Characterization of agarase enzyme produced by Streptomyces sampsonii isolated from marine sediments of Tanjung Kusu-Kusu, North Sulawesi

Agarase is an enzyme that catalyzes the hydrolysis of agar. Numerous agarases have been obtained from different microorganism genera found in sponges, marine water, and marine sediments. Streptomyces sampsonii from marine sediments of Tanjung Kusu-Kusu, Lembeh, North Sulawesi showed potential as a p...

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Hauptverfasser: Yulianti, Siti Eka, Rachmayati, Rike, Agustriana, Eva, Rahmani, Nanik, Atikana, Akhirta, Lisdiyanti, Puspita, Ratnakomala, Shanti, Yopi, Zilda, Dewi Seswita
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Sprache:eng
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Zusammenfassung:Agarase is an enzyme that catalyzes the hydrolysis of agar. Numerous agarases have been obtained from different microorganism genera found in sponges, marine water, and marine sediments. Streptomyces sampsonii from marine sediments of Tanjung Kusu-Kusu, Lembeh, North Sulawesi showed potential as a producer of agarase with various applications in the cosmeceutical, nutraceutical, and pharmaceutical industries, because they have the ability to produce oligosaccharides with high activity. This study aimed to characterize the agarase enzyme produced by S. sampsonii using commercial substrates. The results showed that the agarase enzyme had the highest activity with an optimum pH of 9.0 using the glycine-NaOH buffer and an optimum temperature of 80 °C. The enzyme activity assay with several metal ions and chemical compounds showed that Fe3+, Mn2+, Ca2+, and Mg2+ were activators, Hg2+, Cu2+, and EDTA were inhibitors, while K+, PEG-600, isopropanol, methanol, ethanol, and TritonX-100 ions had no significant effect on enzyme activity. Hydrolysis and thin layer chromatography have shown that it is capable of hydrolyzing Agar, Agarose, and Euchema cottonii seaweed biomass into Neoagarooligosaccharides such as Neo-agarobiose (NA2), Neo-agarotetraose (NA4), and Neo-agarohexaose (NA6), which can be used in nutrition, cosmetic, pharmaceutical, and industrial applications with further development.
ISSN:0094-243X
1551-7616
DOI:10.1063/5.0183367