Purification and characterization of a lectin with refolding ability from Genipa americana bark

Autor(es)

Costa, Ricardo Bezerra ^[1] ; Campana, Patricia Targon ^[2] ; Chambergo, Felipe Santiago ^[2] ; Napoleao, Thiago Henrique ^[3] ; Guedes Paiva, Patricia Maria ^[3] ; Vieira Pereira, Hugo Juarez ^[1] ; Vilela Oliva, Maria Luiza ^[4] ; Gomes, Francis Soares ^[1]

Afiliação do(s) autor(es)

^[1] Univ Fed Alagoas, Inst Quim & Biotecnol, BR-57072900 Maceio, Alagoas - Brazil

^[2] Univ Sao Paulo, Escola Artes Ciencias & Humanidades, BR-03828000 Sao Paulo, SP - Brazil

^[3] Univ Fed Pernambuco, Ctr Biociencias, Dept Bioquim, BR-50670420 Recife, PE - Brazil

^[4] Univ Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 Sao Paulo, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: International Journal of Biological Macromolecules; v. 119, p. 517-523, NOV 2018.
• Citações Web of Science: 4

Resumo

Genipa americana L, commonly known as genipap, is a plant with economical and medicinal importance, and a promising source of bioactive compounds. Lectins are carbohydrate-binding proteins with several biotechnological applications. This study reports the isolation and characterization of a G. americana bark lectin (GaBL). A single chromatographic procedure on Sephacryl S-100 resulted in isolation of GaBL, a protein with native molecular weight of over 200 kDa and p14.02, whose hemagglutinating activity was inhibited by lactose and fetuin, not affected by ions (Ca2+ and Mg2+), and stable upon heating (303-393 K) as well as over the pH range 5-10. The highest activity was found at a temperature lower than 333 K and pH 5. The secondary structure was analyzed by circular dichroism and showed a prevalence of beta structures and unordered forms. GaBL was able to partially refold in acidic pH conditions when dissolved in PBS buffer at pH 7.4. In condusion, GaBL was purified in milligram quantities with high stability against different conditions, and is a new biomaterial with potential biotechnological applications. (C) 2018 Elsevier B.V. All rights reserved. (AU)

• Processo FAPESP: 14/24107-1 - Estudo e caracterização de enzimas oxidases produzidas por fungos filamentosos
• Beneficiário: Felipe Santiago Chambergo Alcalde
• Modalidade de apoio: Auxílio à Pesquisa - Programa BIOEN - Regular