Karakterisasi Biokimia Lektin Makroalga Sargassum polycystum dan Turbinaria ornata -- Biochemical Characterisation of Lectin Derived from Sargassum polycystum and Turbinaria ornata Macroalgae

Nurrahmi Dewi Fajarningsih, Naomi Intaqta, Danar Praseptiangga, Choiroel Anam, Ekowati Chasanah

Abstract


ABSTRAK

Kemampuan lektin untuk mengikat karbohidrat secara spesifik dan reversible dapat dikembangkan dalam berbagai aplikasi, misalnya sebagai reagen histokimia. Penelitian ini bertujuan untuk mempelajari spesifisitas pengikatan lektin makroalga Sargassum polycystum dan Turbinaria ornata pada berbagai jenis karbohidrat, stabilitas aktivitas hemaglutinasi lektin pada berbagai rentang suhu dan pH, serta pengaruh kation divalen pada aktivitasnya. Uji penghambatan hemaglutinasi secara kualitatif dan kuantitatif dilakukan untuk mempelajari spesifisitas pengikatan lektin terhadap 20 jenis gula dan glikoprotein. Untuk melihat stabilitas aktivitasnya, lektin S. polycystum dan T. ornata diberi perlakuan pemanasan pada rentang suhu 30-100 oC, perlakuan pH 3-10 dan perlakuan kation divalen MgCl2 dan CaCl2 kemudian diuji aktivtitas hemagglutinasinya. Ekstrak kaya lektin S. polycystum dan T. ornata mampu mengenali dan mengikat 8 glikoprotein secara kualititatif, yaitu fetuin (Fe), asialo Fe (aFe), thyroglobulin from bovine (BTG), asialo BTG, thyroglobulin from porcine (PTG), asialo PTG (aPTG), asialo mucin from bovine submaxillary glands (aBSM), dan asialo transferrin (aTf), namun tidak mempunyai afinitas terhadap gula sederhana. Lektin S. polycystum memiliki spesifisitas pengikatan terbaik terhadap aFe dan transferrin (Minimum Inhibitory Concentration/MIC 250 µg/ml), sementara Lektin T. ornata memiliki spesifisitas pengikatan terbaik terhadap aPTG (MIC 31.25 µg/ml), PTG (MIC 125 µg/ml), dan BTG (MIC 250 µg/ml). Aktivitas hemaglutinasi lektin S. polycystum stabil pada suhu 30-80 oC dan suasana netral hingga basa (pH 7-10), namun kurang stabil pada suasana asam (pH 3-6). Aktivitas lektin T. ornata relatif tidak stabil pada suhu 40-100 oC, sedikit menurun pada pH sangat asam, namun stabil pada rentang pH 5-10. Keberadaan kation divalent Ca2+ dan Mg2+ sedikit menurunkan aktivitas lektin S. polycystum dan T. ornata.

 

ABSTRACT

The ability of lectins to specifically and reversibly bind carbohydrates is an important characteristics for its various applications. This research aims to study the binding specificity of Sargassum polycystum and Turbinaria ornata lectin rich extracts to various types of carbohydrates, the stability of both lectins hemagglutination activities at various temperatures and pH, and the effects of divalent cations on the lectin activities. The lectin binding specificity was studied through qualitative and quantitative hemagglutination inhibition studies. To study their activity stability, both lectins were treated at 30 to 100 oC, treated with various pH buffers (pH 3-10), treated with MgCl2 and CaCl2 followed with hemagglutination assay. Both lectins bound 8 glycoproteins tested, i.e. fetuin (Fe), asialo Fe (aFe), thyroglobulin from bovine (BTG), asialo BTG, thyroglobulin from porcine (PTG), asialo PTG (aPTG), asialo mucin from bovine submaxillary glands (aBSM), and asialo transferrin (aTf) but did not have any affinity to the simple sugars. The S. polycystum lectin bound to aFe and transferrin (MIC 250 µg/ml). Meanwhile, the T. Ornata lectin specifically bound to aPTG (MIC 31.25 µg/ml), PTG (MIC 125 µg/ml), and BTG (MIC 250 µg/ml). The hemagglutination activity of S. polycystum lectin was stable at 30-80 oC and in neutral to alkaline conditions (pH 7-10), but less stable in acidic conditions (pH 3-6). The T. ornata lectin activity was relatively unstable at 40-100 oC, slightly decreased at a very acidic pH, butwas stable in a pH range of 5-10. The presence of Ca2+ and Mg2+ divalent cations slightly decreased the lectins activities.



Keywords


lektin; makroalga; Sargassum polycystum; Turbinaria ornata

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DOI: http://dx.doi.org/10.15578/jpbkp.v13i2.562

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ISSN : 1907-9133(print), ISSN : 2406-9264(online)
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