Preliminary Characterization of Crude Lectin Fraction of the Red Alga, Acrocystis nana from Wediombo Beach of the Southern Coast of Java Island, Gunung Kidul, Yogyakarta, Indonesia

International Conference On Food Science and Engineering 2016

Anam, C.^1,3 ; Praseptiangga, D.^1 ; Nugraheni, M.A.^1 ; Nurhayati, T.^1 ; Fajarningsih, N.D.^2 ; Zilda, D.S.^2 ; Chasanah, E.^2 ; Yunus, A.^3

Department of Food Science and Technology, Sebelas Maret University (UNS), Jl. Ir. Sutami 36 A, Kentingan, Surakarta

57126, Indonesia^1

Research and Development Center for Marine and Fisheries Product Competitiveness and Biotechnology, Ministry of Marine Affairs and Fisheries, Jl. KS Tubun Petamburan VI, Slipi, Jakarta, Indonesia^2

Graduate School Program, Sebelas Maret University (UNS), Jl. Ir. Sutami 36 A, Kentingan, Surakarta

57126, Indonesia^3

关键词: Activity assays;    After-treatment;    Bioactive compounds;    Coastal regions;    Divalent cation;    High specificity;    Immune response;    Protein contents;   

Others  :  https://iopscience.iop.org/article/10.1088/1757-899X/193/1/012016/pdf
DOI  :  10.1088/1757-899X/193/1/012016

来源: IOP

【 摘 要 】

Lectins, bioactive compounds that found in algae, are bind to sugars or glycoproteins reversibly with high specificity, but are devoid of catalytic activity, and in contrast to antibodies, are not products of an immune response. Acrocystis nana is a species of red alga that is collected from the Wediombo beach, coastal region of Gunungkidul, Yogyakarta. Hemaglutination activity of a crude lectin fraction from Acrocystis nana was examined using trypsin-treated rabbit erythrocytes and its chemical properties, including its protein content, stability on pH, temperature, and divalent cations were determined as a preliminary characterization phase. Crude lectin of Acrocystis nana showed a titer of 212on hemagglutination activity assay and the protein content was 6225.44 μg/ml. Hemagglutination activity of this crude lectin was stable after treatment at various pH from 3 to 10 and its activity was lost by heating at 50°C until 100°C. Moreover, the hemagglutination activity was slightly affected by divalent cations treatment, indicating that the presence of divalent cations may require for its activity, however, further studies are still needed for a more comprehensive understanding about its properties.