Relevant bibliographies by topics / Lactate permease

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Academic literature on the topic 'Lactate permease'

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Published: 14 March 2023

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Journal articles on the topic "Lactate permease"

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Casal, Margarida, Sandra Paiva, Raquel P. Andrade, Carlos Gancedo, and Cecília Leão. "The Lactate-Proton Symport of Saccharomyces cerevisiae Is Encoded by JEN1." Journal of Bacteriology 181, no. 8 (April 15, 1999): 2620–23. http://dx.doi.org/10.1128/jb.181.8.2620-2623.1999.

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ABSTRACT A mutant of Saccharomyces cerevisiae deficient in the lactate-proton symport was isolated. Transformation of the mutant with a yeast genomic library allowed the isolation of the geneJEN1 that restored lactate transport. Disruption ofJEN1 abolished uptake of lactate. The results indicate that, under the experimental conditions tested, no other monocarboxylate permease is able to efficiently transport lactate inS. cerevisiae.
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Stansen, Corinna, Davin Uy, Stephane Delaunay, Lothar Eggeling, Jean-Louis Goergen, and Volker F. Wendisch. "Characterization of a Corynebacterium glutamicum Lactate Utilization Operon Induced during Temperature-Triggered Glutamate Production." Applied and Environmental Microbiology 71, no. 10 (October 2005): 5920–28. http://dx.doi.org/10.1128/aem.71.10.5920-5928.2005.

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ABSTRACT Gene expression changes of glutamate-producing Corynebacterium glutamicum were identified in transcriptome comparisons by DNA microarray analysis. During glutamate production induced by a temperature shift, C. glutamicum strain 2262 showed significantly higher mRNA levels of the NCgl2816 and NCgl2817 genes than its non-glutamate-producing derivative 2262NP. Reverse transcription-PCR analysis showed that the two genes together constitute an operon. NCgl2816 putatively codes for a lactate permease, while NCgl2817 was demonstrated to encode quinone-dependent l-lactate dehydrogenase, which was named LldD. C. glutamicum LldD displayed Michaelis-Menten kinetics for the substrate l-lactate with a Km of about 0.51 mM. The specific activity of LldD was about 10-fold higher during growth on l-lactate or on an l-lactate-glucose mixture than during growth on glucose, d-lactate, or pyruvate, while the specific activity of quinone-dependent d-lactate dehydrogenase differed little with the carbon source. RNA levels of NCgl2816 and lldD were about 18-fold higher during growth on l-lactate than on pyruvate. Disruption of the NCgl2816-lldD operon resulted in loss of the ability to utilize l-lactate as the sole carbon source. Expression of lldD restored l-lactate utilization, indicating that the function of the permease gene NCgl2816 is dispensable, while LldD is essential, for growth of C. glutamicum on l-lactate.
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Exley, Rachel M., Linda Goodwin, Eva Mowe, Jonathan Shaw, Harry Smith, Robert C. Read, and Christoph M. Tang. "Neisseria meningitidis Lactate Permease Is Required for Nasopharyngeal Colonization." Infection and Immunity 73, no. 9 (September 2005): 5762–66. http://dx.doi.org/10.1128/iai.73.9.5762-5766.2005.

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ABSTRACT Neisseria meningitidis is a human specific pathogen that is part of the normal nasopharyngeal flora. Little is known about the metabolic constraints on survival of the meningococcus during colonization of the upper airways. Here we show that glucose and lactate, both carbon energy sources for meningococcal growth, are present in millimolar concentrations within nasopharyngeal tissue. We used a mutant defective for the uptake of lactate (C311ΔlctP) to investigate the contribution of this energy source during colonization. Explants of nasopharyngeal tissue were inoculated with the wild-type strain (C311) and C311ΔlctP; the mutant was recovered at significantly lower levels (P = 0.01) than C311 18 h later. This defect was not due to changes in the expression of adhesins or initial adhesion in C311ΔlctP to epithelial cells. Instead, lactate appears to be important energy source for the bacterium during colonization and is necessary for growth of the bacterium in nasopharyngeal tissue. Studies with other strains defective for the uptake of specific nutrients should provide valuable information about the environment in which N. meningitidis persists during carriage.
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Skory, Christopher D., Ronald E. Hector, Steven W. Gorsich, and Joseph O. Rich. "Analysis of a functional lactate permease in the fungus Rhizopus." Enzyme and Microbial Technology 46, no. 1 (January 2010): 43–50. http://dx.doi.org/10.1016/j.enzmictec.2009.08.014.

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SOARES-SILVA, Isabel, Dorit SCHULLER, Raquel P. ANDRADE, Fátima BALTAZAR, Fernanda CÁSSIO, and Margarida CASAL. "Functional expression of the lactate permease Jen1p of Saccharomyces cerevisiae in Pichia pastoris." Biochemical Journal 376, no. 3 (December 15, 2003): 781–87. http://dx.doi.org/10.1042/bj20031180.

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In Saccharomyces cerevisiae the activity for the lactate–proton symporter is dependent on JEN1 gene expression. Pichia pastoris was transformed with an integrative plasmid containing the JEN1 gene. After 24 h of methanol induction, Northern and Western blotting analyses indicated the expression of JEN1 in the transformants. Lactate permease activity was obtained in P. pastoris cells with a Vmax of 2.1 nmol·s−1·mg of dry weight−1. Reconstitution of the lactate permease activity was achieved by fusing plasma membranes of P. pastoris methanol-induced cells with Escherichia coli liposomes containing cytochrome c oxidase, as proton-motive force. These assays in reconstituted heterologous P. pastoris membrane vesicles demonstrate that S. cerevisiae Jen1p is a functional lactate transporter. Moreover, a S. cerevisiae strain deleted in the JEN1 gene was transformed with a centromeric plasmid containing JEN1 under the control of the glyceraldehyde-3-phosphate dehydrogenase constitutive promotor. Constitutive JEN1 expression and lactic acid uptake were observed in cells grown on either glucose and/or acetic acid. The highest Vmax (0.84 nmol·s−1·mg of dry weight−1) was obtained in acetic acid-grown cells. Thus overexpression of the S. cerevisiae JEN1 gene in both S. cerevisiae and P. pastoris cells resulted in increased activity of lactate transport when compared with the data previously reported in lactic acid-grown cells of native S. cerevisiae strains. Jen1p is the only S. cerevisiae secondary porter characterized so far by heterologous expression in P. pastoris at both the cell and the membrane-vesicle levels.
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PAIVA, Sandra, Arthur L. KRUCKEBERG, and Margarida CASAL. "Utilization of green fluorescent protein as a marker for studying the expression and turnover of the monocarboxylate permease Jen1p of Saccharomyces cerevisiae." Biochemical Journal 363, no. 3 (April 24, 2002): 737–44. http://dx.doi.org/10.1042/bj3630737.

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Green fluorescent protein (GFP) from Aequorea victoria was used as an in vivo reporter protein when fused to the C-terminus of the Jen1 lactate permease of Saccharomyces cerevisiae. The Jen1 protein tagged with GFP is a functional lactate transporter with a cellular abundance of 1670 molecules/cell, and a catalytic-centre activity of 123s−1. It is expressed and tagged to the plasma membrane under induction conditions. The factors involved in proper localization and turnover of Jen1p were revealed by expression of the Jen1p—GFP fusion protein in a set of strains bearing mutations in specific steps of the secretory and endocytic pathways. The chimaeric protein Jen1p—GFP is targeted to the plasma membrane via a Sec6-dependent process; upon treatment with glucose, it is endocytosed via END3 and targeted for degradation in the vacuole. Experiments performed in a Δdoa4 mutant strain showed that ubiquitination is associated with the turnover of the permease.
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Lodi, T., F. Fontanesi, and B. Guiard. "Co-ordinate regulation of lactate metabolism genes in yeast: the role of the lactate permease gene JEN1." Molecular Genetics and Genomics 266, no. 5 (January 2002): 838–47. http://dx.doi.org/10.1007/s00438-001-0604-y.

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Andrade, Raquel P., and Margarida Casal. "Expression of the Lactate Permease Gene JEN1 from the Yeast Saccharomyces cerevisiae." Fungal Genetics and Biology 32, no. 2 (March 2001): 105–11. http://dx.doi.org/10.1006/fgbi.2001.1254.

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Ayala, Julio C., and William M. Shafer. "Transcriptional regulation of a gonococcal gene encoding a virulence factor (L-lactate permease)." PLOS Pathogens 15, no. 12 (December 20, 2019): e1008233. http://dx.doi.org/10.1371/journal.ppat.1008233.

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Exley, Rachel M., Hong Wu, Jonathan Shaw, Muriel C. Schneider, Harry Smith, Ann E. Jerse, and Christoph M. Tang. "Lactate Acquisition Promotes Successful Colonization of the Murine Genital Tract by Neisseria gonorrhoeae." Infection and Immunity 75, no. 3 (December 11, 2006): 1318–24. http://dx.doi.org/10.1128/iai.01530-06.

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ABSTRACT Previous studies on Neisseria gonorrhoeae have demonstrated that metabolism of lactate in the presence of glucose increases the growth rate of the bacterium and enhances its resistance to complement-mediated killing. Although these findings in vitro suggest that the acquisition of lactate promotes gonococcal colonization, the significance of this carbon source to the survival of the gonococcus in vivo remains unknown. To investigate the importance of lactate utilization during Neisseria gonorrhoeae genital tract infection, we identified the gene lctP, which encodes the gonococcal lactate permease. A mutant that lacks a functional copy of lctP was unable to take up exogenous lactate and did not grow in defined medium with lactate as the sole carbon source, in contrast to the wild-type and complemented strains; the mutant strain exhibited no growth defect in defined medium containing glucose. In defined medium containing physiological concentrations of lactate and glucose, the lctP mutant demonstrated reduced early growth and increased sensitivity to complement-mediated killing compared with the wild-type strain; the enhanced susceptibility to complement was associated with a reduction in lipopolysaccharide sialylation of the lctP mutant. The importance of lactate utilization during colonization was evaluated in the murine model of lower genital tract infection. The lctP mutant was significantly attenuated in its ability to colonize and survive in the genital tract, while the complemented mutant exhibited no defect for colonization. Lactate is a micronutrient in the genital tract that contributes to the survival of the gonococcus.
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Dissertations / Theses on the topic "Lactate permease"

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Parillo, Carlo. "FUNCTIONAL CHARACTERIZATION OF ENVIRONMENTAL LACTATE UTILIZATION DURING NTHi in vitro INFECTION OF HUMAN EPITHELIA." Doctoral thesis, Università di Siena, 2018. http://hdl.handle.net/11365/1039777.

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Non-typeable Haemophilus influenzae (NTHi) is a small acapsulate gram-negative coccobacillus and a human restricted nasopharynx commensal. Nevertheless, it is the main cause of chronic obstructive pulmonary disease (COPD) exacerbation. A previous dual RNA-sequencing study highlighted the upregulation of an L-lactate permease gene, suggesting a role for environmental lactate during the infection. Furthermore, a strong downregulation of the sialic acid-specific tripartite ATP-independent periplasmic transporter (TRAP system) was reported, while a gene (pst) with 60% similarity with nanT, an N-acetyl neuraminic acid (NANA) transporter in E. coli, was found to be upregulated during the infection. In order to explore the impact of environmental lactate and NANA utilization during NTHi mucosal colonization, we constructed specific knock out strains for two uptake systems and analysed bacterial fitness and their resistance to complement-mediated killing during infection of human bronchial epithelia in vitro. In vitro assays were performed to analyse NTHi Δpst resistance to serum killing. The pst gene mutant strain did not show any alteration in the complement mediated killing resistance, even when the test was performed after an adaptation of the bacterium by infection of human bronchial epithelial cells. These data suggested a lack of mutuality between the TRAP system and the pst gene as sialic acid transporter during the infection stages. For what concerns the lactate permease knock out (ΔlctP) we observed a faster grow rate compared to the WT strain when lactate is the sole available carbon source. We also reported an impaired membrane composition which may cause this cell instability, more precisely we showed a lipid A decrement in a “lactate environment”. The altered membrane composition results in a strong aggregative phenotype both in bacteria-bacteria and bacteria-epithelia interactions. Despite the low endotoxin levels NTHi ΔlctP was still able to resist to the complement mediated killing when NANA was available. These data open to unknown complement killing evasion systems. In conclusion, our work is aimed to better characterize NTHi infection factors involved in the colonization of the human epithelium.
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Worthen, Denise Lynne. "Lactose binding to the E. coli symport protein Lac permease." Diss., Pasadena, Calif. : California Institute of Technology, 1989. http://resolver.caltech.edu/CaltechTHESIS:11242009-093118312.

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Dragana, Ilić-Udovičić. "Optimizacija tehnološkog procesa proizvodnje napitaka od enzimski hidrolizovanog permeata mleka." Phd thesis, Univerzitet u Novom Sadu, Tehnološki fakultet Novi Sad, 2015. http://www.cris.uns.ac.rs/record.jsf?recordId=95728&source=NDLTD&language=en.

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Valorizacija permeata kao sporednog proizvoda industrije mleka je od izuzetnog ekološkog, ekonomskog i tehnološkog značaja.Cilj doktorske disertacije je razvoj tehnološkog procesa prerade permeata, kao sporednog proizvoda dobijenog nakon ultrafiltracije mleka tokom proizvodnje feta sira i svežeg („mladog“) sira. Ispitana je mogućnost enzimske hidrolize laktoze u permeatu korišćenjem enzima β-galaktozidaze izolovanog iz Kluyveromyces lactis u koncentraciji 0,1, 0,3 i 0,5 g/100g na temperaturama 20º, 30º i 40 ºC. Praćene su promene sadržaja laktoze, D–galaktoze i D–glukoze u vremenskim intervalima tokom 60 minuta. Posebna faza istraživanja obuhvatila je matematičko modelovanje i kinetiku procesa hidrolize laktoze u permeatu pod dejstvom β –galaktozidaze i primenu hidrolizovanog permeata u proizvodnji mlečnih napitaka po odabranoj formulaciji. Predložen je tehnološki proces proizvodnje napitka na bazi hidrolizovanog permeata sa dodatkom voćnih baza. Utvrđeni su parametri kvaliteta i trajnosti napitaka tokom 60 dana skladištenja.Na temperaturi 40°C dodatkom enzima β -galaktozidaze u koncentraciji 0,1g/100g za 60 minuta postiže se 100% stepen hidrolize prisutne laktoze u permeatu. Sa većom koncentracijom enzima, 0,3 g/100g odnosno 0,5g/100g, na istoj temperaturi, isti efekat se postiže za 20 minuta.Ispitivanjem kinetike hidrolize laktoze potvrđena je kinetika prvog reda. Generalno posmatrano visoki koeficijenti determinacije pokazuju dobro poklapanje eksperimentalnih rezultata i matematičkog modela reakcije prvog reda. Vrednosti se kreću od 0,974 (temperatura 20°C) do preko 0,990 (na temperaturama 30°C i 40°C) pri koncentraciji enzima 0,1g/100g.Proizvedeni napici od hidrolizovanog permeata su delaktozirani i ne sadrže mlečnu mast. Od ukupnih šećera u svim napicima više od 50% čini glukoza: 50,16% - napitak šumsko voće, 50,42% - napitak pomorandža/šargarepa, 54,65% - napitak multivitamin, odnosno 55,13% - napitak crveno voće.Najveći sadržaj vitamina C nakon proizvodnje imao je napitak sa dodatkom voćne baze multivitamin 0,3972 mg/100g, zatim šumsko voće 0,2887 mg/100g i pomo-randža/šargarepa 0,1999 mg/100g.Najveću vrednost antioksidativne aktivnosti nakon proizvodnje pokazali su uzorci napitka sa multivitaminom i šumskim voćem. Tokom perioda skladištenja dolazi do smanjenja DPPH vrednosti. Najmanji pad je u napitku sa pomorandžom / šargarepom (smanjenje za 17%), a najveći u napitku sa šumskim voćem (za 39%). Analizirani uzorci sadrže ukupnih polifenola u intervalu od 47,84 do 120,38 mg GAE/l u zavisnosti od vrste napitka, odnosno dodatih voćnih baza.Generalno može se zaključiti da se prime-njenim tehnološkim procesom dobijaju napici stabilnog fizičko-hemijskog sastava tokom 60 dana skladištenja, visoke nutritivne i niske energetske vrednosti.
Valuation of the permeate as a by-product of the dairy industry is of great ecological, economic and technological importance.The aim of the PhD thesis is the development of the technological process of refining permeate, as a by-product obtained after ultrafiltration of milk during the production of feta cheese and fresh cheese. The possibility of enzymatic hydrolysis of the lactose in the permeate using the enzyme β-galactosidase isolated from Kluyveromyces lactis in a concentration of 0.1, 0.3 and 0.5 g / 100 g at a temperature of 20°, 30° and 40° C was examined. Changes in the content of lactose, D-galactose and D-glucose at intervals of 60 minutes were monitored. A special stage of the research included mathematical modeling and kinetics of lactose hydrolysis in the permeate under the influence of β-galactosidase and application of hydrolyzed permeate in the production of dairy products under the selected formulation. A technological process of producing a beverage on the basis of hydrolyzed permeate with the addition of fruit bases was suggested. Quality and durability parameters were determined for drinks during the 60 days of storage.Addition of the enzyme β-galactosidase at a concentration of 0.1 g / 100 g for 60 minutes at a temperature of 40 ° C a 100% degree of hydrolysis of lactose is achieved, present in the permeate. With a higher concentration of enzyme, 0.3 g / 100 g or 0.5 g / 100g, at the same temperature, the same effect can be achieved in 20 minutes.By examining the kinetics of lactose hydrolysis the first order kinetics was confirmed. Generally high coefficients of determination show good correspondence between the experimental results and the mathematical model of the first order reaction. Values range from 0.974 (at a temperature of 20° C) up to over 0.990 (at temperatures 30° C and 40° C) at a an enzyme concentration of 0.1g / 100g.Beverages produced from hydrolyzed permeate are lactose-free and fat-free products. More than half of the total sugar content in all beverages consists of glucose: 50.16%-forest fruit beverage, 50.42%-beverage orange/carrot, 54.65% beverage multivitamin and 55.13% - beverage red fruit.The highest vitamin C content after production was in a beverage with the addition of fruit base multivitamin (0.3972 mg/100g), followed by forest fruit (0.2887 mg/100g) and orange/carrot (0.1999 mg/100g).Beverage samples with multivitamin and forest fruits showed the highest value of antioxidant activity after production. During the storage period there is a reduction of DPPH values. The smallest decrease was in the beverage with orange/carrot (decreased 17%), and the biggest in the beverage with forest fruit (39%). The content of polyphenols in analyzed samples ranges from 47.84 to 120.38 mg GAE/L depending on the type of beverage and added fruit base.Overall it can be concluded that the applied technological process gives beverages of stable physical and chemical content during the 60 days of storage, of high nutritional value and low energy.
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Costa, Ricardo Calvo. "Obtenção de lactose a partir de permeado de soro de queijo e permeado de leite." [s.n.], 1995. http://repositorio.unicamp.br/jspui/handle/REPOSIP/255587.

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Orientador: Salvador M. Roig
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos
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Resumo: Neste trabalho foi estudada a extração de lactose a partir de permeado de leite e de permeado de soro de queijo, obtidos por ultrafiltração de leite e soro de queijo. A antecipação da etapa de descoloração foi estudada com o objetivo de eliminar a etapa de refino no processo tradicional e obter uma lactose de alto teor de pureza. A pasta descorante composta de 750/0 de carvão ativo e negro de ossos e 25% de ácido clorídrico concentrado foi adicionada aos permeados de leite e de soro de queijo, e somente resultou em descoloração quando foram utilizados teores de pasta superiores a 8% da massa de lactose presente no permeado. Os melhores resultados foram obtidos a partir de permeado de leite, obtido através de ultrafiltração de leite em um sistema de ultrafiltração dotado de membranas minerais, sem descoloracão do permeado. Os compostos coloridos foram retidos durante o processo de ultrafiltração resultando em um permeado límpido. O melhor processo obtido para extração de lactose a partir de permeado foi ultrafiltração do leite em membrana mineral, seguido de concentração à vácuo do permeado, cristalização, separação, lavagem dos cristais com água a 5°e e secagem. A partir de permeado de leite com 0,027% de nitrogênio total 0,49% de cinzas e 4,71 % de lactose foi obtida lactose com 99,3% de pureza 0,66% de cinzas e 0,07% de nitrogênio total
Abstract: The lactose extraction by ultrafiltration from milk and whey permeates was studied. The aim of this work was to eliminate the refining step of the traditional process and produce a high purity level lactose yield before the discolouring step. The discolouring paste which is made of 75% of a mixture of active carbon and black bone and 25% of concentrated hydrogen chloride was added to milk and whey permeates resulting in discolouring only when the paste concentration was higher than 8% in relation to the lactose mass in the permeate. The best results carne from milk permeate processed in a mineral membranes milk ultrafiltration system without the discolouring step. The colouring compounds were retained in the ultrafiltration process resulting in a cleaned permeate. The best process to lactose extraction from permeate was milk ultrafiltration in a mineral membrane system followed by permeate vacuum concentration, crystallization, separation and crystal washing with 't\1Iter at 5°e and drying. From mill permeate with 0,027% total nitrogen, 0,49% ash and 4,71% of lactose it was possible to obtain lactose with a purity of 99,3%, 0.660% ash and 0,07% total nitrogen contents
Mestrado
Mestre em Tecnologia de Alimentos
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Suárez, Germà Carme. "Investigation of the phospholipid peripheral region of lactose permease in model membranes." Doctoral thesis, Universitat de Barcelona, 2013. http://hdl.handle.net/10803/125470.

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The interaction between a membrane protein and its surrounding phospholipids is thought to be crucial for the correct folding and function of the protein. This thesis is focused on the investigation of the interplay between Lactose permease (LacY), a paradigm for secondary transporters present in the inner membrane of Escherichia coli and model systems mimicking its natural lipid environment. Since the role of phospholipids in LacY’s activity is currently being refined, this work represents a contribution to the field by studying the interaction at two different levels: (i) the LacY interplay with the phospholipids present at the annular region in the vicinity of the protein was studied through FRET measurements between a single-tryptophan LacY mutant and diverse pyrene-marked phospholipids, and (ii) the LacY interaction with the more distanced bulk phospholipids was studied through supported proteo-lipid sheets that were analysed using topography, force-spectroscopy and force-volume Atomic Force Microscopy modes. First, after validating LacY preference for phospholipid fluid (Lα) phases in the studied two-component model systems, a different composition between bulk and annular regions was confirmed. Hence, bulk lipids, which were assimilated to the phospholipids in Lα phase, were mainly formed by PG, while PE was the main component of the annular region. This points to a direct annular phospholipid-LacY selectivity because it discards a random phospholipid distribution near the protein. Second, the LacY selectivity for precise phospholipid species at the annular region was found to be related to: (i) a neutral charged phosholipid (PE or PC, with preference for the former), and (ii) phospholipids with large negative spontaneous curvature (C0) (DOPE > POPE). In addition, D68 was revealed as an important amino acid for the protein annular lipid selectivity. Third, the interaction between LacY and the bulk lipids was described as reciprocal. Accordingly, the presence of the protein largely modified the topography and the nanomechanics of the lipid system, especially for the Lα phase, whilst the nanomechanics of LacY itself were different depending on the surrounding lipid matrix: more force was needed to pull LacY form the DPPE:POPG (3:1, mol/mol) system than from the POPE:POPG (3:1, mol/mol) one. Therefore, the bilayer lipid composition seems to determine the forces governing the LacY tight interaction with the membrane and can be thus decisive for the protein correct insertion and activity.
La interacció entre una proteïna de membrana i els fosfolípids que l’envolten és crucial pel bon plegament i la correcta funció de la proteïna. Aquesta tesi està centrada en la investigació de la interacció entre la Lactosa permeasa (LacY), un paradigma dels transportadors secundaris situat a la membrana interna d’Escherichia coli, i sistemes models que mimetitzen el seu entorn lipídic. Aquest treball representa una contribució al camp a través de l’estudi de la interacció a dos nivells: (i) la interacció entre LacY i els fosfolípids presents a la regió anular propera a la proteïna ha estat estudiada a través de mesures de FRET entre un mutant de LacY amb un únic triptòfan i diversos fosfolípids marcats i (ii) la interacció entre LacY amb els fosfolípids més llunyans o bulk s’ha investigat a través de làmines de lípid i proteïna sobre un suport, les quals s’han analitzat a partir de diversos modes de microscòpia de força atòmica (topografia, espectroscòpia de força i force-volume). En primer lloc, s’ha validat la preferència de LacY pels fosfolípids en fases fluïdes (Lα). A més, s’ha confirmat una composició lipídica entre la regió anulars i el bulk. Així, els fosfolípids bulk, considerats com a fosfolípids en fase Lα, tenen PG com a principal component, mentre que PE és el major component de la regió anular. Això sembla indicar una selectivitat entre LacY i els fosfolípids anulars. En segon lloc, s’ha descrit que la selectivitat de LacY per fosfolípid determinat a la regió anular està relacionada amb (i) càrrega neutra i (ii) curvatura espontània (C0) negativa. A més, D68 s’ha assenyalat com un aminoàcid important per la selectivitat de la proteïna envers els lípids anulars. Finalment, s’ha descrit una interacció recíproca entre LacY i els lípids bulk. Així, la presencia de la proteïna modifica la topografia i la nanomecànica del sistema lipídic, especialment de la fase Lα, i, alhora, la nanomecànica de la pròpia LacY varia segons la matriu lipídica que l’envolta. En conseqüència, la composició lipídica de la bicapa sembla determinar les forces que governen l’estreta interacció de LacY amb la membrana i, per tant, aquesta composició és decisiva per la correcta inserció i activitat de la proteïna.
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Fernandes, Tatiana Alves Rigamonte. "Internalização da permease de lactose de Kluyveromyces lactis em resposta a fontes de carbono." Universidade Federal de Viçosa, 2010. http://www.locus.ufv.br/handle/123456789/6584.

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Fundação de Amparo à Pesquisa do Estado de Minas Gerais
A permease de lactose de Kluyveromyces lactis, Lac12, media o transporte de lactose e o de galactose de baixa afinidade. Aqui é apresentado o estudo do efeito de fontes de carbono na internalização de Lac12 através do uso de linhagens contendo o gene quimérico LAC12-GFP. Quando células de K. lactis pré-cultivadas em galactose ou lactose foram transferidas para um novo meio, Lac12-GFP foi removida da membrana plasmática e localizada intracelularmente. Surpreendentemente, mesmo a presença de galactose ou lactose no novo meio de transferência causou essa internalização, e a resposta celular foi diferente para esse dois açúcares. Os resultados obtidos revelam que o processo de internalização é dependente do tipo de açúcar presente e de sua concentração. A internalização de Lac12-GFP causou redução nas taxas de captação de lactose[C14] e também foi observada em uma linhagem mutante Klsnf1; portanto, esse evento independe da atividade de KlSnf1. Evidências indicam que glicose-6-fosfato é o sinal intracelular, uma vez que a internalização foi induzida por 2-deoxiglicose, e a inibição da atividade da enzima fosfoglimutase por lítio impediu a internalização por galactose, mas não por lactose ou glicose. A internalização não ocorreu em 6-deoxiglicose, e, em ausência de síntese protéica, o evento foi irreversível.
Kluyveromyces lactis Lac12 permease mediates lactose and low-affinity galactose transports. In this study we have investigated the effects of carbon sources on internalization of Lac12 by using a LAC12-GFP fusion construct. When galactose- or lactose-grown cells are shifted to a fresh sugar medium, Lac12-GFP is removed from the plasma membrane and localized intracellularly. Surprisingly, even galactose or lactose in the new media caused the internalization, and cells responded differently to theses two sugars. Our results reveal that this process is dependent of sugar species and also sugar concentration. Lac12-GFP internalization causes reduction on [C14]lactose uptake rates and also occurs in a Klsnf1 mutant strain; thereby, it is independent of KlSnf1 activity. We suggest that glucose-6-phosphate is the intracellular signal, since internalization was induced by 2-deoxyglucose and inhibition of phosphoglucomutase by lithium prevented galactose- but not lactose- or glucose-induced internalization. Lac12-GFP internalization was not triggered by 6-deoxyglucose, and was irreversible in absence of protein synthesis.
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Ghazi, Alexandre. "La Lactose perméase d'Escherichia coli cotransport lactose proton et théorie chimiosmotique localisée : inactivation in vivo de la protéine /." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb376054042.

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Wakeling, Lara. "Utilisation of Kluyveromyces marxianus for the ethanolic fermentation of lactose in skim milk permeate." Thesis, University of Ballarat, School of Biological and Chemical Sciences [Mt. Helen, Vic.] :, 1994. http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/44690.

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Chaudhary, Manoja Nand, of Western Sydney Hawkesbury University, of Science Technology and Agriculture Faculty, and School of Food Science and Technology. "An evaluation of nanofiltration and lactose hydrolysis of milk UF permeate for use in ice cream." THESIS_FSTA_FST_Chaudhary_M.xml, 1997. http://handle.uws.edu.au:8081/1959.7/741.

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This study aimed to obtain 15% total solids and reduced mineral content in milk UF permeate by nanofiltration, hydrolysing the lactose content of nano-concentrate enzymically, partially substituting sucrose in ice cream formulations with hydrolysed lactose nano-concentrate (HLNC), and investigating the effects of HLNC on the physio-chemical and sensory characteristics of ice cream. The desired 15% total solids in the nano-concentrate was achieved after three fold concentration of milk UF permeate. The colour of milk permeate changed, pH and mineral content decreased, and crude protein content, lactose content and titratable acidity increased. The lactose content was hydrolysed by enzyme lactase. HLNC was used to replace 25% and 50% of sucrose in ice cream formulations. Springiness, cohesiveness, chewiness, adhesiveness, hardness, iciness, Ph and colour were not significantly affected. Viscosity, freezing point, glass transition temperature, melting temperature, gumminess and sweetness were significantly decreased, whereas freezing time, saltiness and cooked flavour were significantly increased. The overall acceptability of ice cream significantly decreased at 50% but was insignificantly affected at the 25% level. These results indicate that about one quarter of sucrose could be replaced by HLNC.
Master of Science (Hons) (Food Technology)
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Hsu, Ching-Suei. "Integrated Rotating Fibrous Bed Bioreactor-Ultrafiltration Process for Xanthan Gum Production from Whey Lactose." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1308303490.

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Book chapters on the topic "Lactate permease"

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Zall, R. R. "Sources and Composition of Whey and Permeate." In Whey and Lactose Processing, 1–72. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2894-0_1.

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Guan, Lan, and H. Ronald Kaback. "Lactose Permease: From Membrane to Molecule to Mechanism." In Biogenesis of Fatty Acids, Lipids and Membranes, 1–13. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-43676-0_48-1.

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Guan, Lan, and H. Ronald Kaback. "Lactose Permease: From Membrane to Molecule to Mechanism." In Biogenesis of Fatty Acids, Lipids and Membranes, 637–49. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-50430-8_48.

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Kaback, H. Ronald. "The Lactose Permease of Escherichia coli An Update." In Molecular Biology of Membrane Transport Disorders, 111–28. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1143-0_6.

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Guo, Xuewu, Yazhou Wang, Xiangyu Guan, Yefu Chen, Cuiying Zhang, and Dongguang Xiao. "Improved Lactose Utilization by Overexpression β-Galactosidase and Lactose Permease in Klebsiella pneumoniae." In Lecture Notes in Electrical Engineering, 121–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-45657-6_13.

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Kaback, H. Ronald. "β-Galactoside Transport in Escherichia Coli: The Ins and Outs of Lactose Permease." In Dynamics of Membrane Assembly, 293–308. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-662-02860-5_22.

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"Lactose Permease." In Encyclopedia of Biophysics, 1226. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_100513.

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"Lactose Permease." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1077. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_9169.

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Kaback, H. Ronald, Kirsten Jung, Heinrich Jung, Jianhua Wu, Gilbert G. Privé, and Kevin Zen. "Helix packing in the C-terminal half of lactose permease." In Protein Export and Membrane Biogenesis, 129–44. Elsevier, 1995. http://dx.doi.org/10.1016/s1874-5172(06)80010-6.

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Kaback, H. R. "Chapter 10 The lactose permease of Escherichia coli: Past, present and future." In Handbook of Biological Physics, 203–27. Elsevier, 1996. http://dx.doi.org/10.1016/s1383-8121(96)80051-0.

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Conference papers on the topic "Lactate permease"

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Jewel, Yead, Prashanta Dutta, and Jin Liu. "Coarse-Grained Molecular Dynamics Simulations of Sugar Transport Across Lactose Permease." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52337.

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Sugar (one of the critical nutrition elements for all life forms) transport across the cell membranes play essential roles in a wide range of living organism. One of the most important active transport (against the sugar concentration) mechanisms is facilitated by the transmembrane transporter proteins, such as the Escherichia coli lactose permease (LacY) proteins. Active transport of sugar molecules with LacY proteins requires a proton gradient and a sequence of complicated protein conformational changes. However, the exact molecular mechanisms and the protein structural information involved in the transport process are largely unknown. All atom atomistic simulations are able to provide full details but are limited to relative small length and time scales due to the computational cost. The protein conformational changes during sugar transport across LacY are large scale structural reorganization and inaccessible to all atom simulations. In this work, we investigate the molecular mechanisms and conformational changes during sugar transport using coarse-grained molecular dynamics (CGMD) simulations. In our coarse-grained force field, we follow the procedures developed by Han et al. [1, 2], in which the protein model is united-atom based and each heavy atom together with the attached hydrogen atoms is represented by one site, then the protein force filed is coupled with the MARTINI [3] water and lipid force fields. This hybrid force field takes the advantage of the efficiency of MARTINI force field for the environment (water and lipid), while retaining the detailed conformational information for the proteins. Specifically, we develop the new force fields for interactions between sugar molecules and protein by matching the potential of mean force between all-atom and coarse-grained models. Then we validate our force field by comparing the potential of mean force for a glucose interaction with a carbohydrate binding protein from our new force field, with the results from all atom simulations. After validation, we implement the force field for sugar transport across LacY proteins. Through our simulations we are able to capture the formation/breakage of the important hydrogen bonds and salt bridges, which are crucial to the overall conformational changes of LacY.
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Zolnere, Kristine, and Inga Ciprovica. "Lactose hydrolysis in different solids content whey and milk permeates." In 13th Baltic Conference on Food Science and Technology “FOOD. NUTRITION. WELL-BEING”. Latvia University of Life Sciences and Technologies. Faculty of Food Technology,, 2019. http://dx.doi.org/10.22616/foodbalt.2019.011.

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Pandey, Surabhi, Marie Josee Dumont, and Valerie Orsat. "Comparative kinetic study for the conversion of lactose and whey permeate powder into 5-hydroxymethylfurfural." In 2021 ASABE Annual International Virtual Meeting, July 12-16, 2021. St. Joseph, MI: American Society of Agricultural and Biological Engineers, 2021. http://dx.doi.org/10.13031/aim.202100747.

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Avtandilyan, N. G., R. R. Halkechev, and Aleksei Lodygin. "FORMATION OF REQUIREMENTS FOR THE COMPOSITION AND PHYSICOCHEMICAL PARAMETERS OF LACTOSE-CONTAINING RAW MATERIALS FOR THE PRODUCTION OF LACTULOSE CONCENTRATES." In I International Congress “The Latest Achievements of Medicine, Healthcare, and Health-Saving Technologies”. Kemerovo State University, 2023. http://dx.doi.org/10.21603/-i-ic-4.

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The relevance of lactulose concentrates development for the production of functional foods is substantiated. The results of studies of the effect of the amount of an alkaline catalyst of the isomerization reaction on the physico-chemical parameters of permeates of secondary dairy raw materials are presented.
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SCHULTZ, G., R. C. GIORDANO, and M. P. A. RIBEIRO. "CINÉTICA ENZIMÁTICA DA SÍNTESE DE GALACTO-OLIGOSSACARÍDEOS A PARTIR DE LACTOSE E PERMEADO DE SORO DE LEITE." In XXII Congresso Brasileiro de Engenharia Química. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/cobeq2018-pt.0935.

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Baller, Leocir, Gracinda Marina Castelo da Silva, and Clóvis Bombardelli. "ESTUDO DA HIDRÓLISE DA LACTOSE DO PERMEADO DE SORO DE LEITE PELA ENZIMA -GALACTOSIDASE SEGUIDO DA FERMENTAÇÃO ALCOÓLICA." In Simpósio Nacional de Bioprocessos e Simpósio de Hidrólise Enzimática de Biomassa. Campinas - SP, Brazil: Galoá, 2015. http://dx.doi.org/10.17648/sinaferm-2015-33389.

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Wang, C. T., J. Y. Lee, J. C. Chen, Y. J. Shiao, and W. J. Tsai. "EFFECT OF TRIFLUOPERAZINE (TFP) ON HUMAN PLATELET MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644816.

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TFP is a lipophilic antipsychotic drug. The drug will first encounter with cell membrane when adding it into a cell suspension. The effect of TFP on plasma membrane of the gel-filtered human platelet was investigated by : 1) scanning electron microscopy (SEM); 2) measuring theleakiness of marker enzymes and compound; 3) estimating its solubility in membrane. The cells were suspended in the modified Tyrode's buffer containing 0.1% dextrose, 0.2% of bovine serum albumin and without calcium. The SEM study showed that platelet changed shape from disc to ellipsoid in 10 μM TFP.,Increasingthe TFP concentration from 20 μM to 50 μM resulted in changing thecell from ellipsoid to sphere with a wavy surface. The drug did not cause any significant change in the cell volume. TFPof 70 μM caused platelet becoming a round ball shape with a spongy-like cell surface. 100 μM TFP caused more than 90% of cells to lyse and to agglutinate with each other. The time courseof morphological change of the TFP-affected platelets showed that the cellsswelled into irregular shape within 2 min. Apparent leakiness of serotonin was observed at 20 μM TFP, while the leakages of both lactate dehydrogenase and acid hydrolase were found at 40 μM TFP. The TFP uptake study showed that platelet was permeable to TFP by simple diffusion. The partition coefficient of TFP in platelet membrane was estimated to be 1 x 104. These results indicate that TFP molecules are solubilized in membrane. The extent in perturbation of the membrane structure depends on concentration of the drug used. (This research was supported by a grant from the National Science Council of the Republic of China.)
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