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2. Psidium guajava L. and Psidium brownianum Mart ex DC.: Chemical composition and anti – Candida effect in association with fluconazole

Author

Morais-Braga, Maria Flaviana B., Sales, Débora L., Carneiro, Joara Nalyda P., Machado, Antonio Júdson T., dos Santos, Antonia Thassya L., de Freitas, Maria Audilene, Martins, Gioconda Morais de A. Bezerra, Leite, Nadghia Figueiredo, de Matos, Yedda Maria L.S., Tintino, Saulo R., Souza, Djair S.L., Menezes, Irwin R.A., Ribeiro-Filho, Jaime, Costa, José G.M., and Coutinho, Henrique D.M.

Published
2016
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4. Identification of a novel β- N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)

Author

Souza, Djair S.L., Grossi-de-Sa, Maria F., Silva, Luciano P., Franco, Octavio L., Gomes-Junior, José E., Oliveira, Gustavo R., Rocha, Thales L., Magalhães, Cláudio P., Marra, Brener M., Grossi-de-Sa, Maíra, Romano, Eduardo, de Sá, César Martins, Kombrink, Erich, Jiménez, Arnubio V., and Abreu, Luiz R.D.

Published
2008
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5. Identification of a novel B-N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)

Author

Souza, Djair S.L., Grossi-de-Sá, Maria Fátima, Silva, Luciano P., Franco, Octavio L., Gomes-Júnior, José E., Oliveira, Gustavo R., Rocha, Thales L., Magalhães, Cláudio P., Marra, Brener M., Grossi-de-Sá, Maíra, Romano, Eduardo, Martins de Sá, César, Kombrink, Erich, Jiménez, Arnubio V., and Abreu, Luiz R.D.

Subjects
Palythoa caribaeorum, b-N-Acetylhexosaminidase, Chitin-active-enzymes, Inactivated chitinases
Abstract

Made available in DSpace on 2016-10-10T03:52:23Z (GMT). No. of bitstreams: 5 Identification of a novel B N acetylhexosaminidase_Pcb_NAHA1.pdf: 298920 bytes, checksum: b6ceb77cf2800c60845c35248addc653 (MD5) license_url: 52 bytes, checksum: 2f32edb9c19a57e928372a33fd08dba5 (MD5) license_text: 24259 bytes, checksum: f1f24f769b03eb8f9cd3f53c1090841c (MD5) license_rdf: 24658 bytes, checksum: 9d3847733d3c0b59c7c89a1d40d3d240 (MD5) license.txt: 1887 bytes, checksum: 445d1980f282ec865917de35a4c622f6 (MD5) Previous issue date: 2008 B-N-Acetylhexosaminidases (EC 3.2.1.52) belong to an enzyme family that hydrolyzes terminal b-D-N-glucosamine and b-D-N-galactosamine residues from oligosaccharides. In this report, we purified a novel b-N- acetylhexosaminidase (Pcb-NAHA1) from the marine zoanthid Palythoa caribaeorum by applying ammonium sulfate fractionation, affinity chromatography on a chitin column, followed by two rounds of size exclusion chromatography. SDS–PAGE analysis indicated a single band protein of apparent homogeneity with a molecular mass of 25 kDa. The purified enzyme preferentially hydrolyzed p-nitrophenyl-2-acetoamide-2-deoxyamide-2-deoxy-b-D-Nacetylglucosamide (pNP-GlcNAc) and to a lesser extent p-nitrophenyl-2-acetoamide-2-deoxyamide-2-deoxy-b-D-N-acetylgalactosamide (pNP-GalNAc). Detailed kinetic analysis using pNP-GlcNAc resulted in a specific activity of 57.9 U/mg, a Km value of 0.53 mM and a Vmax value of 88.1 lmol/h/mg and kcat value of 0.61 s_1. Furthermore, purified Pcb-NAHA1 enzyme activity was decreased by HgCl2 or maltose and stimulated in the presence of Na2SeO4, BaCl2, MgCl2, chondroitin 6-sulfate, and phenylmethylsulfonylfluoride. The optimum activity of Pcb-NAHA1 was observed at pH 5.0 and elevated temperatures (45–60 _C). Direct sequencing of proteolytic fragments generated from Pcb-NAHA1 revealed remarkable similarities to plant chitinases, which belong to family 18, although no chitinase activity was detected with Pcb-NAHA1. We conclude that b-N-acetylhexosaminidases, representing a type of exochitinolytic activity, and endo-chitinases share common functional domains and/or may have evolved from a common ancestor. Sim Publicado

Published
2008

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