Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor

Extraction and partial characterization of lectin from Indonesian Padina australis and Padina minor had been carried out. The crude extract of the P. australis and P. minor were examined for hemagglutination activity (HA) using native and trypsin-treated of rabbit and human A, B, O type erythrocytes...

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Main Authors: Nurrahmi Dewi Fajarningsih, Naomi Intaqta, Danar Praseptiangga, Choiroel Anam
Format: Article
Language:English
Published: Kementerian Kelautan dan Perikanan 2019-12-01
Series:Squalen
Subjects:
Online Access:https://www.bbp4b.litbang.kkp.go.id/squalen-bulletin/index.php/squalen/article/view/400
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spelling doaj-4a4d4a115a6d4961a711817a206b69f22020-11-25T01:36:33ZengKementerian Kelautan dan PerikananSqualen2089-56902406-92722019-12-0114310311110.15578/squalen.v14i3.400254Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minorNurrahmi Dewi Fajarningsih0Naomi Intaqta1Danar Praseptiangga2Choiroel Anam3Research Center for Marine and Fisheries Product Processing and BiotechnologyUNSUNSUNSExtraction and partial characterization of lectin from Indonesian Padina australis and Padina minor had been carried out. The crude extract of the P. australis and P. minor were examined for hemagglutination activity (HA) using native and trypsin-treated of rabbit and human A, B, O type erythrocytes. Both extracts agglutinated all of the trypsin-treated erythrocytes tested in the HA assay. Strong HA was detected in the crude extract of P. minor with trypsin-treated of human type A and O erythrocytes. However, the sugar-binding specificity study through the quantitative hemagglutination inhibition (HI) assay showed that P. minor extract could not specifically recognize the glycans tested. Apparently, the HA of the P. minor was more due to its co-extracted polyphenols content than its lectin content. On the other hand, the HI assay showed that asialo transferrin human (aTf) and asialo porcine thyroglobulin (aPTG) were the most powerful in inhibiting the HA of P. australis. Those indicated that P. australis protein extract was able to specifically recognized aTf and aPTG. The stability of P. australis and P. minor HA over various temperatures, pH ranges, and divalent cations studies showed that the P. minor HA was stable on a wide range of pH and temperature; not affected by the presence of EDTA, but decreased by Ca2+ and Mg2+ additions showed that P. minor protein extract  was not a metallic protein. The HA of P. australis decreased at 60 oC and was inactivated at 90 oC; increased at strong acidic (pH 3 & 4) and strong basic (pH 9 & 10) and dependent by the presence of either EDTA or Ca2+ and Mg2+ divalent cation.https://www.bbp4b.litbang.kkp.go.id/squalen-bulletin/index.php/squalen/article/view/400hemagglutinin, brown seaweed, phaeophyta, padina australis, padina minor
collection DOAJ
language English
format Article
sources DOAJ
author Nurrahmi Dewi Fajarningsih
Naomi Intaqta
Danar Praseptiangga
Choiroel Anam
spellingShingle Nurrahmi Dewi Fajarningsih
Naomi Intaqta
Danar Praseptiangga
Choiroel Anam
Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor
Squalen
hemagglutinin, brown seaweed, phaeophyta, padina australis, padina minor
author_facet Nurrahmi Dewi Fajarningsih
Naomi Intaqta
Danar Praseptiangga
Choiroel Anam
author_sort Nurrahmi Dewi Fajarningsih
title Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor
title_short Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor
title_full Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor
title_fullStr Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor
title_full_unstemmed Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor
title_sort extraction and partial characterization of lectin from indonesian brown algae padina australis and padina minor
publisher Kementerian Kelautan dan Perikanan
series Squalen
issn 2089-5690
2406-9272
publishDate 2019-12-01
description Extraction and partial characterization of lectin from Indonesian Padina australis and Padina minor had been carried out. The crude extract of the P. australis and P. minor were examined for hemagglutination activity (HA) using native and trypsin-treated of rabbit and human A, B, O type erythrocytes. Both extracts agglutinated all of the trypsin-treated erythrocytes tested in the HA assay. Strong HA was detected in the crude extract of P. minor with trypsin-treated of human type A and O erythrocytes. However, the sugar-binding specificity study through the quantitative hemagglutination inhibition (HI) assay showed that P. minor extract could not specifically recognize the glycans tested. Apparently, the HA of the P. minor was more due to its co-extracted polyphenols content than its lectin content. On the other hand, the HI assay showed that asialo transferrin human (aTf) and asialo porcine thyroglobulin (aPTG) were the most powerful in inhibiting the HA of P. australis. Those indicated that P. australis protein extract was able to specifically recognized aTf and aPTG. The stability of P. australis and P. minor HA over various temperatures, pH ranges, and divalent cations studies showed that the P. minor HA was stable on a wide range of pH and temperature; not affected by the presence of EDTA, but decreased by Ca2+ and Mg2+ additions showed that P. minor protein extract  was not a metallic protein. The HA of P. australis decreased at 60 oC and was inactivated at 90 oC; increased at strong acidic (pH 3 & 4) and strong basic (pH 9 & 10) and dependent by the presence of either EDTA or Ca2+ and Mg2+ divalent cation.
topic hemagglutinin, brown seaweed, phaeophyta, padina australis, padina minor
url https://www.bbp4b.litbang.kkp.go.id/squalen-bulletin/index.php/squalen/article/view/400
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