996.00629.x.
Nasiripourdori, Adak, Hossein Naderi-Manesh, Bijan Ranjbar und Khosro Khajeh. „Co-solvent effects on structure and function properties of savinase: Solvent-induced thermal stabilization“. International Journal of Biological Macromolecules 44, Nr. 4 (Mai 2009): 311–15. http://dx.doi.org/10.1016/j.ijbiomac.2008.09.018.
Christiansen, Torben, Søren Michaelsen, Mogens Wümpelmann und Jens Nielsen. „Production of savinase and population viability ofBacillus clausiiduring high-cell-density fed-batch cultivations“. Biotechnology and Bioengineering 83, Nr. 3 (28.05.2003): 344–52. http://dx.doi.org/10.1002/bit.10675.
Frankaer, Christian G., Olga V. Moroz, Johan P. Turkenburg, Stein I. Aspmo, Majbritt Thymark, Esben P. Friis, Kenny Stahl, Jens E. Nielsen, Keith S. Wilson und Pernille Harris. „Analysis of an industrial production suspension ofBacillus lentussubtilisin crystals by powder diffraction: a powerful quality-control tool“. Acta Crystallographica Section D Biological Crystallography 70, Nr. 4 (21.03.2014): 1115–23. http://dx.doi.org/10.1107/s1399004714001497.
Andrea, Torres, Ferrándiz Marcela, Capablanca Lucía, Franco Esther, Mira Elena und Moldovan Simona. „Microencapsulation of Lipase and Savinase Enzymes by Spray Drying Using Arabic Gum as Wall Material“. Journal of Encapsulation and Adsorption Sciences 06, Nr. 04 (2016): 161–73. http://dx.doi.org/10.4236/jeas.2016.64012.
Wang, Ping, Qiang Wang, Li Cui, Xuerong Fan, Jiugang Yuan und Murong Gao. „A comparative evaluation of the action of savinase and papain to the cutinase-pretreated wool“. Fibers and Polymers 11, Nr. 4 (Juli 2010): 586–92. http://dx.doi.org/10.1007/s12221-010-0586-9.
Betzel, Christian, Silke Klupsch, Gerlind Papendorf, Sven Hastrup, Sven Branner und Keith S. Wilson. „Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution“. Journal of Molecular Biology 223, Nr. 2 (Januar 1992): 427–45. http://dx.doi.org/10.1016/0022-2836(92)90662-4.
Bautista-Expósito, Sara, Elena Peñas, Montserrat Dueñas, José Manuel Silván, Juana Frias und Cristina Martínez-Villaluenga. „Individual contributions of Savinase and Lactobacillus plantarum to lentil functionalization during alkaline pH-controlled fermentation“. Food Chemistry 257 (August 2018): 341–49. http://dx.doi.org/10.1016/j.foodchem.2018.03.044.
Georgieva, Dessislava Nikolova, Peter Nikolov, Veneta Ivanova, Adriana Gusterova und Christian Betzel. „Fluorescence properties of Savinase®: the X-ray structure in the region of the tryptophyl residues“. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 55, Nr. 11 (September 1999): 2309–19. http://dx.doi.org/10.1016/s1386-1425(99)00098-0.
Arlian, L. G., D. L. Vyszenski-Moher, J. A. Merski, H. L. Ritz, T. L. Nusair und E. R. Wilson. „Antigenic and Allergenic Characterization of the Enzymes Alcalase and Savinase by Crossed Immunoelectrophoresis and Crossed Radioimmunoelectrophoresis“. International Archives of Allergy and Immunology 91, Nr. 3 (1990): 278–84. http://dx.doi.org/10.1159/000235128.
Maste, Marc C. L., Willem Norde und Antonie J. W. G. Visser. „Adsorption-Induced Conformational Changes in the Serine Proteinase Savinase: A Tryptophan Fluorescence and Circular Dichroism Study“. Journal of Colloid and Interface Science 196, Nr. 2 (Dezember 1997): 224–30. http://dx.doi.org/10.1006/jcis.1997.5205.
Bekiroglu, Hatice, Gorkem Ozulku und Osman Sagdic. „Effects of Casein Hydrolysate Prepared with Savinase on the Quality of Bread Made by Frozen Dough“. Foods 12, Nr. 20 (20.10.2023): 3845. http://dx.doi.org/10.3390/foods12203845.
Lipin´ska‐Ojrzanowska, Agnieszka, Dominika S>´wierczyn´ska‐Machura, Diana Tymoszuk, Ewa Nowakowska‐S´wirta und Jolanta Walusiak‐Skorupa. „Occupational Asthma in Female Factory Worker Resulting from Exposure to Savinase in Dishwashing Tablets—A Case Study“. Journal of Occupational Health 55, Nr. 4 (Juli 2013): 318–21. http://dx.doi.org/10.1539/joh.12-0169-cs.
Tekle, Sefik, Gorkem Ozulku, Hatice Bekiroglu und Osman Sagdic. „Effects of Fish Skin Gelatin Hydrolysates Treated with Alcalase and Savinase on Frozen Dough and Bread Quality“. Foods 13, Nr. 1 (30.12.2023): 139. http://dx.doi.org/10.3390/foods13010139.
Georgieva, Dessislava, Nicolay Genov, Wolfgang Voelter und Christian Betzel. „Catalytic Efficiencies of Alkaline Proteinases from Microorganisms“. Zeitschrift für Naturforschung C 61, Nr. 5-6 (01.06.2006): 445–52. http://dx.doi.org/10.1515/znc-2006-5-623.
Garcia-Mora, Patricia, Elena Peñas, Juana Frias und Cristina Martínez-Villaluenga. „Savinase, the Most Suitable Enzyme for Releasing Peptides from Lentil (Lens culinaris var. Castellana) Protein Concentrates with Multifunctional Properties“. Journal of Agricultural and Food Chemistry 62, Nr. 18 (28.04.2014): 4166–74. http://dx.doi.org/10.1021/jf500849u.
Bech, L. M., S. Branner, S. Hastrup und K. Breddam. „Introduction of a free cysteinyl residue at position 68 in the subtilisin Savinase, based on homology with proteinase K“. FEBS Letters 297, Nr. 1-2 (03.02.1992): 164–66. http://dx.doi.org/10.1016/0014-5793(92)80351-g.
González-Osuna, María Fernanda, Wilfrido Torres-Arreola, Enrique Márquez-Ríos, Francisco Javier Wong-Corral, Eugenia Lugo-Cervantes, José Carlos Rodríguez-Figueroa, Guillermina García-Sánchez et al. „Antioxidant Activity of Peptide Fractions from Chickpea Globulin Obtained by Pulsed Ultrasound Pretreatment“. Horticulturae 9, Nr. 4 (23.03.2023): 415. http://dx.doi.org/10.3390/horticulturae9040415.
Balashev, K., Tz Ivanova, K. Mircheva und I. Panaiotov. „Savinase proteolysis of insulin Langmuir monolayers studied by surface pressure and surface potential measurements accompanied by atomic force microscopy (AFM) imaging“. Journal of Colloid and Interface Science 360, Nr. 2 (August 2011): 654–61. http://dx.doi.org/10.1016/j.jcis.2011.04.101.
Sørensen, Margrethe, Arne Redsted Rasmussen und Kim Pilkjær Simonsen. „Enzymatic detection of formalin-fixed museum specimens for DNA analysis and enzymatic maceration of formalin-fixed specimens“. Collection Forum 30, Nr. 1-2 (01.01.2016): 1–6. http://dx.doi.org/10.14351/0831-4985-30.1.1.
Bautista-Expósito, Sara, Cristina Martínez-Villaluenga, Montserrat Dueñas, Jose Manuel Silván, Juana Frias und Elena Peñas. „Combination of pH-controlled fermentation in mild acidic conditions and enzymatic hydrolysis by Savinase to improve metabolic health-promoting properties of lentil“. Journal of Functional Foods 48 (September 2018): 9–18. http://dx.doi.org/10.1016/j.jff.2018.06.019.
Balashev, Konstantin, Thomas H. Callisen, Allan Svendsen und Thomas Bjørnholm. „Savinase action on bovine serum albumin (BSA) monolayers demonstrated with measurements at the air–water interface and liquid Atomic Force Microscopy (AFM) imaging“. Colloids and Surfaces B: Biointerfaces 88, Nr. 2 (Dezember 2011): 582–86. http://dx.doi.org/10.1016/j.colsurfb.2011.07.043.
Pedrosa, Nely de Almeida, Cristiano José de Andrade, José Carlos Cunha Petrus und Alcilene Rodrigues Monteiro. „Sequential Hydrolysis of Chicken Feathers Composed of Ultrasound and Enzymatic Steps: An Enhanced Protein Source with Bioactive Peptides“. Biomass 2, Nr. 4 (30.09.2022): 237–49. http://dx.doi.org/10.3390/biomass2040016.
Wang, Le, Jinbo Yao, Jiarong Niu, Jianyong Liu, Bo Li und Mao Feng. „Eco-Friendly and Highly Efficient Enzyme-Based Wool Shrinkproofing Finishing by Multiple Padding Techniques“. Polymers 10, Nr. 11 (31.10.2018): 1213. http://dx.doi.org/10.3390/polym10111213.
Micheelsen, Pernille Ollendorff, Jitka Vévodová, Leonardo De Maria, Peter Rahbek Østergaard, Esben Peter Friis, Keith Wilson und Michael Skjøt. „Structural and Mutational Analyses of the Interaction between the Barley α-Amylase/Subtilisin Inhibitor and the Subtilisin Savinase Reveal a Novel Mode of Inhibition“. Journal of Molecular Biology 380, Nr. 4 (Juli 2008): 681–90. http://dx.doi.org/10.1016/j.jmb.2008.05.034.
Georgieva, Dessislava Nikolova, Stanka Stoeva, Wolfgang Voelter, Nicolay Genov und Christian Betzel. „Differences in the Specificities of the Highly Alkalophilic Proteinases Savinase and Esperase Imposed by Changes in the Rigidity and Geometry of the Substrate Binding Sites“. Archives of Biochemistry and Biophysics 387, Nr. 2 (März 2001): 197–201. http://dx.doi.org/10.1006/abbi.2000.2249.
Jeon, Mi-Jin, und Yong-Woo Jeon. „Enhanced Enzymatic Degradability of Livestock Blood Pretreated with Ultrasonic Technique“. Applied Sciences 14, Nr. 4 (19.02.2024): 1676. http://dx.doi.org/10.3390/app14041676.
Christinawati, Evi Lusiana. „ANALISA FAKTOR – FAKTOR YANG MEMPENGARUHI TABUNGAN MASYARAKAT PADA BANK UMUM DENGAN PENDEKATAN MODEL ECM“. Jurnal Ekonomi Pembangunan 11, Nr. 1 (01.12.2013): 35. http://dx.doi.org/10.22219/jep.v11i1.3729.
Weiss, Jernej. „Klavirske skladbe Rista Savina“. Musicological Annual 48, Nr. 2 (01.12.2012): 217–27. http://dx.doi.org/10.4312/mz.48.2.217-227.
Neubauer, Henrik. „Baletna glasba Rista Savina“. Musicological Annual 48, Nr. 2 (01.12.2012): 165–85. http://dx.doi.org/10.4312/mz.48.2.165-185.
Levy, R. „Savings? What savings?“ BMJ 343, jul05 3 (05.07.2011): d4035. http://dx.doi.org/10.1136/bmj.d4035.
Abramov, Alexander E., und Maria I. Chernova. „Improving pension savings investing: The case of Russia“. Russian Journal of Economics 10, Nr. 1 (29.03.2024): 34–59. http://dx.doi.org/10.32609/j.ruje.10.115594.
Nagode, Aleš. „Med domom in svetom: pesmi za glas in klavir Rista Savina“. Musicological Annual 48, Nr. 2 (01.12.2012): 79–89. http://dx.doi.org/10.4312/mz.48.2.79-89.
Kasim, Arena Che. „SAVINGS PATTERNS AMONG Gen Z YOUTHS“. International Journal of Psychosocial Rehabilitation 24, Nr. 4 (28.02.2020): 4623–33. http://dx.doi.org/10.37200/ijpr/v24i4/pr201562.
Berner, Robert L., und Linda Hogan. „Savings“. World Literature Today 63, Nr. 4 (1989): 723. http://dx.doi.org/10.2307/40145718.
Klyczek, J. P. „Savings“. American Journal of Occupational Therapy 47, Nr. 3 (01.03.1993): 270. http://dx.doi.org/10.5014/ajot.47.3.270.