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Academic literature on the topic 'Optimization of protease'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "Optimization of protease"

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Chourasia, P., B. Patel, M. M. Prakash, and S. Gaherwal. "Screening and Optimization of Extracellular Alkaline Protease Production from Bacillus Spp." Environment Conservation Journal 13, no. 3 (December 20, 2012): 49–52. http://dx.doi.org/10.36953/ecj.2012.130309.

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Protease enzyme catalyzes the hydrolysis of protein. Among the various proteases, bacterial proteases are most significant when compared with animal and fungal proteases. In the present study a protease producing bacteria were isolated from soil collected from Govt. Holkar Science College, Indore campus and identified as Bacillus spp. They were grown within a temperature range between 25°C & 45 °C and pH range of 6.0 to 11.0. The optimum condition for protease production obtained was 35 °C at pH 9. The best carbon and organic nitrogen sources for this bacterial strain were fructose and yeast extract, respectively, while the most effective inorganic nitrogen sources was urea. It is envisaged that the isolate can be a potential source of alkaline protease for use as additive in industrial applications like detergent industry.

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Patra, Madhumita Dandopath. "Rational Lead Optimization Based on the Modeled Structure of Cysteine Protease of Leishmania donovani." Asian Journal of Organic & Medicinal Chemistry 4, no. 4 (2019): 256–66. http://dx.doi.org/10.14233/ajomc.2019.ajomc-p239.

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In present study, the molecular modeling techniques were applied to generate a refined model of a cysteine protease of Leishmania donovani using the crystal structure of a homologous protease and used for lead optimization. The structures of a series of complexes of the protease with the designed inhibitors were predicted using a novel docking technique comprising of repeated cycles of molecular dynamics and energy minimization. Calculation of the free energies of binding of the model with the designed inhibitors suggested that three compounds can form stable complexes with dissociation constants in the nanomolar range (0.038-1.41 nM). Search in the human genome revealed that a number of proteases of the cathepsin family had high homology with the parasite protease with amino acid identity around 45 %. The X-ray structures of all these were available in the protein data bank. The structures of the complexes of the selected inhibitors with a few homologous human proteases of known 3-D structures were also predicted using the same technique of optimization. The electrostatic potentials around the binding sites of the proteases were highly negative, which served as a clue for the introduction of positively charged groups in the designed inhibitors for higher affinity. The comparison of interaction energies and hydrogen bonding patterns among these complexes and similar complexes with homologous human proteases allowed us to short-listed three molecules as effective antileishmanial cysteine protease inhibitors.

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Ferrall-Fairbanks, Meghan C., Chris A. Kieslich, and Manu O. Platt. "Reassessing enzyme kinetics: Considering protease-as-substrate interactions in proteolytic networks." Proceedings of the National Academy of Sciences 117, no. 6 (January 24, 2020): 3307–18. http://dx.doi.org/10.1073/pnas.1912207117.

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Enzymes are catalysts in biochemical reactions that, by definition, increase rates of reactions without being altered or destroyed. However, when that enzyme is a protease, a subclass of enzymes that hydrolyze other proteins, and that protease is in a multiprotease system, protease-as-substrate dynamics must be included, challenging assumptions of enzyme inertness, shifting kinetic predictions of that system. Protease-on-protease inactivating hydrolysis can alter predicted protease concentrations used to determine pharmaceutical dosing strategies. Cysteine cathepsins are proteases capable of cathepsin cannibalism, where one cathepsin hydrolyzes another with substrate present, and misunderstanding of these dynamics may cause miscalculations of multiple proteases working in one proteolytic network of interactions occurring in a defined compartment. Once rates for individual protease-on-protease binding and catalysis are determined, proteolytic network dynamics can be explored using computational models of cooperative/competitive degradation by multiple proteases in one system, while simultaneously incorporating substrate cleavage. During parameter optimization, it was revealed that additional distraction reactions, where inactivated proteases become competitive inhibitors to remaining, active proteases, occurred, introducing another network reaction node. Taken together, improved predictions of substrate degradation in a multiple protease network were achieved after including reaction terms of autodigestion, inactivation, cannibalism, and distraction, altering kinetic considerations from other enzymatic systems, since enzyme can be lost to proteolytic degradation. We compiled and encoded these dynamics into an online platform (https://plattlab.shinyapps.io/catKLS/) for individual users to test hypotheses of specific perturbations to multiple cathepsins, substrates, and inhibitors, and predict shifts in proteolytic network reactions and system dynamics.

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Mostafa, El-Sayed E., Moataza M. Saad, Hassan M. Awad, Mohsen H. Selim, and Helmy M. Hassan. "Optimization Conditions of Extracellular Proteases Production from a Newly IsolatedStreptomyces PseudogrisiolusNRC-15." E-Journal of Chemistry 9, no. 2 (2012): 949–61. http://dx.doi.org/10.1155/2012/168540.

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Microbial protease represents the most important industrial enzymes, which have an active role in biotechnological processes. The objective of this study was to isolate new strain ofStreptomycesthat produce proteolytic enzymes with novel properties and the development of the low-cost medium. An alkaline protease producer strain NRC-15 was isolated from Egyptian soil sample. The cultural, morphological, physiological characters and chemotaxonomic evidence strongly indicated that the NRC-15 strain represents a novel species of the genusStreptomyces, hence the nameStrptomyces pseudogrisiolusNRC-15. The culture conditions for higher protease production by NRC-15 were optimized with respect to carbon and nitrogen sources, metal ions, pH and temperature. Maximum protease production was obtained in the medium supplemented with 1% glucose, 1% yeast extract, 6% NaCl and 100 μmol/L of Tween 20, initial pH 9.0 at 50 °C for 96 h. The current results confirm that for this strain, a great ability to produce alkaline proteases, which supports the use of applications in industry.

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Alias, Norsyuhada, Mu’adz Ahmad Mazian, Abu Bakar Salleh, Mahiran Basri, and Raja Noor Zaliha Raja Abd Rahman. "Molecular Cloning and Optimization for High Level Expression of Cold-Adapted Serine Protease from Antarctic Yeast Glaciozyma antarctica PI12." Enzyme Research 2014 (June 30, 2014): 1–20. http://dx.doi.org/10.1155/2014/197938.

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Psychrophilic basidiomycete yeast, Glaciozyma antarctica strain PI12, was shown to be a protease-producer. Isolation of the PI12 protease gene from genomic and mRNA sequences allowed determination of 19 exons and 18 introns. Full-length cDNA of PI12 protease gene was amplified by rapid amplification of cDNA ends (RACE) strategy with an open reading frame (ORF) of 2892 bp, coded for 963 amino acids. PI12 protease showed low homology with the subtilisin-like protease from fungus Rhodosporidium toruloides (42% identity) and no homology to other psychrophilic proteases. The gene encoding mature PI12 protease was cloned into Pichia pastoris expression vector, pPIC9, and positioned under the induction of methanol-alcohol oxidase (AOX) promoter. The recombinant PI12 protease was efficiently secreted into the culture medium driven by the Saccharomyces cerevisiae α-factor signal sequence. The highest protease production (28.3 U/ml) was obtained from P. pastoris GS115 host (GpPro2) at 20°C after 72 hours of postinduction time with 0.5% (v/v) of methanol inducer. The expressed protein was detected by SDS-PAGE and activity staining with a molecular weight of 99 kDa.

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Usman, Abdilbar, Said Mohammed, and Jermen Mamo. "Production, Optimization, and Characterization of an Acid Protease from a Filamentous Fungus by Solid-State Fermentation." International Journal of Microbiology 2021 (April 29, 2021): 1–12. http://dx.doi.org/10.1155/2021/6685963.

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Acid proteases represent an important group of enzymes, extensively used in food and beverage industries. There is an increased demand for acid proteases adapting to the industrial extreme environment, especially lower pH. Thus, this necessitates the search for a better acid protease from fungi that best performs in industrial conditions. The fungal isolates were isolated from grape and dairy farm soil using potato dextrose agar and further screened for protease production based on the hydrolysis of clear zone on skim milk agar. The potential fungi were then subjected to secondary screening under solid-state fermentation (SSF). After the secondary screening, the potential fungus was identified to the genus level by the macroscopic and microscopic methods. The growth conditions and media composition for the potential fungus were further optimized under SSF. The crude enzyme produced by the potential isolate was characterized after partial purification by acetone and ammonium sulfate precipitation. A total of 9 fungal isolates showed protease production in primary and secondary screening; however, one potential isolate (Z1BL1) was selected for further study based on its protease activity. The isolate was identified to the genus Aspergillus based on their morphological features. The maximum acid protease from the isolate Z1BL1 was obtained using fermentation media containing wheat bran as a solid substrate, 1 mL of 3.2 × 106 inoculum size, 50% moisture content, and pH 4.5 upon 120-h incubation at 30°C. The acetone-precipitated enzyme exhibited the maximum activity at 50°C and pH 5 with stability at pH 4–6 and temperature 40–60°C. Thus, the acid protease produced from Aspergillus showed suitable enzyme characteristics required in the industry and could be a candidate for application in the food industry after further purification.

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Hashmi, Sidra, Sajid Iqbal, Iftikhar Ahmed, and Hussnain Ahmed Janjua. "Production, Optimization, and Partial Purification of Alkali-Thermotolerant Proteases from Newly Isolated Bacillus subtilis S1 and Bacillus amyloliquefaciens KSM12." Processes 10, no. 6 (May 25, 2022): 1050. http://dx.doi.org/10.3390/pr10061050.

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Proteases that can remain active under extreme conditions such as high temperature, pH, and salt concentration are widely applicable in the commercial sector. The majority of the proteases are rendered useless under harsh conditions in industries. Therefore, there is a need to search for new proteases that can tolerate and function in harsh conditions, thus improving their commercial value. In this study, 142 bacterial isolates were isolated from diverse alkaline soil habitats. The two highest protease-producing bacterial isolates were identified as Bacillus subtilis S1 and Bacillus amyloliquefaciens KSM12, respectively, based on 16S rRNA sequencing. Optimal protease production was detected at pH 8, 37 °C, 48 h, 5% (w/v) NaCl for Bacillus subtilis S1 (99.8 U/mL) and pH 9, 37 °C, 72 h, 10% (w/v) NaCl for Bacillus amyloliquefaciens KSM12 (94.6 U/mL). The molecular weight of these partially purified proteases was then assessed on SDS-PAGE (17 kDa for Bacillus subtilis S1 and 65 kDa for Bacillus amyloliquefaciens KSM12), respectively. The maximum protease activity for Bacillus subtilis S1 was detected at pH 8, 40 °C, and for Bacillus amyloliquefaciens KSM12 at pH 9, 60 °C. These results suggest that the proteases secreted by Bacillus subtilis S1 and Bacillus amyloliquefaciens KSM12 are suitable for industries working in a highly alkaline environment.

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CAI, KANGTAO, HUAYOU CHEN, XINYU HENG, LINGYU KANG, JUNMING WU, CHENXI LU, and XIAOYU LIANG. "Optimization of Small Peptide Feed from Milk Thistle Residue by Synergistic Fermentation of Multiple Strains and Proteases." Romanian Biotechnological Letters 26, no. 6 (December 30, 2021): 3102–9. http://dx.doi.org/10.25083/rbl/26.6/3102-3109.

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In order to improve the utilization rate of the milk thistle residue, this study used the synergistic fermentation of multiple strains and proteases to increase the small peptide content of the fermented feed produced by the milk thistle residue. Taking the small peptide content of the milk thistle residue fermented feed as an indicator, the optimal fermentation process was obtained by single-factor optimization experiments and the response surface methodology. The optimal fermentation process was as follows: fermentation time of 7 days, inoculum size of 15%, inoculation ratio of aerobic strains: anaerobic strains = 1: 2, solid-state fermentation water content of 66%, fermentation temperature of 36℃, and amount of protease was 0.25% acid protease+0.25% bromelain. Under the above process, the small peptide content of the fermented feed from milk thistle residue was greatly improved to 57.86%. These results inferred that the added proteases were beneficial to the growth of fermentative microorganisms, the secretion of protease and the increase of the small peptide content.

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Maheswari, P., S. Mahendran, and A. Kamilabanu. "Isolation and Optimization of Protease Producing Bacteria from Marine Sediment." International Journal of Trend in Scientific Research and Development Volume-2, Issue-3 (April 30, 2018): 122–32. http://dx.doi.org/10.31142/ijtsrd9674.

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Braaksma, Machtelt, Age K. Smilde, Mariët J. van der Werf, and Peter J. Punt. "The effect of environmental conditions on extracellular protease activity in controlled fermentations of Aspergillus niger." Microbiology 155, no. 10 (October 1, 2009): 3430–39. http://dx.doi.org/10.1099/mic.0.031062-0.

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Proteolytic degradation by host proteases is one of the key issues in the application of filamentous fungi for non-fungal protein production. In this study the influence of several environmental factors on the production of extracellular proteases of Aspergillus niger was investigated systematically in controlled batch cultures. Of all factors investigated in a series of initial screening experiments, culture pH and nitrogen concentration in particular strongly affected extracellular protease activities. For instance, at a culture pH of 4, protease activity was higher than at pH 5, and protease activity increased with increasing concentrations of ammonium as nitrogen source. Interestingly, an interdependence was observed for several of the factors studied. These possible interaction effects were investigated further using a full factorial experimental design. Amongst others, the results showed a clear interaction effect between nitrogen source and nitrogen concentration. Based on the observed interactions, the selection of environmental factors to reduce protease activity is not straightforward, as unexpected antagonistic or synergistic effects occur. Furthermore, not only were the effects of the process parameters on maximum protease activity investigated, but five other protease-related phenotypes were studied as well, such as maximum specific protease activity and maximum protease productivity. There were significant differences in the effect of the environmental parameters on the various protease-related phenotypes. For instance, pH significantly affected final levels of protease activity, but not protease productivity. The results obtained in this study are important for the optimization of A. niger for protein production.

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Dissertations / Theses on the topic "Optimization of protease"

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Peterson, Shane. "Improved CoMFA Modeling by Optimization of Settings : Toward the Design of Inhibitors of the HCV NS3 Protease." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-8140.

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De, Wet Tinus Andre. "Laboratory optimization of a protease extraction and purification process from bovine pancreas in preparation for industrial scale up." Thesis, Stellenbosch : Stellenbosch University, 2012. http://hdl.handle.net/10019.1/71790.

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Thesis (MSc)--Stellenbosch University, 2012.
ENGLISH ABSTRACT: This study describes: a) Characterization of traditional methodologies and testing methods used to purify and quantify trypsin and α-chymotrypsin b) Re-engineering / development of a new method for purifying trypsin and α-chymotrypsin that delivered higher product yields and improved control exercised over the process by investigating: i. Extraction methods ii. Centrifugation iii. Ultrafiltration iv. Chymotrypsinogen and trypsin crystallization v. Column chromatography vi. Investigation into different raw material sources for pancreatic enzyme production c) Development of kinetic and ELISA testing methodologies for in-process QC analysis.
AFRIKAANSE OPSOMMING: Hierdie Studie beskryf: a) Karakterisering van die ou prosessering metodes en toets metodes wat gebruik word om Tripsien en Alpha-chimotripsien te suiwer en te kwantifiseer. b) Herontwerp / ontwikkeling van 'n nuwe metode vir die suiwering Tripsien en Chimotripsien wat „n hoër opbrengs lewer en meer kontrole oor die proses uit oefen deur ondersoek in te stel na: i. Ekstraksie- metodes ii. Sentrifugering iii. Ultrafiltrasie iv. Chymotripsienogeen - en tripsien kristallisasie v. Kolom chromatografie vi. Ondersoek na verskillende rou materiaal bronne vir die produksie van pankreas ensieme. c) Die ontwikkeling van kinetiese- en ELISA toets metodes vir die in-proses kwaliteitkontrole.

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Wang, Liping. "Enhanced Production of Heterologous Protein by Recombinant Aspergillus niger Through Bioprocessing Strategies in Submerged Culture." Ohio University / OhioLINK, 2002. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1038425153.

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Souza, Paula Monteiro de. "Produção de proteases por fungos filamentosos isolados do cerrado do centro-oeste brasileiro." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/9/9134/tde-15052015-134608/.

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Proteases ácidas pertencem a um importante grupo de enzimas industriais produzidas por fungos filamentosos, com aplicações na indústria de alimentos, de couro, farmacêutica e de cosméticos. O objetivo principal deste trabalho foi avaliar a produção de proteases ácidas extracelulares de fungos filamentosos isolados do solo do cerrado do centro-oeste brasileiro. Inicialmente, foi realizada uma triagem para avaliar a capacidade de 17 linhagens de fungos quanto à produção de protease em meio de cultura contendo Agar-leite. O fungo Aspergillus foetidus foi selecionado como melhor produtor de protease ácida extracelular. Visando à otimização da produção de proteases pelo fungo selecionado, avaliou-se a influência de diversos fatores no cultivo (pH, temperatura, agitação e diferentes fontes de nitrogênio e carbono). Após essa etapa, um planejamento experimental estatístico foi realizado com as variáveis independentes temperatura, pH inicial do meio e fonte de carbono e nitrogênio. A produção máxima de protease foi encontrada (63,7 U/mL) nas condições: pH inicial do meio igual a 7,0 a 28 ºC, 150 rpm em peptona 2% (p/v). Os estudos em biorreator demonstraram produção de protease nas condições de agitação e aeração iguais à 300 rpm e 1,0 vvm, após 120 h de cultivo. Os ensaios com diferentes temperaturas para a estimativa dos parâmetros termodinâmicos demonstraram que a protease ácida produzida pelo fungo é altamente estável apresentando máxima atividade em pH 5,0 e temperatura ótima igual a 55ºC. E, finalmente, para a purificação da enzima foi realizada cromatografia de gel-filtração. A enzima apresentou massa molecular de 50,6 kDa, e a análise do zimograma confirmou a atividade proteolítica. Além disso, a protease purificada foi inibida pelo composto pepstatina, indicando uma característica de protease ácida. Esses resultados obtidos demonstram um fungo filamentoso produtor de uma nova protease ácida com potencial aplicação para indústria farmacêutica e de cosméticos.
The acid proteases belong to the most important group of industrial enzymes produced by filamentous fungi, with applications in the food, leather, pharmaceutical and cosmetics industries. This study aimed the evaluation of extracellular acid proteases production from filamentous fungi isolated from different samples of the midwestern Brazil cerrado. Initially, a screening was performed to assess the ability of the 17 strains of yeast for production of protease-agar medium containing milk culture. The Aspergillus foetidus was selected as the best producer. Aimed at optimizing the production of proteases by the selected fungus, first evaluated the influence of various factors on the cultivation (pH, temperatura, agitation and different sources of nitrogen and carbon). After this step, a statistical experimental design was carried out with the independent variables temperatura, initial pH of the medium and source of carbon and nitrogen. The best conditions for protease production were (63.7 U / mL): initial pH values greater than 7.0, at 28 °C, 150 rpm peptone 2% (w/v). Aiming future production of this protease in industrial scale, studies have shown better in bioreactor protease production under the conditions of agitation and aeration equal to 300 rpm and 1.0 vvm, after 120 h of cultive. The tests at different temperaturas to estimate the thermodynamic parameters showed that the acid protease produced by the fungus is highly stable with maximum activity at pH 5.0 and optimum temperatura of 55 °C. And finally, for the purification of the enzyme were performed gel-filtration chromatography. The enzyme had a molecular mass of 50.6 kDa, and the analysis of the zymogram showed a proteolytic band. Furthermore, the purified protease was inhibited by pepstatin compound, indicating a feature of acid protease. These results demonstrate a new filamentous fungus producing acid protease with potential application to pharmaceuticals and cosmetics.

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Bourscheid, Cristiane. "OTIMIZAÇÃO DO PROCESSO DE HIDRÓLISE ENZIMÁTICA DE COPRODUTO DA DESOSSA DE FRANGO E APLICAÇÃO DO HIDROLISADO EM HAMBÚRGUER." UNIVERSIDADE ESTADUAL DE PONTA GROSSA, 2015. http://tede2.uepg.br/jspui/handle/prefix/645.

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Made available in DSpace on 2017-07-21T18:53:04Z (GMT). No. of bitstreams: 1 CRISTIANE BOURSCHEID.pdf: 1448163 bytes, checksum: 21f79c9c1335f39830bfef99ee3f5f19 (MD5) Previous issue date: 2015-03-11
The chicken slaughterhouse generate co-products during slaughter, for example, feathers, bones, blood and guts, usually intended for animal feed with low added value. In bone part of the meat remains bound even after deboning and is a good source of substrate for the enzymatic hydrolysis. The protein hydrolysates may be applied as a nutritional supplement in foods. Given this context, the objective was to optimize the enzymatic hydrolysis process for obtaining protein hydrolyzate coproduct of chicken bones (Gallus gallus domesticus) and the addition of the hydrolyzate as a protein supplement in burger. The co-product selected to carry out the work was thigh and drumstick bone from the chicken bones in a slaughterhouse. The study was conducted in two stages. In the first one a central composite design (CCRD), a total of 17 tests was adopted to evaluate the influence of temperature, enzyme: substrate ratio and time on the degree of hydrolysis. Following the statistical optimization was performed to obtain the best conditions of enzymatic hydrolysis of co-product of chicken bones. The co-product of chicken bones and the optimized protein hydrolyzate were characterized in terms of chemical composition, total amino acids and pattern. In the second step, the hydrolyzate was added as a protein supplement in poultry burger, where two formulations were prepared, Hamburger control (no addition of protein hydrolyzate) and hamburger with hydrolyzed (with addition of 8% protein hydrolyzate). The burgers were characterized in terms of physical-chemical, microbiological and sensory analysis. The optimum conditions for the enzymatic hydrolysis were temperature (T) of 50 ° C, enzyme: substrate ratio (E:S) from 4.96% to time (t) of 110.16 minutes under these conditions the degree of hydrolysis was 24, 0.22 ± 21%. The protein hydrolyzate has the potential to supplementation in food, it is good source of essential amino acids, meeting the recommendations established by FAO / WHO, except for leucine, phenylalanine, and valine, and had a higher concentration of protein fractions from 14.437 kDa and 3,496 kDa. The results obtained for microbiological analysis and physical-chemical analysis of the burger control and burger with hydrolyzed, are in accordance with the respective standards set by law. The burger with hydrolyzate showed 1.02% more protein than the burger control, giving a protein supplementation to the product developed. In the sensorial analysis for flavor attribute evaluators preferred the burger with protein hydrolyzate. The burger with protein hydrolyzate and the burger control achieved 84.2% and 81.8% of general acceptance, respectively. The intention to buy for the burger with added protein hydrolyzate was 76.4% and for the burger control was 67%. In this light, the protein hydrolyzate obtained from chicken bones of the co-product is an alternative to supplementation in foods, as well as add value to the co-product of chicken dessosa and increase the competitiveness of slaughterhouse.
Os frigoríficos de frango geram coprodutos durante o abate, por exemplo, penas, ossos, sangue e vísceras, geralmente, destinados para ração animal com baixo valor agregado. Uma parte de carne permanece aderida aos ossos, mesmo após a desossa, sendo uma boa fonte de substrato para a hidrólise enzimática. Os hidrolisados proteicos podem ser aplicados como suplemento nutricional em alimentos. Diante desse contexto, o objetivo do trabalho foi otimizar o processo de hidrólise enzimática para obtenção de hidrolisado proteico de coproduto da desossa de frango (Gallus gallus domesticus) e a adição do hidrolisado como suplemento proteico em hambúrguer. O coproduto selecionado para realização do trabalho foi osso de coxa e sobrecoxa proveniente da desossa de frango em frigorífico. O trabalho foi realizado em duas etapas. Na primeira um delineamento composto central rotacional (DCCR), totalizando 17 ensaios foi adotado para avaliar a influência da temperatura, relação enzima:substrato e tempo sobre o grau de hidrólise. Na sequência, foi realizada a otimização estatística para obter as melhores condições da hidrólise enzimática. O coproduto da desossa de frango e o hidrolisado proteico otimizado foram caracterizados em termos de composição centesimal, aminoácidos totais e perfil eletroforético. Na segunda etapa, o hidrolisado foi adicionado como suplemento proteico em hambúrguer de frango. Foram elaboradas duas formulações, hambúrguer controle (sem adição de hidrolisado proteico) e hambúrguer com hidrolisado (com adição de 8% de hidrolisado proteico). Os hambúrgueres foram caracterizados em termos de análises físico-químicas, análises microbiológicas e análise sensorial. As condições ótimas para a hidrólise enzimática foram temperatura (T) de 50ºC, relação enzima:substrato (E:S) de 4,96% e tempo (t) de 110,16 minutos, nessas condições o grau de hidrólise foi de 24,21% ±0,22. O hidrolisado proteico apresentou potencial para suplementação em alimentos, pois é boa fonte de aminoácidos essenciais, atendendo as recomendações estabelecidas pela FAO/WHO, exceto para leucina, fenilalanina e valina, bem como apresentou maior concentração de frações proteicas entre 14,437 kDa e 3,496 kDa. Os resultados obtidos para a análise microbiológica e análises físico-químicas do hambúrguer controle e do hambúrguer com hidrolisado, estão de acordo com os respectivos padrões estabelecidos pela legislação vigente. O hambúrguer com hidrolisado apresentou 6% mais proteína do que o hambúrguer controle, conferindo uma suplementação proteica ao produto desenvolvido. Em relação à análise sensorial para o atributo sabor, os avaliadores preferiram o hambúrguer com hidrolisado proteico. O hambúrguer com hidrolisado proteico e o hambúrguer controle obtiveram 84,2% e 81,8% de aceitação geral, respectivamente. A intenção de compra para o hambúrguer com adição de hidrolisado proteico foi de 76,4% e para o hambúrguer controle foi de 67%. Diante do exposto, o hidrolisado proteico obtido a partir de coproduto da desossa de frango é uma alternativa para a suplementação em alimentos, além de agregar valor ao coproduto da dessosa de frango e aumentar a competitividade dos frigoríficos.

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Stewart, Gaynelle. "Engineering Saccharomyces ceresisiae for the Secretion of an Extracellular Lipase." ScholarWorks@UNO, 2007. http://scholarworks.uno.edu/td/577.

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Developing microbial systems capable of converting low cost lipids into value added products depends on the ability to acquire substrates from the growth media. Saccharomyces cerevisiae can acquire free fatty acids from the growth media and a portion of these lipids can be converted into new lipid products. However, they cannot acquire complex lipids from the growth media unless a nonspecific lipase is included. To circumvent lipase addition, we are genetically engineering S. cerevisiae to secrete a lipase into the growth media. We selected the LIP2 gene from Yarrowia lipolytica, which encodes a nonspecific lipase. Several modifications were made to the LIP2 gene to improve processing. Results identified strains secreting the most lipase. From these results, high producing strains were inserted into an oil inducible vector. Halo assays confirmed lipase secretion, while measuring the fatty acid composition confirmed triacylglycerol breakdown, and yeast uptake of the free fatty acids released.

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Lalanne, Jean-Benoît. "Multiscale dissection of bacterial proteome optimization." Thesis, Massachusetts Institute of Technology, 2020. https://hdl.handle.net/1721.1/130217.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Physics, May, 2020
Cataloged from student-submitted PDF version of thesis.
Includes bibliographical references (pages 315-348).
The quantitative composition of proteomes results from biophysical and biochemical selective pressures acting under system-level resource allocation constraints. The nature and strength of these evolutionary driving forces remain obscure. Through the development of analytical tools and precision measurement platforms spanning biological scales, we found evidence of optimization in bacterial gene expression programs. We compared protein synthesis rates across distant lineages and found tight conservation of in-pathway enzyme expression stoichiometry, suggesting generic selective pressures on expression setpoints. Beyond conservation, we used high-resolution transcriptomics to identify numerous examples of stoichiometry preserving cis-elements compensation in pathway operons. Genome-wide mapping of transcription termination sites also led to the discovery of a phylogenetically widespread mode of bacterial gene expression, 'runaway transcription', whereby RNA polymerases are functionally uncoupled from pioneering ribosomes on mRNAs. To delineate biophysical rationales underlying these pressures, we formulated a parsimonious ribosome allocation model capturing the trade-off between reaction flux and protein production cost. The model correctly predicts the expression hierarchy of key translation factors. We then directly measured the quantitative relationship between expression and fitness for specific translation factors in the Gram-positive species Bacillus subtilis. These precision measurements confirmed that endogenous expression maximizes growth rate. Idiosyncratic transcriptional changes in regulons were however observed away from endogenous expression. The resulting physiological burdens sharpened the fitness landscapes. Spurious system-level responses to targeted expression perturbations, called 'regulatory entrenchment', thus exacerbate the requirement for precisely set expression stoichiometry.
by Jean-Benoît Lalanne.
Ph. D.
Ph.D. Massachusetts Institute of Technology, Department of Physics

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Oliveira, Cibele Freitas de. "Estudo da hidrólise da proteína de soja utilizando proteases de Chryseobacterium sp. para o uso como antioxidante em alimentos." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2011. http://hdl.handle.net/10183/61061.

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A demanda por antioxidantes naturais vem aumentando devido à toxicidade de alguns antioxidantes sintéticos. Estudos vêm identificando antioxidantes de origem natural, como a proteína da soja, que é capaz de contribuir na melhoria de propriedades funcionais e biológicas de alimentos. A hidrólise enzimática da proteína de soja aumenta sua atividade antioxidante, assim como a capacidade emulsificante e a capacidade de formação de espuma. O objetivo deste trabalho foi o estudo da hidrólise da proteína de soja através de uma protease produzida por Chryseobacterium sp., a verificação da capacidade antioxidante e aplicação do hidrolisado em diferentes tipos de carnes para evitar a oxidação lipídica. A eficácia da hidrólise foi determinada através da proteína solúvel utilizando o método de Folin enquanto que a atividade antioxidante foi avaliada pelos métodos referentes à captura do radical DPPH e ABTS. Os hidrolisados foram adicionados em carne de porco e peixe e foi verificada a inibição da oxidação lipídica. A influência de três parâmetros (temperatura, pH, relação enzima/substrato) na hidrólise foi estudada através um experimento fatorial 23 . Como respostas foram avaliadas a atividade antioxidante (DPPH e ABTS), atividade quelante de ferro, proteína solúvel, capacidade de formação de espuma e capacidade emulsificante. Observou-se um aumento na concentração de proteína solúvel em função do tempo, sendo que os hidrolisados foram capazes de inibir tanto o radical DPPH quanto o ABTS. Os hidrolisados inibiram em parte a oxidação lipídica em carne suína e peixe. Ainda foi possível concluir que dependendo da finalidade para que se deseja o hidrolisado, diferentes condições devem ser utilizadas. Os resultados demonstram uma potencial aplicação da protease microbiana para gerar hidrolisados antioxidantes da proteína de soja.
The demand for natural antioxidants has been increasing due to the toxicity of some synthetic antioxidants. Studies have identified naturally occurring antioxidants, such as soy protein, which can contribute to improve functional and biological properties of food. Enzymatic hydrolysis of soy protein increases its antioxidant activity, as well as emulsifying capacity and foaming capacity. The purpose of this work was to study the hydrolysis of soy protein, verifying the antioxidant capacity, application of the hydrolysate in different types of meat and optimization of hydrolysis. The efficiency of hydrolysis was determined by the soluble protein by the method of Folin while the antioxidant activity was evaluated by the methods related to the capture of the radical DPPH and ABTS. The hydrolysates were added to pork and fish and the extent of lipid oxidation was determined by TBARS. In optimizing of the hydrolysis three parameters were varied (T, pH, enzyme substrate), it was applied to a surface response methodology for conducting trials using a 23 factorial experiment. As answers were evaluated antioxidant activity (DPPH and ABTS), iron chelating activity, Lowry, foaming capacity and emulsifying capacity. There was an increase in soluble protein concentration versus time, and the hydrolysates were able to inhibit both the ABTS and the DPPH radical. The hydrolysates were able of inhibit lipid oxidation in pork and fish. Was still possible to conclude that depending on the finality that will be given to hydrolysates different treatment conditions should be used. The results demonstrate a significant potential for application of microbial protease to generate antioxidants of hydrolyzed soy protein.

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Myhara, Robert Michael. "Optimization of cultural factors influencing the production of extracellular vesicles and proteinase by Pseudomonas fragi ATCC 4973." Thesis, University of British Columbia, 1989. http://hdl.handle.net/2429/29249.

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Pseudomonas fragi ATCC 4973 was grown in trypticase soy broth (TSB), on a trypticase soy broth + 1.5% agar (TSA) surface, and in a defined citrate broth. The citrate broth contained glutamine as the sole nitrogen source, Pseudomonas fragi grown in TSB started proteinase production at 24 h, during the late logarithmic early stationary growth phase. Pseudomonas fragi grown on TSA surfaces initiated proteinase production at 4 h, 20 hours earlier than in liquid medium. Electron micrographs of P. fragi grown on TSA revealed extracellular vesicles ca. 20 nm in diameter "blebbing" off the surface of the cells. These vesicles were absent from the surface of P. fragi cells grown in TSB, although vesicles could be isolated from the culture supernatant. Isolated extracellular vesicles were ca. 20 nm in diameter and contained a proteinase similar to that found in the supernatant. Electrophoretic analysis showed the vesicles and outer cell membrane of P. fragi to share similarities in their composition. Use of the centroid search technique of Aishima and Nakai, showed the optimum cultural conditions for proteinase production by P. fragi, in defined citrate broth to be: incubation temperature, 12.5 C; incubation time, 38 h; initial pH, 6.8; organic nitrogen concentration, 314 mmole nitrogen/L (glutamine); a gas mixture containing 16.4% oxygen flowing over the medium (7.42 ppm dissolved oxygen). Oxygen was the major factor influencing proteinase production by P. fragi. A comparison of optimization techniques suitable for microbiological experiments showed that the centroid search technique of Aishima and Nakai, the modified super simplex of Nakai and Kaneko and the simplex technique of Morgan and Deming all required similar time and experiment numbers to obtain the optimum point.
Land and Food Systems, Faculty of
Graduate

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Bayraktar, Eda. "Effects Of Ph On Human Growth Hormone Production By Pichia Pastoris Considering The Expression Levels Of Regulatory Genes." Master's thesis, METU, 2009. http://etd.lib.metu.edu.tr/upload/12610882/index.pdf.

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In this study, the aim was to investigate the effects of pH on therapeutically important protein, recombinant human growth hormone (rhGH), production by Pichia pastoris considering the expression levels of regulatory genes. In this frame, firstly the host microorganism was selected between two different methanol utilization phenotypes of P. pastoris, Mut+ and MutS on media containing glycerol/methanol or sorbitol/methanol. The highest rhGH production, 120 g L-1, and hGH gene expression, 9.84x109 copies mg-1 CDW, were achieved in the medium containing 30 g L-1 sorbitol and 1% (v/v) methanol by P. pastoris hGH-Mut+ strain. Thereafter, effects of pH on rhGH production and stability were investigated in laboratory scale bioreactors. RhGH was more stable at pH 5.0. Throughout the production, it is seen that medium of pH decreased. Thereafter, effects of pH on rhGH were investigated in pH controlled pilot-scale bioreactor. In addition to rhGH concentration, AOX intracellular enzyme activity, extracellular proteases concentrations
expression levels of hGH, AOX, pep4, prb1 and prc1 genes were determined. The highest cell concentration was obtained as 53 g L-1 at pH 6.0 but hGH concentration was found as 24 mg L-1 at t=24 h. The highest rhGH concentration was obtained as 271 g L-1 with 42 g L-1 cell density at pH 5.0 in medium containing sorbitol at t=24 h. At this condition, the overall product and cell yield on total substrate were found as 2.08 mg g-1 and 0.15 g g-1. Furthermore, the highest expression levels of hGH and AOX were attained at pH 5.0. Moreover, by keeping pH at 5.0, expression levels of three types of vacuolar proteases were minimized.

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Books on the topic "Optimization of protease"

1

Chiang, Jason. Proteine-based fluorescence resonance energy transfer biosensors: Design, simulation, and optimization. 2006, 2006.

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Book chapters on the topic "Optimization of protease"

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Dauber, Deborah S., Fiona McPhee, Ayçe Ünal, and Charles S. Craik. "Optimization of a Macromolecular Inhibitor of HIV-1 Protease." In Aspartic Proteinases, 65–70. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5373-1_9.

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Nakai, S., S. Nakamura, and M. Ogawa. "Computer-Aided Optimization of Site-Directed Mutagenesis ofBacillus stearothermophilusNeutral Protease for Improving Thermostability." In ACS Symposium Series, 19–35. Washington, DC: American Chemical Society, 1998. http://dx.doi.org/10.1021/bk-1998-0708.ch002.

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Malathi, S., D. Mohana Priya, and P. Palani. "Optimization of Protease Enzyme Production by the Halo-Tolerant Vibrio alginolyticus Isolated from Marine Sources." In Microbial Diversity and Biotechnology in Food Security, 451–62. New Delhi: Springer India, 2014. http://dx.doi.org/10.1007/978-81-322-1801-2_40.

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Bayer, E., L. Zhang, W. Rapp, and D. Waidelich. "Optimization of fast continuous flow protein synthesis using new analytical techniques on the example of HIV-1 protease sequence 59–99." In Peptides 1990, 352–55. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_149.

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Susanti, E., Suharti, R. A. Wahab, N. D. Sari, and J. Firdaus. "Production and optimization of protease from Bacillus Sp. HTcUM7.1 in the process of extracting collagen from milkfish scales as part of the efforts to support the availability of halal collagen in Indonesia." In Halal Development: Trends, Opportunities and Challenges, 45–50. London: Routledge, 2021. http://dx.doi.org/10.1201/9781003189282-8.

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Olineka, Tammi L., Apostolos Spiropoulos, Paula A. Mara, and Linda F. Bisson. "Optimization of Proteome Analysis for Wine Yeast Strains." In Microbial Processes and Products, 345–68. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-847-1:345.

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Fung, Jia Jun, Karla Blöcher-Juárez, and Anton Khmelinskii. "High-Throughput Analysis of Protein Turnover with Tandem Fluorescent Protein Timers." In Methods in Molecular Biology, 85–100. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1732-8_6.

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AbstractTandem fluorescent protein timers (tFTs) are versatile reporters of protein dynamics. A tFT consists of two fluorescent proteins with different maturation kinetics and provides a ratiometric readout of protein age, which can be exploited to follow intracellular trafficking, inheritance and turnover of tFT-tagged proteins. Here, we detail a protocol for high-throughput analysis of protein turnover with tFTs in yeast using fluorescence measurements of ordered colony arrays. We describe guidelines on optimization of experimental design with regard to the layout of colony arrays, growth conditions, and instrument choice. Combined with semi-automated genetic crossing using synthetic genetic array (SGA) methodology and high-throughput protein tagging with SWAp-Tag (SWAT) libraries, this approach can be used to compare protein turnover across the proteome and to identify regulators of protein turnover genome-wide.

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Janetka, James W., and Robert A. Galemmo. "Inhibitors of the Growth-Factor Activating Proteases Matriptase, Hepsin and HGFA: Strategies for Rational Drug Design and Optimization." In Extracellular Targeting of Cell Signaling in Cancer, 247–75. Chichester, UK: John Wiley & Sons, Ltd, 2018. http://dx.doi.org/10.1002/9781119300229.ch9.

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S Mainkar, Prathama, Surender Singh Jadav, and Kiranmai Nayani. "Peptidomimetics: Current and Future Perspectives on HIV Protease Inhibitors." In Advances in Organic Synthesis, 174–290. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815040524122170007.

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The peptidomimetic-based design and synthesis of HIV-1 protease and other entry inhibitors are generally oriented to block the viral receptor functionalities in the host cells. Most of the drugs classified under HIV-1 protease inhibitors are primarily optimized through substrate-based design strategies. The peptidomimetic drugs present in the market are non-hydrolyzable by the catalytic aspartic acid residues, an indispensable approach still used in designing potential pharmacophores for protease inhibitors. Thus, a variety of amino acid-containing hybrid small molecules are tested against the HIV-1 protease enzyme by incorporating essential fragments required to block protease functionalities. However, the appearance of mutations in HIV polyproteins is a key parameter to be seriously considered while designing peptidomimetics. Hence, comprehensive knowledge regarding HIV peptidomimetic/medicinal chemistry along with optimization strategy and organic synthesis awareness is critical in the current scenario. The present chapter is aimed to provide in-depth literature on medicinally optimized HIV-1 protease inhibitors, Tat TAR RNA blockers with their synthesis, and later it is expanded to the peptidomimetics (entry inhibitors) involved in the envelope glycoprotein (gp120/gp41) and capsid inhibitors. Furthermore, the knowledge-based classification of HIV-1 protease inhibitors, anti-dimer agents, Tat-TAR RNA blockers, and entry inhibitors, along with their synthetic procedures, would serve as a single model template for scientific as well as academic research towards the development of anti-HIV peptidomimetics.

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Fguiri, Imen, Amel Sboui, Manel Ziadi, Naziha Ayeb, Samira Arroum, Mohamed Dbara, Mohamed Hammadi, and Touhami Khorchani. "Optimization of Camel Milk Cheese Processing Using Protease from Latex (Ficus carica)." In Research Aspects in Agriculture and Veterinary Science Vol. 5, 27–36. Book Publisher International (a part of SCIENCEDOMAIN International), 2022. http://dx.doi.org/10.9734/bpi/raavs/v5/14538d.

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Conference papers on the topic "Optimization of protease"

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Novitasari, Dian Putri, Suharti Suharti, and Evi Susanti. "Optimization production of crude extract protease from Bacillus megaterium TR-10." In THE 5TH INTERNATIONAL CONFERENCE ON MATERIALS ENGINEERING AND NANOTECHNOLOGY (ICMEN 2021). AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0133667.

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Ochoa, Rodrigo, and Pilar Cossio. "Protocol for the Computational Optimization of Modified Peptides as Potential Protease Inhibitors." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.233.

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Ochoa, Rodrigo, and Pilar Cossio. "Protocol for the Computational Optimization of Modified Peptides as Potential Protease Inhibitors." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps.2022.233.

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Zhang, Na, Qing Qi Guo, and Xin Huai Zhao. "Optimization of Liquid Culture Conditions of Protease from Mucor by Box-Behnken Design." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE 2010). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5515783.

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Yeh, Alice, and Wei-Chang Yeh. "Mining Classification Rules for HIV-1 Protease Cleavage Sites Using Simplified Swarm Optimization." In the 2019 International Conference. New York, New York, USA: ACM Press, 2019. http://dx.doi.org/10.1145/3358331.3358335.

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Miles, Linde A., John T. Poirier, and Charles M. Rudin. "Abstract 5675: Optimization of a Seneca Valley Virus (SVV) 3C protease substrate for virus-directed enzyme prodrug therapy." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5675.

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Solis-Calero, C., and HF Carvalho. "A molecular dynamics simulation study of interactions between aprotinin and transmembrane serine proteases TMPRSS2 and prostasin." In VIII Simpósio de Estrutura Eletrônica e Dinâmica Molecular. Universidade de Brasília, 2020. http://dx.doi.org/10.21826/viiiseedmol2020186.

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Aprotinin is a small protein, which inhibits trypsin and related proteolytic enzymes, it has been shown experimentally that it can inhibit SARS-CoV-2 replication.However, the molecular mechanisms relate to it are not totally known. TMPRSS2 is a human transmembrane serine protease which is important for viral spread and pathogenesis. In the current study, we use homology modeling for obtaining an initial structure of the complex between aprotinin and TMPRSS2, having as template the crystallographic structure of the complex between aprotinin and prostasin, other transmembrane serine protease which is related to other processes such as the regulation of hypertension. The binding modes of both complexes were predicted based on initial geometry optimization, and molecular dynamic simulations, calculating MM/PBSA and MM/GBSA free-energy calculations after the simulations. The calculated binding free energies suggested a better affinity of TMPRSS2 to aprotinin than prostasin. Moreover, hydrogen bond analyses along the trajectory simulation showed that the hydrogen-bond networks between TMPRSS2 and aprotinin are more stable than the corresponding to prostasin and aprotinin which explain their higher binding free energies. Additionally, in order to elucidate the different contributions of KLK14 residues to the free energy of binding, MM/GBSA free-energy decomposition analyses were performed. Based on their results, Glu97, Glu144H, Asp189 and Ser190 residues have been postulated as TMPRSS2 potential hotspots for its binding to aprotinin and by extension to other possible inhibitors.

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Mechri, Sondes, Bassem Jaouadi, Khelifa Bouacem, Mouna Kriaa, Alif Chebbi, Sami Sayadi, Mohamed Chamkha, Amel Bouanane-Darenfed, and Hocine Hacene. "Protease production from <em>Lysinibacillus fusiformis</em> strain C250R: Statistical optimization and compatibility study for use in detergent formulations." In MOL2NET'21, Conference on Molecular, Biomedical & Computational Sciences and Engineering, 7th ed. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/mol2net-07-09542.

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Haidoury, Mohamed, Aziz El Fatimi, Hatim Jbari, and Mohammed Rachidi. "Modeling of Fuel Cell by using Proteus." In 2022 IEEE 3rd International Conference on Electronics, Control, Optimization and Computer Science (ICECOCS). IEEE, 2022. http://dx.doi.org/10.1109/icecocs55148.2022.9983222.

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Begum, Fatema, Krishna Mridha, Md Golam Rabbani, Shamin Ashfaq, S. MD Iftekhar Islam, and Sapna Sinha. "Bioactivity classification of SARS-CoV-2 Proteinase using Machine Learning Approaches." In 2022 10th International Conference on Reliability, Infocom Technologies and Optimization (Trends and Future Directions) (ICRITO). IEEE, 2022. http://dx.doi.org/10.1109/icrito56286.2022.9965051.

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