Search

Your search keyword '"Gomes, Eleni"' showing total 20 results
Start Over Author "Gomes, Eleni" Publication Type Books
20 results on '"Gomes, Eleni"'

1. Microbial plant material–degrading enzymes

Author

de Cassia Pereira, Josiani, primary, Bocchini, Daniela Alonso, additional, Gomes, Eleni, additional, da Silva, Roberto, additional, Galindo Gomes, José Erick, additional, Déli de Oliveira Sanches, Raísa, additional, Spressão de Lima Junior, David, additional, Simioni Pereira, Waldir Eduardo, additional, Okamura da Silva, Gabriela, additional, and Eduardo de Oliveira do Nascimento, Carlos, additional

Published
2023
Full Text
View/download PDF

2. Contributors

Author

Altaf, Muhammad, primary, Amin, Muhammad, additional, Angelin Swetha, T., additional, Arun, A., additional, Ashraf, Raja Shahid, additional, Ay, Hasan, additional, Ayub, Humaira, additional, Balaji, P., additional, Bandehali, S., additional, Barbieri, Douglas, additional, Baredar, Prashant, additional, Behura, Aruna K., additional, Bekmezci, Muhammed, additional, Bhattacharya, Priyanjali, additional, Bocchini, Daniela Alonso, additional, Bora, Abhispa, additional, Chhabra, Mayank, additional, Chong, Woon Chan, additional, Colin, Verónica Leticia, additional, da Silva, Classius Ferreira, additional, da Silva, Roberto, additional, de Cassia Pereira, Josiani, additional, Del Gobbo, Luciana Melisa, additional, Déli de Oliveira Sanches, Raísa, additional, Dharani, G., additional, Dwivedi, Gaurav, additional, Eduardo de Oliveira do Nascimento, Carlos, additional, Galindo Gomes, José Erick, additional, Gogoi, Gitashree, additional, Gomes, Eleni, additional, Guliani, Eksha, additional, Guru Raj Rao, R., additional, Hosseini, S.M., additional, Jeyaseelan, Christine, additional, Khalid, Ayesha, additional, Khan, Taous, additional, Khanra, Anwesha, additional, Kulanthaisamy, Mohanrasu, additional, Lai, Soon Onn, additional, Lim, Steven, additional, Madni, Ahmed, additional, Maji, Tarun K., additional, Mallakpour, Shadpour, additional, Mandal, Moon, additional, Mitra, Sayak, additional, Moghadassi, A.R., additional, Muhammad, Gulzar, additional, Naghdi, Mina, additional, Nalini, S., additional, Ochi, Deise, additional, Okamura da Silva, Gabriela, additional, Pang, Yean Ling, additional, Panneerselvan, Logeshwaran, additional, Parvizian, F., additional, Patel, Trupti N., additional, Pedroso Yoshida, Cristiana Maria, additional, Prakash Rai, Monika, additional, Prakash, Rajiv, additional, Raza, Muhammad Arshad, additional, Reis, Andresa Ferreira, additional, Rulli, Macarena María, additional, Saini, B.S., additional, Saleem, Sumaira, additional, Sathiyamurthi, S., additional, Sen, Fatih, additional, Sen, Shampa, additional, Severino, Patrícia, additional, Shahid, Munazza, additional, Simioni Pereira, Waldir Eduardo, additional, Singh, N.B., additional, Sivaprakash, G., additional, Souto, Eliana B., additional, Spressão de Lima Junior, David, additional, Sudhakar, M.P., additional, Vasistha, Shrasti, additional, Venkatnarayanan, S., additional, Venturini, Anna Cecília, additional, and Wahid, Fazli, additional

Published
2023
Full Text
View/download PDF

4. List of Contributors

Author

Aguieiras, Erika C.G., primary, Ahluwalia, Vivek, additional, Amorim, Graziella M., additional, Ángeles Sanromán, Ma, additional, Barreto, Maysa S., additional, Barrios-González, Javier, additional, Binod, Parameswaran, additional, Bissoqui, Lucas, additional, Cammarota, Magali C., additional, Cavalcanti-Oliveira, Elisa D., additional, Chen, Hong-Zhang, additional, Costa, Jorge A.V., additional, da Silva, Roberto, additional, de Carvalho, Júlio C., additional, de Cassia Pereira, Josiani, additional, de Oliveira, Priscilla Z., additional, de Oliveira Mendes, Gilberto, additional, Destéfanis Vítola, Francisco M., additional, Farinas, Cristiane S., additional, Favela-Torres, Ernesto, additional, Ferreira da Costa, Eduardo S., additional, Figueroa-Montero, Arturo, additional, Fragoso dos Santos, Anderson, additional, Freire, Denise M.G., additional, Garg, Vinod Kumar, additional, Godoy, Mateus G., additional, Gomes, Eleni, additional, Junior Letti, Luiz A., additional, Kachrimanidou, Vasiliki, additional, Karp, Susan G., additional, Koutinas, Apostolis A., additional, Krishania, Meena, additional, Kumar, Vinod, additional, Ladino-Orjuela, Guillermo, additional, Liu, Yang, additional, Loera-Corral, Octavio, additional, Machado de Castro, Aline, additional, Martins, Vilásia G., additional, Méndez-González, Fernando, additional, Nampoothiri, Kesavan Madhavan, additional, Pandey, Ashok, additional, Pazos, Marta, additional, Pedroni Medeiros, Adriane B., additional, Rodrigues, Cristine, additional, Rodríguez-Couto, Susana, additional, Rodríguez-Fernández, Daniel E., additional, Rodríguez-León, Jose A., additional, Rosales-Zamora, Gabriel, additional, Rosales, Emilio, additional, Sangwan, Rajender Singh, additional, Santos, Lucielen O., additional, Saucedo-Castañeda, Gerardo, additional, Sharma, Kavita, additional, Sindhu, Raveendran, additional, Soccol, Carlos R., additional, Torres-Mancera, María T., additional, Treichel, Helen, additional, Vandenberghe, Luciana P.S., additional, Vassilev, Nikolay, additional, Vinícius de Melo Pereira, Gilberto, additional, and Wang, Lan, additional

Published
2018
Full Text
View/download PDF

19. Purification and Characterization of Two Xylanases From Alkalophilic and Thermophilic Bacillus licheniformis 77-2.

Author

McMillan, James D., Adney, William S., Mielenz, Jonathan R., Klasson, K. Thomas, Damiano, Valquiria B., Ward, Richard, Gomes, Eleni, Alves-Prado, Heloiza Ferreira, and Da Silva, Roberto

Abstract

The alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermostable cellulase-free xylanases. The crude xylanase was purified to apparent homogeneity by gel filtration (G-75) and ionic exchange chromatography (carboxymethyl sephadex, Q sepharose, and Mono Q), resulting in the isolation of two xylanases. The molecular masses of the enzymes were estimated to be 17 kDa (X-I) and 40 kDa (X-II), as determined by SDS-PAGE. The Km and Vmax values were 1.8 mg/mL and 7.05 U/mg protein (X-I), and 1.05 mg/mL and 9.1 U/mg protein (X-II). The xylanases demonstrated optimum activity at pH 7.0 and 8.0-10.0 for xylanase X-I and X-II, respectively, and, retained more than 75% of hydrolytic activity up to pH 11.0. The purified enzymes were most active at 70 and 75°C for X-I and X-II, respectively, and, retained more than 90% of hydrolytic activity after 1 h of heating at 50°C and 60°C for X-I and X-II, respectively. The predominant products of xylan hydrolysates indicated that these enzymes were endoxylanases. [ABSTRACT FROM AUTHOR]

Published
2006
Full Text
View/download PDF

20. Evaluation of Solid and Submerged Fermentations for the Production of Cyclodextrin Glycosyltransferase by Paenibacillus campinasensis H69-3 and Characterization of Crude Enzyme.

Author

McMillan, James D., Adney, William S., Mielenz, Jonathan R., Klasson, K. Thomas, Alves-Prado, Heloiza Ferreira, Gomes, Eleni, and Da Silva, Roberto

Abstract

Cyclodextrin glycosyltransferase (CGTase) is an enzyme that produces cyclodextrins from starch by an intramolecular transglycosylation reaction. Cyclodextrins have been shown to have a number of applications in the food, cosmetic, pharmaceutical, and chemical industries. In the current study, the production of CGTase by Paenibacillus campinasensis strain H69-3 was examined in submerged and solid-state fermentations. P. campinasensis strain H69-3 was isolated from the soil, which grows at 45°C, and is a Gramvariable bacterium. Different substrate sources such as wheat bran, soybean bran, soybean extract, cassava solid residue, cassava starch, corn starch, and other combinations were used in the enzyme production. CGTase activity was highest in submerged fermentations with the greatest production observed at 48-72 h. The physical and chemical properties of CGTase were determined from the crude enzyme produced from submerged fermentations. The optimum temperature was found to be 70-75°C, and the activity was stable at 55°C for 1 h. The enzyme displayed two optimum pH values, 5.5 and 9.0 and was found to be stable between a pH of 4.5 and 11.0. [ABSTRACT FROM AUTHOR]

Published
2006
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results