Academic literature on the topic 'Β-galactosidases'
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Journal articles on the topic "Β-galactosidases"
Kumar, Vijay, Nikhil Sharma, and Tek Chand Bhalla. "In Silico Analysis of β-Galactosidases Primary and Secondary Structure in relation to Temperature Adaptation." Journal of Amino Acids 2014 (March 24, 2014): 1–9. http://dx.doi.org/10.1155/2014/475839.
Full textMøller, Peter L., Flemming Jørgensen, Ole C. Hansen, Søren M. Madsen, and Peter Stougaard. "Intra- and Extracellular β-Galactosidases fromBifidobacterium bifidum and B. infantis: Molecular Cloning, Heterologous Expression, and Comparative Characterization." Applied and Environmental Microbiology 67, no. 5 (May 1, 2001): 2276–83. http://dx.doi.org/10.1128/aem.67.5.2276-2283.2001.
Full textPressey, Russell, and C. M. Sean Carrington. "β-Galactosidase II in Ripening Tomatoes." HortScience 30, no. 4 (July 1995): 817A—817. http://dx.doi.org/10.21273/hortsci.30.4.817a.
Full textNúñez-Montero, Kattia, Rodrigo Salazar, Andrés Santos, Olman Gómez-Espinoza, Scandar Farah, Claudia Troncoso, Catalina Hoffmann, Damaris Melivilu, Felipe Scott, and Leticia Barrientos Díaz. "Antarctic Rahnella inusitata: A Producer of Cold-Stable β-Galactosidase Enzymes." International Journal of Molecular Sciences 22, no. 8 (April 16, 2021): 4144. http://dx.doi.org/10.3390/ijms22084144.
Full textEda, Masahiro, Megumi Ishimaru, and Toshiji Tada. "Expression, purification, crystallization and preliminary X-ray crystallographic analysis of tomato β-galactosidase 4." Acta Crystallographica Section F Structural Biology Communications 71, no. 2 (January 28, 2015): 153–56. http://dx.doi.org/10.1107/s2053230x14027800.
Full textDutra Rosolen, Michele, Adriano Gennari, Giandra Volpato, and Claucia Fernanda Volken de Souza. "Lactose Hydrolysis in Milk and Dairy Whey Using Microbial β-Galactosidases." Enzyme Research 2015 (October 26, 2015): 1–7. http://dx.doi.org/10.1155/2015/806240.
Full textFerreira-Lazarte, Alvaro, F. Javier Moreno, and Mar Villamiel. "Application of a commercial digestive supplement formulated with enzymes and probiotics in lactase non-persistence management." Food & Function 9, no. 9 (2018): 4642–50. http://dx.doi.org/10.1039/c8fo01091a.
Full textPham, Mai-Lan, Anh-Minh Tran, Suwapat Kittibunchakul, Tien-Thanh Nguyen, Geir Mathiesen, and Thu-Ha Nguyen. "Immobilization of β-Galactosidases on the Lactobacillus Cell Surface Using the Peptidoglycan-Binding Motif LysM." Catalysts 9, no. 5 (May 12, 2019): 443. http://dx.doi.org/10.3390/catal9050443.
Full textRutkiewicz-Krotewicz, Maria, Agnieszka J. Pietrzyk-Brzezinska, Bartosz Sekula, Hubert Cieśliński, Anna Wierzbicka-Woś, Józef Kur, and Anna Bujacz. "Structural studies of a cold-adapted dimeric β-D-galactosidase fromParacoccussp. 32d." Acta Crystallographica Section D Structural Biology 72, no. 9 (August 31, 2016): 1049–61. http://dx.doi.org/10.1107/s2059798316012535.
Full textThoma, Julia, David Stenitzer, Reingard Grabherr, and Erika Staudacher. "Identification, Characterization, and Expression of a β-Galactosidase from Arion Species (Mollusca)." Biomolecules 12, no. 11 (October 27, 2022): 1578. http://dx.doi.org/10.3390/biom12111578.
Full textDissertations / Theses on the topic "Β-galactosidases"
Goulas, Theodoros K. "Biological and biotechnological aspects of β- and α-galactosidases from Bifidobacterium bifidum ncimb41171." Thesis, University of Reading, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.494990.
Full textAttal, Sandra. "Utilisation des enzymes en chimie organique : application à la synthèse d'esters de dipeptides par la papai͏̈ne et de galactosyl-sérines par les α-et β-galactosidases." Paris 5, 1992. http://www.theses.fr/1992PA05P614.
Full textYates, Francesca Jo. "Towards novel luminescent probes for monitoring β- galactosidase activity." Thesis, University of Birmingham, 2010. http://etheses.bham.ac.uk//id/eprint/1376/.
Full textPavel-Licsandru, Ileana-Alexandra. "Silica based materials for the encapsulation of β-Galactosidase." Thesis, Université de Lorraine, 2017. http://www.theses.fr/2017LORR0322/document.
Full textThe engineering of solid dietary supplements provides several advantages in the industrial formulation of food products, in terms of its production, storage and handling. Thereby, the goal of this doctoral work is to design bio-responsive carriers for the encapsulation of an exogenous enzyme able to catalyze the hydrolysis of lactose towards simple sugar molecules. In fact, there is a consensus that the onset of symptoms characteristic of lactose intolerance are associated with lactase deficiency in the small intestine. Providing the organism with exogenous lactase is the underlying application targeted by this work through the design of silicabased materials for encapsulation. The different types of bio-carriers developed had to overcome the simulated gastric conditions in order to release active enzyme molecules in the small intestine. Amorphous porous silica is a very good and non-toxic component affording protection versus acidic conditions, while providing controlled release. This inorganic material approved by the US Food and Drug Administration (FDA) has a relatively low cost, and presents a controlled structure (shape, size, pore diameter), as well as tunable surface chemistry. In agreement with the main objectives, four bio-adapted encapsulation strategies were investigated as potential routes to produce solid dietary supplements for lactose intolerance treatment: (i) physical entrapment of the enzyme in pre-synthesized meso-macroporous silica materials, (ii) physical entrapment of the enzyme in low porosity silica particles coated by liposomes, (iii) encapsulation of the enzyme into thermosensitive solid lipid nanoparticles (SLNs) (iv) encapsulation of the enzyme into a biopolymer matrix coated in a mesoporous silica shell
Belhacene, Kalim. "Conception de BioMEMS assistée par plasma froid : nouvelles approches." Thesis, Lille 1, 2016. http://www.theses.fr/2016LIL10034/document.
Full textThe micro and nanotechnology has created an upheaval in many field such as industry or research. For research, economic issues (quantity) and ecological (waste, chemical hazards) go straight in the direction of this miniaturization process for obtaining safe, clean and less expensive. This thesis presents the development of a new BioMEMS design process assisted by cold plasma. The objective is to develop a micro-device from a non-toxic material, tetramethyldisiloxane (TMDSO), through a plasma enhanced thin film deposition technology, and incorporating an enzyme, for carrying out catalytic reaction. For this, an immobilizer protocol and integration of the enzyme, β-galactosidase, was developed to verify TMDSO's ability to retain enzymes and retain its biological function. Then, an evaluation of the catalytic activity of the immobilized enzyme was carried out by carrying out the reaction millifluidic scale, validating the asset and the biocompatibility of ppTMDSO. Then, an immobilized enzyme microreactor was conducted to assess the influence of the transition to the microfluidic scale and understand the phenomena related to the diffusion and reaction of the species within the device. Finally, the design of a microchannel ppTMDSO and incorporating the enzyme, was conducted to study the feasibility of a "bio-integral 'methodology for establishing a BioMEMS. The use of a bio-integral method may be regarded as a promising alternative for the development of new research tools
Rafael, Ruan Da Silva. "Imobilização de β-galactosidase através de ligações covalentes multipontuais em suporte contendo grupamentos epoxi." reponame:Repositório Institucional da UNIVATES, 2014. http://hdl.handle.net/10737/604.
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A enzima β – galactosidase é reconhecida por catalisar a hidrólise da lactose e possibilitar a formação de galactooligossacarídeos. O objetivo do presente trabalho foi estudar diferentes condições de imobilização de β – galactosidases de Aspergillus oryzae e Kluyveromyces lactis utilizando suporte comercial Immobead. Ambas as enzimas foram imobilizadas nos suportes tratados e não tratados com etilenodiamina e submetidas a processos de imobilização uni e multipontual. Os derivados também foram avaliados quanto ao bloqueio dos grupamentos epóxi com glicina. As análises de estabilidade ao armazenamento sob refrigeração, estabilidade térmica, ciclos de reuso para hidrólise da lactose, determinação das propriedades cinéticas e determinação de pH e temperatura ótimos foram realizadas nos derivados obtidos. Os resultados de eficiência de imobilização variaram de 30 a 50% e os valores de rendimento variaram entre 80 e 90%. Modificações químicas no suporte foram realizadas utilizando etilenodiamina com o objetivo de gerar modificações químicas no suporte, causando a rápida adsorção de enzimas e favorecendo a formação de ligações covalentes multipontuais em tempo reduzido. Verificou-se que suportes modificados com etilenodiamina imobilizaram a mesma carga de enzimas em menor tempo, quando comparados a suportes sem modificação. Entretanto, a significativa perda de atividade verificada nesses suportes durante os ciclos de reuso sugere que a superfície do suporte possa ter sido modificada em sua totalidade, dificultando a formação de ligações covalentes e permitindo a lixiviação de enzimas para o meio reacional. Derivados não bloqueados apresentaram perda considerável de atividade enzimática durante a armazenagem, indicando a ocorrência de possíveis distorções da enzima, ocasionadas pela interação de grupamentos epóxi livres. Ensaios submetidos à imobilização multipontual apresentaram melhorias em sua estabilidade térmica. Os valores de Km para as enzimas imobilizadas de K. lactis e A. oryzae foram 49,69 e 55,29 mM, valores superiores àqueles verificados para as enzimas livres (19,11 e 17,37 mM, respectivamente), indicando possíveis alterações conformacionais na estrutura da proteína, resultantes do processo de imobilização. Os resultados indicaram que derivados não tratados com etilenodiamina, submetidos à imobilização covalente multipontual e bloqueio com glicina apresentaram os resultados mais expressivos para as condições estudadas de estabilidade ao armazenamento, estabilidade térmica e ciclos de reuso para hidrólise de lactose. Esses derivados não apresentaram distorções em relação às condições ótimas de temperatura e pH quando comparadas com as respectivas enzimas livres. As β – galactosidases de A. oryzae e K. lactis submetidas à imobilização covalente multipontual no suporte Immobead posteriormente bloqueado com glicina apresentaram as melhores propriedades para futura aplicação industrial.
Martins, André Rosa. "Conversão de lactose e síntese de galactoologossacarídeos por acão de β-galactosidade e de microrganismos probióticos em bioprocessos simultâneos com catálise e fermentação láctica." reponame:Repositório Institucional da FURG, 2009. http://repositorio.furg.br/handle/1/2434.
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Esse projeto desenvolveu um processo simultâneo de catálise e fermentação láctica visando obter um iogurte com características nutracêuticas. O objetivo principal foi avaliar a conversão da lactose e a síntese de galactooligossacarídeos (GOS) para um substrato específico, comparando biocatálises conduzidas simultaneamente à fermentação com os processos sem adição de enzima. A fermentação foi realizada a partir de cultura láctica liofilizada comercial contendo dois microrganismos probióticos, Bifidobacterium animalis e Lactobacillus acidophilus, associados aos microrganismos característicos do iogurte, Lactobacillus delbruekii subs. bulgaricus e Streptococcus salivarius subs. thermophilus. Foi utilizado um preparado enzimático contendo β- galactosidases obtidas de duas origens distintas: Kluyveromyces lactis e Aspergillus niger. Foram avaliados os efeitos das variações da concentração de lactose no substrato, da concentração de enzima e do tempo de adição da enzima em um planejamento experimental 23. As respostas foram o tempo de processo, a lactose final, a conversão da lactose, a densidade, a viscosidade, a sinérese e a concentração de GOS, comparando os processos enzimáticos e fermentativos simultâneos com a fermentação sem a adição de enzima. Os resultados indicaram um percentual de conversão da lactose entre 97,7 e 99,7% e uma produção de GOS nas condições de maior concentração inicial de lactose no substrato, menor concentração de enzima e maior tempo de defasagem na adição da enzima. Os efeitos sobre os parâmetros de textura foram negativos, indicando a necessidade de um acréscimo de agentes espessantes e estabilizantes nos bioprocessos simultâneos, quando do aumento da concentração de enzima. Observou-se, ainda, um impacto positivo no tempo de processamento quando da comparação entre os bioprocessos simultâneos e os processos de múltiplos estágios, na elaboração de fermentados lácticos com baixa concentração de lactose.
This project developed a simultaneous process of catalysis and lactic fermentation aiming to obtain a yogurt with nutraceuticals characteristics. The main objective was the conversion of lactose and the synthesis of galactooligosaccharides (GOS) for a specific substrate, comparing the biocatalysis conducted simultaneously to the fermentation with the processes without adding enzymes. Fermentation started with a commercial lactic lyophilized containing two probiotics microorganisms, Bifidobacterium animalis and Lactobacillus acidophilus, associated with microorganisms characteristics of yogurts, Lactobacillus delbruekii subs. bulgaricus and Streptococcus salivarius substhermophilus. It was used an enzymatic preparation containing β-galactosidases obtained from two distinct sources: Kluyveromyces lactis and Aspergillus niger. It were evaluated the effects of the variation of lactose concentration on the substrate, the enzyme concentration and the time of enzyme addition in an experimental design 23. The results were the process time, final lactose, lactose conversion, density, viscosity, sineresys and GOS concentration, comparing simultaneous enzymatic and fermentation processes with fermentation without the addition of enzymes. Results indicated a lactose conversion percentage between 97,7% and 99,7%, and a production of GOS in the condition of higher initial concentration of lactose in the substrate, lower enzyme concentration and more time of delayed in the addition of enzyme. The effects on texture parameters were negative, indicating the need for an increase of thickening agents and stabilizers in simultaneous bioprocesses when the increasing the enzyme concentration. It was also observed a positive impact on processing time when it was compared the simultaneous bioprocesses with the multiple stages processes in the elaboration of lactic fermented with low concentration of lactose.
Klein, Manuela Poletto. "Imobilização de β-galactosidase para obtenção de produtos lácteos com baixo teor de lactose." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2010. http://hdl.handle.net/10183/24803.
Full textβ-galactosidase (E.C 3.2.1.23) is the most widely used enzymes in the food industry and its employed in the lactose hydrolysis process. In this study, two methodologies were used to test their immobilization. In the first, the enzyme was immobilized by adsorption in one silica based hybrid material that contains a cationic organic group covalently linked. The efficiency of immobilization showed a decrease of 74 to 53% by increasing the protein load applied to the support. The low thermo stability of the immobilized enzyme and the probable weak interactions involved in their adsorption, could explain the decrease in enzyme activity observed in the successive batch hydrolysis of lactose. In the first run, the degree of lactose hydrolysis was 90.9% and, at the end of the last run (4th), the enzyme was able to convert only 13% of the substrate. The second methodology used was the covalent immobilization of the enzyme on a cellulose/ionic liquid film, modified with a polyamine and activated using glutaraldehyde. The presence of a polyamine was confirmed by infrared analysis. After immobilization, the enzyme retained 60% of its initial activity. Highly efficient lactose conversion was achieved in a batch process at 7ºC and 35ºC and was possible to reuse the immobilized enzyme in 16 repeated cycles, at 7ºC, without any drastic decrease in enzyme activity. Km value for the immobilized enzyme in silica based hybrid material was 9.17 mM and for the enzyme immobilized in the film of cellulose/ionic liquid was 11.22 mM, both showing an increase compared with the Km value for free enzyme (1.25 mM), due to the difficulty of access of the substrate to the active sites of the enzyme. The immobilized enzyme did not show any changes in the optimal pH and temperature when compared to the free enzyme in both methods tested.
Bezerra, Camilla Salviano. "Imobilização de β-galactosidase de Kluyveromyces lactis em diferentes suportes e protocolos de ativação." reponame:Repositório Institucional da UFC, 2012. http://www.repositorio.ufc.br/handle/riufc/10788.
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β-galactosidase immobilization was studied seeking to add value to cheese whey trough lactose hydrolyze producing galactose and glucose. This work aimed to develop biocatalysts using different organic supports and activation protocols. Firstly, some supports were prepared as chitosan 2.5% (w/v) (with and without pretreatment with dimethylformamide) and 2.0% (w/v), chitosan-alginate-epoxide (QAE), cashew bagasse (BC) and coconut shell fiber (CV), which were activated in different ways with glutaraldehyde, epichlorohydrin or glycidol. Initially, it was determined the immobilization yield, couple yield and apparent activity from obtained catalysts, being chosen six derivatives according to better results parameters: 2.5% chitosan (w/v) glutaraldehyde activated (QUITGLU1), 2.0% chitosan (w/v) KOH coagulated at 50°C glutaraldehyde activated (QUITGLU2) and epichlorohydrin (QUITEPI) or glycidol (QUITGLI), chitosan 2.5% (w/v) dimethylformamide treated with epichlorohydrin (QUIT-DMFEPI) or glycidol (QUIT-DMFGLI). Thus, catalysts (QUITGLU1, QUITGLU2, QUITEPI, QUITGLI) were studied as operational stability by using a continuous reactor, as well as, maximum enzyme loading and effectiveness assays. Then, it was determined QUITGLU2 as the best biocatalyst and following studies were carried out: immobilization time, enzyme optimum temperature and pH, kinetic parameters using lactose as substrate at 37°C, storage at 10°C and operational stability using high load enzyme and cheese whey as substrate. CV and BC supports did not present good results for β-Kluyveromyces lactis galactosidase immobilization, as well as, QAE support. Supports treated with dimethylformamide presented low immobilization yields. The results for QUITGLU2 derivative presented maximum loading of 75 mgProtein.g-1support and higher effectiveness than others. The operational stability for this derivative remained stable, with constant glucose production for 10 h of reaction. Immobilization time of 3h proved enough for the process. The Km and Vmáx values were respectively: free enzyme (46.79 mM and 7,142.86 μmol.(mL.min)-1) and catalyst (69.56 mM and 113.25 μmol.(g.min)-1). During 120 days of storage at 10°C, no decrease derivative hydrolitic activity was noted, demonstrating satisfactory storage stability. Finally, the biocatalyst showed good results as operational stability when used high offered enzyme load (theoretically immobilized load 255.9 mgProtein.g-1chitosan) for cheese whey hydrolysis
A imobilização de β-galactosidase para hidrólise de lactose é uma proposta para agregar valor ao soro de leite com conseqüente produção de galactose e glicose. O objetivo deste trabalho foi desenvolver biocatalisadores a partir de diferentes suportes orgânicos e protocolos de ativação visando à hidrólise de lactose proveniente do soro de leite. Inicialmente, prepararam-se os suportes a serem aplicados no estudo como quitosana 2,5% (m/v) (sem e com pré-tratamento com dimetilformamida) e 2,0% (m/v), quitosana-alginato-epoxilado (QAE), bagaço de caju (BC) e fibra de casca de coco verde (CV), os quais foram ativados de diferentes formas, com glutaraldeído, epicloridrina ou glicidol. Na primeira etapa, determinaram-se o rendimento de imobilização, atividade recuperada e atividade aparente dos diferentes derivados obtidos para assim determinar os seis melhores – quitosana 2,5% (m/v) ativada com glutaraldeído (QUITGLU1), quitosana 2,0% (m/v) coagulada com KOH a 50°C ativada com glutaraldeído (QUITGLU2) ou epicloridrina (QUITEPI) ou glicidol (QUITGLI), quitosana 2,5% (m/v) tratada com dimetilformamida ativada com epicloridrina (QUIT-DMFEPI) ou glicidol (QUIT-DMFGLI). Para segunda fase, os catalisadores (QUITGLU1, QUITGLU2, QUITEPI, QUITGLI) foram estudados quanto à estabilidade operacional com o uso de reator contínuo, assim como ensaios de carga máxima e efetividade. Baseado nestes ensaios determinou-se QUITGLU2 como melhor biocatalisador e realizaram-se os seguintes estudos: variação do tempo de imobilização, determinação da melhor temperatura e pH para atividade enzimática, determinação de parâmetros cinéticos, estocagem sob 10°C e estabilidade operacional com o uso de alta carga enzimática usando soro de leite como substrato. Suportes como CV e BC não apresentaram boa adequação para imobilização de β-galactosidase de Kluyveromyces lactis, assim como o suporte QAE. Suportes com tratamento com dimetilformamida apresentaram baixos rendimentos de imobilização. Os resultados para o derivado QUITGLU2 apresentaram carga máxima de 75 mgProteína.g-1 de suporte e efetividade superiores aos demais. A estabilidade operacional para este derivado apresentou-se estável, visto sua produção de glicose constante por 10 h de reação. O tempo 3 h mostrou-se suficiente para imobilização. Os valores de Km e Vmáx tanto para enzima solúvel (46,79 mM e 7.142,86 μmol.(mL.min)-1) quanto para o derivado (69,56 mM e 113,25 μmol.(g.min)-1). Durante os 120 dias de armazenamento sob 10°C, não houve decréscimo da atividade hidrolítica do derivado, demonstrando ótima estabilidade à estocagem. Por fim, o biocatalisador mostrou bons resultados de estabilidade operacional quando utilizado em alta carga oferecida (255,9 mgProteína.g-1 de quitosana de carga teoricamente imobilizada) para hidrólise de soro de leite
Lima, Micael de Andrade. "Recuperação e purificação de β-galactosidase de Kluyveromyces lactis utilizando cromatografia de modo misto." reponame:Repositório Institucional da UFC, 2014. http://www.repositorio.ufc.br/handle/riufc/10781.
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The most important lactases, as far as biotechnological interest is concerned, are those produced by Kluyveromyces yeasts, which are intracellular and currently obtained mostly by submerged-state fermentation. This technique, just as the mainstream biotechnological processes, involves a need for protein and peptide purification from a variety of sources. In this context, one of the most promising notable techniques that can be highlighted is Mixed Mode Chromatography, which allows simultaneous ionic and hydrophobic interactions between the adsorbent and the adsorbate. Thus, the aim of this work was to assess the feasibility of recovery and purification of a Kluyveromyces lactis β-galactosidase, produced via fermentation process, by employing Mixed Mode Chromatography. Unit operations, such as protein precipitation and dialysis were also performed in order to concentrate the enzyme of interest and eliminate cell debris and other interferences inherent in the fermentation medium, something that would result in a decrease in the process yield. The production showed satisfactory results, with mean values for total enzyme concentration of 0.45 mg/mL, enzymatic activity of 77 U/mL and specific activity of 167,9 U/mg. The Purification Factor obtained was 1.17. A precipitation step, followed by a dialysis process, was performed and the later chromatographic run carried out in fixed bed with this material yielded recovery values of 41.0 and 48.2% of total protein and activity, respectively. SDS-PAGE Electrophoresis confirmed the purification evolution throughout the unit operations employed, confirming the viability of the employment of the techniques used to obtain an enzyme of considerable degree of purity and possessing high-added value.
As mais importantes lactases, em termos de interesse biotecnológico, são aquelas produzidas por leveduras do gênero Kluyveromyces, que são intracelulares e, em sua maioria, são obtidas por fermentação em cultura submersa. Esta técnica, assim como a maioria dos processos biotecnológicos, envolve a necessidade de purificação de proteínas e peptídeos a partir de uma variedade de fontes. Neste contexto, uma das técnicas mais notavelmente promissoras é a cromatografia de modo misto, que permite interações iônicas e hidrofóbicas simultaneamente entre o adsorvente e o adsorbato. O objetivo do presente trabalho foi estudar a viabilidade da recuperação e purificação da enzima β-galactosidase, produzida por meio de processo fermentativo e utilizando o micro-organismo Kluyveromyces lactis, por técnica de cromatografia de modo misto. Operações unitárias de precipitação proteica e diálise foram também realizadas com o intuito de concentrar a enzima de interesse e eliminar detritos celulares e outros interferentes advindos do meio de fermentação, o que ocasionaria uma diminuição do rendimento do processo. A produção se apresentou satisfatória, com uma média de valores de concentração de enzimas totais de 0,45 mg/mL, atividade enzimática de 67 U/mL, atividade específica de 167,9 U/mg. O Fator de Purificação obtido foi de 1,17. Uma precipitação seguida de diálise foi realizada e a posterior corrida cromatográfica em leito fixo com esse material rendeu valores de recuperação de 41,0 e 48,2% de proteína total e atividade total, respectivamente. A análise de eletroforese SDS-PAGE confirmou a evolução do processo de purificação no decorrer das operações unitárias, atestando a viabilidade do emprego das técnicas utilizadas para obtenção de enzimas com considerável grau de pureza com alto valor comercial agregado.
Books on the topic "Β-galactosidases"
Gonawan, Fadzil Noor. Immobilized β-Galactosidase-Mediated Conversion of Lactose: Process, Kinetics and Modeling Studies. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-3468-9.
Full textGonawan, Fadzil Noor. Immobilized β-Galactosidase-Mediated Conversion of Lactose: Process, Kinetics and Modeling Studies. Springer, 2019.
Find full textBook chapters on the topic "Β-galactosidases"
Harju, M. "Hydrolysis of Lactulose and Lactitol with β-Galactosidases." In MILK the vital force, 232. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-3733-8_191.
Full textPlou, Francisco J., Julio Polaina, Julia Sanz-Aparicio, and María Fernández-Lobato. "β-Galactosidases for Lactose Hydrolysis and Galactooligosaccharide Synthesis." In Microbial Enzyme Technology in Food Applications, 121–44. Boca Raton, FL : CRC Press, [2016] | Series: Food biology series | “A science publishers book.”: CRC Press, 2017. http://dx.doi.org/10.1201/9781315368405-9.
Full textCieśliński, Hubert, Marta Wanarska, Anna Pawlak-Szukalska, Ewelina Krajewska, Monika Wicka, and Józef Kur. "Cold-Active β-Galactosidases: Sources, Biochemical Properties and Their Biotechnological Potential." In Biotechnology of Extremophiles:, 445–69. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-13521-2_15.
Full textIsobe, Kimiyasu, and Miwa Yamada. "β-Galactosidases from an Acidophilic Fungus, Teratosphaeria acidotherma AIU BGA-1." In Fungi in Extreme Environments: Ecological Role and Biotechnological Significance, 419–40. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-19030-9_21.
Full textRubens, P., P. Degraeve, P. Lemay, and K. Heremans. "Pressure and Temperature Stability of β-Galactosidases: A Structural and Functional Study." In Advances in High Pressure Bioscience and Biotechnology, 227–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60196-5_50.
Full textZabin, Irving. "From Acetylase to β-Galactosidase." In Origins of Molecular Biology, 189–98. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555817763.ch20.
Full textWisdom, G. Brian. "β-Galactosidase Labeling of IgG Antibody." In Springer Protocols Handbooks, 677–79. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-198-7_65.
Full textMonroe, Dan. "A Novel Homogeneous β-Galactosidase Immunoassay System." In Reviews on Immunoassay Technology, 70–76. London: Palgrave Macmillan UK, 1989. http://dx.doi.org/10.1007/978-1-349-11009-4_5.
Full textWisdom, G. Brian. "β-Galactosidase Labeling of Antibody Using MBS." In Springer Protocols Handbooks, 271–72. Totowa, NJ: Humana Press, 1996. http://dx.doi.org/10.1007/978-1-60327-259-9_42.
Full textItahana, Koji, Yoko Itahana, and Goberdhan P. Dimri. "Colorimetric Detection of Senescence-Associated β Galactosidase." In Methods in Molecular Biology, 143–56. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-239-1_8.
Full textConference papers on the topic "Β-galactosidases"
Zolnere, Kristine, and Inga Ciprovica. "The comparison of commercially available β-galactosidases for dairy industry : review." In Research for Rural Development, 2017. Latvia University of Agriculture, 2017. http://dx.doi.org/10.22616/rrd.23.2017.032.
Full textTian, Jing, Ping Zhao, Longquan Xu, Xu Fei, and Yi Wang. "Purification of soyasaponin -β-galactosidase fromAspergillussp.39." In Third International Conference on Photonics and Image in Agriculture Engineering (PIAGENG 2013), edited by Honghua Tan. SPIE, 2013. http://dx.doi.org/10.1117/12.2019642.
Full textGennari, Adriano, Francielle Herrmann Mobayed, Giandra Volpato, and Claucia Fernanda Volken de Souza. "Caracterização da β-Galactosidase Imobilizada em Immobead 150." In Simpósio de Bioquímica e Biotecnologia. Londrina - PR, Brazil: Galoa, 2017. http://dx.doi.org/10.17648/simbbtec-2017-80818.
Full textBraga, Anna Rafaela Cavalcante, and Veridiana Vera de Rosso. "ATIVIDADE DAS ENZIMAS β-GALACTOSIDASE, β-GLUCOSIDASE E α-GALACTOSIDASE DURANTE A FERMENTAÇÃO DA POLPA DE JUÇARA (Euterpe edulis Mart.)." In Simpósio Nacional de Bioprocessos e Simpósio de Hidrólise Enzimática de Biomassa. Campinas - SP, Brazil: Galoá, 2015. http://dx.doi.org/10.17648/sinaferm-2015-31918.
Full textAthayde, C. M., and M. C. Scrutton. "ROLE OF GUANINE NUCLEOTIDES IN Ca2+ - DEPENDENT LYSOSOMAL SECRETION FROM ELECTROPERMEABILISED PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644513.
Full textZolnere, Kristine, Janis Liepins, and Inga Ciprovica. "The impact of calcium ions on commercially available β-galactosidase." In Baltic Conference on Food Science and Technology FOODBALT “Food for consumer well-being”. Latvia University of Agriculture. Faculty of Food Technology., 2017. http://dx.doi.org/10.22616/foodbalt.2017.017.
Full textBreger, Joyce C., Anthony P. Malanoski, Carl W. Brown, Jeffrey R. Deschamps, Kimhiro Susumu, Eunkeu Oh, George P. Anderson, Scott A. Walper, and Igor L. Medintz. "Probing kinetic enhancement of β-galactosidase-nanoparticle complexes (Conference Presentation)." In Colloidal Nanoparticles for Biomedical Applications XIII, edited by Xing-Jie Liang, Wolfgang J. Parak, and Marek Osiński. SPIE, 2018. http://dx.doi.org/10.1117/12.2289988.
Full textJiang, Jian-Xing, and Yu-kaung Chang. "Process Design for Production of β-Galactosidase from Pichia Pastoris." In 14th Asia Pacific Confederation of Chemical Engineering Congress. Singapore: Research Publishing Services, 2012. http://dx.doi.org/10.3850/978-981-07-1445-1_707.
Full textYuki Grafulin, Vanessa, Bruna Coelho Andrade, Rafaela Rubim, Claucia Fernanda Volken de Souza, Jocelei Maria Chies, Diógenes Santiago Santos, Gaby Renard, and Giandra Volpato. "CLONAGEM DO GENE QUE CODIFICA A β-GALACTOSIDASE DE Kluyveromyces sp." In Simpósio Nacional de Bioprocessos e Simpósio de Hidrólise Enzimática de Biomassa. Campinas - SP, Brazil: Galoá, 2015. http://dx.doi.org/10.17648/sinaferm-2015-33641.
Full textSILVA, E. C. da, P. D. SANTOS, G. A. A. FERNANDES, A. M. O. MOTA, A. L. F. PORTO, and M. T. H. CAVALCANTI. "PRODUÇÃO DE β-GALACTOSIDASE POR BACTÉRIAS ÁCIDO LÁTICAS UTILIZANDO SORO DE LEITE." In XX Congresso Brasileiro de Engenharia Química. São Paulo: Editora Edgard Blücher, 2015. http://dx.doi.org/10.5151/chemeng-cobeq2014-0533-25073-142946.
Full textReports on the topic "Β-galactosidases"
Olson, Joan. Repression of β-galactosidase synthesis in Escherichia coli by salicylates. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1125.
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