Academic literature on the topic 'Pectinase enzyme'
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Journal articles on the topic "Pectinase enzyme"
Roy, Karabi, Sujan Dey, Md Kamal Uddin, Rasel Barua, and Md Towhid Hossain. "Extracellular Pectinase from a Novel Bacterium Chryseobacterium indologenes Strain SD and Its Application in Fruit Juice Clarification." Enzyme Research 2018 (March 21, 2018): 1–7. http://dx.doi.org/10.1155/2018/3859752.
Full text-, Shilpa, Mandheer Kaur, and Yogita Jadon. "Isolation and Screening of Pectinase Producing Bacteria from Soil Sample." CGC International Journal of Contemporary Technology and Research 3, no. 2 (July 17, 2021): 166–70. http://dx.doi.org/10.46860/cgcijctr.2021.06.31.166.
Full textBerutu, Cocok Ana Maryani, Fahrurrozi Fahrurrozi, and Anja Meryandini. "Pectinase Production and Clarification Treatments of Apple (Malus Domestica) Juice." ANNALES BOGORIENSES 21, no. 2 (February 28, 2018): 63. http://dx.doi.org/10.14203/ab.v21i2.311.
Full textBerutu, Cocok Ana Maryani, Fahrurrozi Fahrurrozi, and Anja Meryandini. "Pectinase Production and Clarification Treatments of Apple (Malus Domestica) Juice." ANNALES BOGORIENSES 21, no. 2 (December 22, 2017): 63. http://dx.doi.org/10.14203/ann.bogor.2017.v21.n2.63-68.
Full textAmanat, Fatima, Amna Yaqoob, Asif Ali, and Muhammad Sajjad. "Extracellular Production of Pectinase from Bacteria Isolated from Rotten Apples from Lahore, Pakistan." BioScientific Review 01, no. 03 (September 2019): 37–45. http://dx.doi.org/10.32350/bsr.0103.05.
Full textMohan, Nayana, and Archana Prabhat. "Isolation, Production and Application of Bacterial Pectinase for Industrial Use." Indian Journal of Nutrition and Dietetics 55, no. 4 (October 9, 2018): 442. http://dx.doi.org/10.21048/ijnd.2018.55.4.22116.
Full textAlqahtani, Yahya S., Sunil S. More, Keerthana R., Ibrahim Ahmed Shaikh, Anusha K. J., Veena S. More, Francois N. Niyonzima, Uday M. Muddapur, and Aejaz A. Khan. "Production and Purification of Pectinase from Bacillus subtilis 15A-B92 and Its Biotechnological Applications." Molecules 27, no. 13 (June 29, 2022): 4195. http://dx.doi.org/10.3390/molecules27134195.
Full textAguilar, Guillermo, Blanca A. Trejo, Juan M. García, and Carlos Huitrón. "Influence of pH on endo- and exo-pectinase production by Aspergillus sp. CH-Y-1043." Canadian Journal of Microbiology 37, no. 12 (December 1, 1991): 912–17. http://dx.doi.org/10.1139/m91-158.
Full textKC, Sudeep, Jitendra Upadhyaya, Dev Raj Joshi, Binod Lekhak, Dhiraj Kumar Chaudhary, Bhoj Raj Pant, Tirtha Raj Bajgai, et al. "Production, Characterization, and Industrial Application of Pectinase Enzyme Isolated from Fungal Strains." Fermentation 6, no. 2 (June 9, 2020): 59. http://dx.doi.org/10.3390/fermentation6020059.
Full textCHAMANI, Esmaeil, Seyyed Karim TAHAMI, Nasser ZARE, Rasool Asghari-ZAKARIA, Mehdi MOHEBODINI, and Daryl JOYCE. "Effect of Different Cellulase and Pectinase Enzyme Treatments on Protoplast Isolation and Viability in Lilium ledebeourii Bioss." Notulae Botanicae Horti Agrobotanici Cluj-Napoca 40, no. 2 (November 5, 2012): 123. http://dx.doi.org/10.15835/nbha4028055.
Full textDissertations / Theses on the topic "Pectinase enzyme"
Göğüş, Nihan Tarı Canan. "Effect of The Morphology of Aspergillus Sojae on Pectinase Enzyme and The Optimization of Fermentation Conditions/." [s.l.]: [s.n.], 2006. http://library.iyte.edu.tr/tezlerengelli/master/gidamuh/T000578.pdf.
Full textDalagnol, Luíza Merlini Garcia. "Avaliação do uso do ultrassom na extração do mosto da uva cabernet sauvignon e na atividade enzimática." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2017. http://hdl.handle.net/10183/158743.
Full textGrape processing for juice and wine production encompasses different technological processes, such as enzymatic treatment, that usually uses commercial enzyme preparations to improve clarification and extraction processes. However, this is a treatment that demands high processing time, being relevant the search for new technologies in order to improve the whole process. Ultrasound (US) can be used as an alternative to reduce the processing time and improve the quality of the product, moreover, it can provide benefits in the combined use with enzymes, favoring the enzymatic reactions. In this work, the combined use of enzymatic treatment (ET), ultrasound (US), and mechanical agitation (MS) was studied in order to understand the effects of the techniques on Cabernet Sauvignon must extraction. Initially, nine commercial enzyme preparations were characterized according to their enzymatic activities and applied to must extraction, evaluating temperature (40, 50 and 60 °C), time (15 and 30 min), and enzyme concentration (0.01 to 2.0 Ug-1). The best results were obtained for the preparation Zimopec PX5® under conditions of 1.0 U.g-1 of pectinase at 50 °C for 30 min. A significant increase on quality parameters (color, °Brix, yield, antioxidant capacity, total anthocyanins) was obtained to extraction combining the three methods (US, MS and ET), mainly when US were applied. Based on these previous results, a new study was conducted to investigate the influence of sonication on the catalytic efficiency of the enzymes pectinase (PE), xylanase (XLN) and cellulase (CE). The enzymatic activities were evaluated at different pH and in samples of enzyme and substrates submitted to a previous treatment of sonication by determined times (0 - 30 min). The kinetic and thermodynamic parameters were estimated, showing a positive effect of the ultrasonic treatment on the enzymatic activity. Previous sonication of the substrate contributed significantly to the increase in XLN activity, whereas the previous sonication of the enzyme improved the activity of CE and PE. This research showed the potential benefits of ultrasound treatment on reaction rate and catalytic efficiency (Vmax/Km) improvement of enzymes, attesting that US can be used to increase the catalytic efficiency of pectinase, xylanase and cellulase enzymes. According to the obtained results, it can be affirmed that ultrasound improved the extraction process, and can be applied as an alternative technique, as well as provided beneficial effects on the enzymatic activity.
Gacura, Matthew David. "Drivers of Fungal Community Composition and Function In Temperate Forests." Kent State University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=kent1543579763552776.
Full textByarugaba-Bazirake, George William. "The effect of enzymatic processing on banana juice and wine." Thesis, Link to the online version, 2008. http://hdl.handle.net/10019/1633.
Full textPedrolli, Danielle Biscaro [UNESP]. "Caracterização físico-química de pectinases extracelulares purificadas de Aspergillus giganteus." Universidade Estadual Paulista (UNESP), 2008. http://hdl.handle.net/11449/95014.
Full textFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
O fungo Aspergillus giganteus produz uma única poligalacturonase (PG) quando cultivado em meio líquido com pectina de citrus como única fonte de carbono, e pelo menos três pectina liases (PL) quando cultivado em meio líquido com resíduo de laranja como fonte de carbono. A PG de A. giganteus foi purificada em duas etapas: precipitação de proteínas com 70% de saturação com sulfato de amônio e troca aniônica. A PG purificada apresentou massa molar de 69,7±0,07 kDa. A máxima atividade da enzima foi observada em pH 6,0 a 55-60ºC, sendo essa estável em meio neutro e alcalino. A PG apresentou meias-vidas de 115, 18 e 6 min quando incubada a 40, 50 e 55 ºC, respectivamente. A enzima mostrou-se ativa sobre substratos de qualquer grau de metilação, com maior especificidade para substratos de baixa ou nenhuma metilação, apresentando Vmax 669,6 e 602,8 μmol/mg.min, Km 3,25 e 1,16 mg/mL, kcat 770 e 690 s-1 sobre pectina de citrus 34 % esterificada e ácido poligalacturônico, respectivamente. A PG apresentou atividade exo liberando apenas ácido galacturônico como produto de hidrólise. 2-Mercaptoetanol, DTT, Co2+, Mn2+, Mg2+, NH4 + e Na+ agiram como estimulantes da atividade PG. Já Hg2+, EDTA, citrato de sódio, ácido iodoacético, SDS, Ba2+, Cu2+, Pb2+ e Zn2+ inibiram essa atividade enzimática. A principal pectina liase de A. giganteus, a PL I, foi purificada em três etapas: troca aniônica, troca catiônica e filtração em gel. A massa molar da PL I foi estimada em 55,7±1,4 kDa. A máxima atividade da enzima foi obtida em pH 8,5 a 50ºC. A PL I apresentou meias-vidas de 19, 9 e 6 min a 40, 45 e 50ºC, respectivamente. As maiores atividades da PL I foram observadas em pectinas de citrus com 34 e 72% de metilação, nas quais apresentou Vmax 1.488,1 e 1.129,8 U/mg.min, respectivamente, e Km 4,8 mg/mL para ambos os substratos. O padrão de degradação da pectina...
Aspergillus giganteus produces one polygalacturonase (PG) on liquid medium with citrus pectin as the only carbon source, and at least three pectin lyases (PL) with orange waste. Homogenous PG was obtained after two steps: protein precipitation with 70 % ammonium sulphate saturation and anionexchange chromatography. The purified PG showed molecular weight of 69.7±0,07 kDa. The enzyme exhibited maximal activity at pH 6.0 and 55-60 °C, and was stable in neutral and alkaline medium. The half-live for PG at 40, 50 and 55 °C was 115, 18 and 6 min, respectively. The enzyme was active on substrates with any methyl-esterification degree, and hydrolysed better low esterified and not esterified substrates, showing Vmax 669.6 and 602.8 μmol. mg-1.min-1, Km 3.25 and 1.16 mg/mL, kcat 770 and 690 s-1 on 34 % esterified citrus pectin and polygalacturonic acid, respectively. The unique soluble product released in the reaction with pectin and polygalacturonic acid was monogalacturonic acid, and according to this results the enzyme can be classified as exoPG. PG activity enhanced in presence of 2-mercaptoethanol, DTT, Co2+, Mn2+, Mg2+, NH4 + and Na+, and was completely inhibited in presence of Hg2+. EDTA, sodium citrate, iodoacetic acid, SDS, Ba2+, Cu2+, Pb2+ and Zn2+ inhibited enzyme activity. The main PL from A. giganteus was called PL I and was purified after three steps: anion-exchange and cation-exchange chromatographies, and gel filtration. The purified PL I showed molecular weight of 55.7±1.4 kDa. The enzyme exhibited maximal activity at pH 8.5 and 50 °C, and was stable in neutral and acid medium. The half-live for PL I at 40, 45 and 50 °C was 19, 9 and 6 min, respectively. The enzyme was more active on citrus pectins with 34 and 72% of esterification, showing Vmax 1,488.1 and 1,129.8 U. mg-1.min-1, repectively, and Km 4.8 mg/mL on both substrates. The degradation pathern on 34% esterified...(Complete abstract click electronic access below)
Hassan, Sozan. "Caractérisation de nouvelles enzymes impliquées dans la dégradation de polysaccharides végétaux à partir de la bactérie Dickeya dadantii 3937." Thesis, Lyon, INSA, 2011. http://www.theses.fr/2011ISAL0115.
Full textThe phytopathogenic bacterium Dickeya dadantii is responsible for soft rot diseases of various plants. It secretes in the external medium a large array of enzymes which are able to degrade the constituents of the plant-cell wall. The first part of my work was related to the féruloyl esterases FaeD and FaeT. Feruloyl esterases are responsible for the hydrolysis of ester linkages between ferulic acid and the xylan or pectin chains. By cleaving these linkages, they improve the complete degradation of the plant-cell wall. The importance of these enzymes led us to search whether D. dadantii produces such esterases. A gene bank screening using a specific detection test for the feruloyl esterase activity allowed us to identify two genes which were characterized. While faeT is weakly transcribed in all the conditions, the faeD transcription is strongly induced in the presence of ferulic acid and it is controlled by the regulator FaeR. Whereas FaeT is a cytoplasmic protein, FaeD is secreted by the Out system responsible for the secretion of several pectinases. The enzymes FaeD and FaeT were overproduced in E. coli and their main biochemical properties were determined. The determination of the complete sequence of the D. dadantii genome makes it possible to develop functional genomic studies. This sequence confirms the presence of genes encoding the previously characterized pectinases and it reveals that this genome encodes new potential pectinases. The second part of my work was related to the gene pelN identified by genome analysis. Pectate lyases cleave the glycosidic bounds in the polygalacturonate chain by a β-elimination reaction, generating unsaturated products. This reaction mechanism requires cations as cofactor, generally Ca2+. After cloning of the gene pelN, the protein PelN was overproduced in E. coli. Its pectate lyase activity was demonstrated by its capacity to produce unsaturated derivatives from polygalacturonate or pectins. This study showed that PelN is the first pectate lyase that uses Fe2+ ions as the preferential cofactor. In D. dadantii, the pelN expression depends on various regulators controlling the pectinase synthesis, such as PecS or GacA. PelN is an extracellular protein secreted by the Out system. These studies contribute to increase the knowledge on the respective role of the different enzymes involved in the degradation of the plant-cell wall and the cooperative interactions in this pluri-enzymatic system
Zhang, Jing. "Biochemical Study and Technical Applications of Fungal Pectinase." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Universitetsbiblioteket [distributör], 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-6295.
Full textAltan, Asena Yenidünya Ali Fazıl. "Isolation And Molecular Characterization of Extracellular Lipase And Pectinase Producing Bacteria From Olive Oil Mills/." [s.l.]: [s.n.], 2004. http://library.iyte.edu.tr/tezler/master/biyoteknoloji/T000497.pdf.
Full textSykes, Melissa. "Do zoospores of Phytophthora cinnamomi produce enzymes such as cutinases, cellulases and pectinases?" Thesis, Sykes, Melissa (1995) Do zoospores of Phytophthora cinnamomi produce enzymes such as cutinases, cellulases and pectinases? Honours thesis, Murdoch University, 1995. https://researchrepository.murdoch.edu.au/id/eprint/32817/.
Full textSandri, Ivana Greice. "Enzimas pectinolíticas : seleção de linhagens fúngicas produtoras, caracterização e aplicação em processos da indústria de alimentos." reponame:Repositório Institucional da UCS, 2010. https://repositorio.ucs.br/handle/11338/516.
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In this work, fungus samples isolated from decomposing vegetables were tested with respect to their capacity of producing pectinases to be applied to the enzymatic treatment of apple and bilberry juices. Taking in account the secretion of endo-polygalacturonase (endo-PG), two isolates which were identified and named Aspergillus niger LB23 e Aspergillus fumigatus LB39J were selected for solid-state and submerged cultivations, respectively. The enzymatic extracts from these strains did not present total aflatoxin (B1, B2, G1, G2) levels up to detection limit of 2 μg/Kg. The enzyme preparation obtained from solid-state cultivation of A. niger LB23 showed the largest activities of both endo-PG and exo-polygalacturonase (exo-PG) at pH 4.0, whereas the reaction with submerged A. fumigatus L39J enzymatic extracts was favoured at pH between 4.0 and 5.0 for endo-PG and 5.0 for exo-PG. With respect to the reaction temperature for A. niger LB23 pectinolytic preparation, endo and exo-PG showed the best performances at the ranges 40-50ºC and 50-60ºC, respectively. For A. fumigatus L39J polygalacturonases, a range from 40 to 60ºC, for endo-PG, and 60ºC, for exo-PG, were defined as the best temperatures. When the thermal stability of polygalacturonases present in both preparations was evaluated, preservation of about 70% of activities was observed after exposing the enzymes to temperatures up to 40ºC for 150 minutes. The influence of different glucose and pectin concentrations on the results of the solid-state process with A. niger LB23 was assessed and an increment in endo and exo-PG activities were observed in medium containing 6% (w/w) of pectin and absence of glucose, with activities of 65 units per gram of dry medium (U/gdm) and 198 U/gdm being achieved. In submerged cultivation of A. fumigatus LB39, highest enzyme activities were obtained in medium with 20 g/L of pectin and without glucose: 42 U/mL for endo-PG and 32 U/mL for exo-PG. In the conditions defined for the submerged process, different medium initial pH values were tested. Maximum activities were observed at initial pH of 3.0 for endo-PG (44 U/mL) and 4.0 for exo-PG (37 U/mL). Furthermore, in bench bioreactor, it was observed that an initial pH of 4.0, with uncontrolled minimum value and, afterwards, maximum value controlled at 3.5 led to the largest enzyme production with 81 U/mL of endo-PG and 49 U/mL of exo-PG. By comparing the enzymatic preparations produced by the selected strains, it was noticed that the pectinase produced by A. niger LB23 were more efficient for the hydrolysis of pectic substances present in both apple and bilberry juices, since it improved reduction of turbidity (90 and 40%) and viscosity (40 and 60%) and increasing clarification (90 and 55%), respectively. These results indicate the potential of A. niger LB23 pectinases for the enzymatic treatment of fruit juices, being remarkable that both the level of phenolic compounds and antioxidant capacity of juices were mostly preserved after treatment.
Book chapters on the topic "Pectinase enzyme"
Dongowski, G., S. Förster, and H. Kunzek. "Effect of Pectolytic and Cellulolytic Enzyme Treatments on Functional and Nutritional Properties of Cell Wall Materials from Apples." In Advances in Pectin and Pectinase Research, 491–504. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0331-4_36.
Full textFavela-Torres, Ernesto, Cristobal Aguilar, Juan Carlos Contreras-Esquivel, and Gustavo Viniegra-González. "Pectinases." In Enzyme Technology, 273–96. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_14.
Full textTewari, Rupinder, Ram P. Tewari, and Gurinder S. Hoondal. "Microbial Pectinases." In Microbial Enzymes and Biotransformations, 191–208. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-846-3:191.
Full textLee, Jason T., and Kyle D. Brown. "Mannanase, α-galactosidase and pectinase: minor players or yet to be exploited?" In Enzymes in farm animal nutrition, 70–88. 3rd ed. Wallingford: CABI, 2022. http://dx.doi.org/10.1079/9781789241563.0005.
Full textVohra, Anuja, and Reena Gupta. "Pectinases and their Biotechnological Applications." In Microbial Enzyme Technology in Food Applications, 145–61. Boca Raton, FL : CRC Press, [2016] | Series: Food biology series | “A science publishers book.”: CRC Press, 2017. http://dx.doi.org/10.1201/9781315368405-10.
Full textGunjal, Aparna B., Neha N. Patil, and Sonali S. Shinde. "Pectinase in Degradation of Lignocellulosic Wastes." In Enzymes in Degradation of the Lignocellulosic Wastes, 71–103. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-44671-0_5.
Full textBenen, J. A. E., G. J. W. M. van Alebeek, A. G. J. Voragen, and J. Visser. "Mode of Action Analysis and Structure-Function Relationships of Aspergillus Niger Pectinolytic Enzymes." In Advances in Pectin and Pectinase Research, 235–56. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0331-4_18.
Full textAntony, Cecil, Praveen Kumar Ghodke, and Saravanakumar Thiyagarajan. "The Role of Pectinases in Waste Valorization." In Enzymes in the Valorization of Waste, 127–53. Boca Raton: CRC Press, 2022. http://dx.doi.org/10.1201/9781003187684-6.
Full textVoragen, A. G. J., P. J. H. Daas, and H. A. Schols. "Enzymes as tools for structural studies of pectins." In Bioactive Carbohydrate Polymers, 129–45. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-015-9572-8_11.
Full textde Vries, J. A., A. G. J. Voragen, F. M. Rombouts, and W. Pilnik. "Structural Studies of Apple Pectins with Pectolytic Enzymes." In ACS Symposium Series, 38–48. Washington, DC: American Chemical Society, 1986. http://dx.doi.org/10.1021/bk-1986-0310.ch004.
Full textConference papers on the topic "Pectinase enzyme"
Doković, Vladimir, and Snežana Bogosavljević-Bošković. "ENZIMI U ISHRANI BROJLERA." In XXVII savetovanje o biotehnologiji. University of Kragujevac, Faculty of Agronomy, 2022. http://dx.doi.org/10.46793/sbt27.229d.
Full textKabir, Md Fauzul, and Lu-Kwang Ju. "Temperature effects on enzyme stability for carbohydrate hydrolysis of soy materials." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/srjx5896.
Full textHai-ning Zhang, Jia He, Dan Luo, Chun-yang Zheng, Gai-ping Zhai, and Shuo-guo Zhang. "Study on effect on pulp enzyme and pectinase on the juice yield of kiwi fruit." In 2011 International Conference on New Technology of Agricultural Engineering (ICAE). IEEE, 2011. http://dx.doi.org/10.1109/icae.2011.5943991.
Full textAlpiger, Simone Bleibach, and Milena Corredig. "Influence of Process Conditions on Enzyme Assisted Aqueous Extraction of Protein from Whole Rapeseed Using Pectinase." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists’ Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.51.
Full textSINGHAL, ANSHUL, AMY LANGHORST, MIHAELA BANU, and ALAN TAUB. "EFFECT OF ENZYMATIC RETTING CONDITIONS ON THE DIAMETER AND MECHANICAL PROPERTIES OF FLAX FIBERS." In Proceedings for the American Society for Composites-Thirty Seventh Technical Conference. Destech Publications, Inc., 2022. http://dx.doi.org/10.12783/asc37/36478.
Full textUnluturk, S., S. Oncu, C. Tari, and N. Gogus. "Various Factors Affecting the Pellet Morphology, Broth Reology and Pectinase Enzyme Production in Submerged Fermentation of Aspergillus Sojae." In 13th World Congress of Food Science & Technology. Les Ulis, France: EDP Sciences, 2006. http://dx.doi.org/10.1051/iufost:20060271.
Full textReports on the topic "Pectinase enzyme"
Lurie, Susan, John Labavitch, Ruth Ben-Arie, and Ken Shackel. Woolliness in Peaches and Nectarines. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7570557.bard.
Full textJoel, Daniel M., John C. Steffens, and Alfred M. Mayer. Host-Elicited Germination and Mechanism of Penetration in Broomrape (Orobanche Spp.). United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568107.bard.
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