Nelly Marliani, Winni Astuti, Rudi Kartika

Kondisi Kerja Optimum Lipase Bakteri Endofit dari Daun Macaranga hullettii King ex Hook.f.

Introduction

Kondisi kerja optimum lipase bakteri endofit dari daun macaranga hullettii king ex hook.f.. Penelitian mengisolasi & mengkarakterisasi lipase ekstraseluler dari bakteri endofit daun Macaranga hullettii. Temukan kondisi optimum lipase serta pengaruh ion dan pelarut.

Abstract

Lipase ekstraseluler telah berhasil diisolasi dari bakteri endofit daun Macaranga hullettii King ex hook f.. Skrining lipase ekstraseluler menggunakan media nutrien agar yang mengandung minyak zaitun dan rodhamin B. Hasil skriining menunjukkan terdapat 6 isolat bakteri endofit yang menghasilkan lipase ekstraseluler. Selanjutnya, lipase dari salah satu dari 6 isolat dikarakterisasi. Lipase diproduksi selama 72 jam. Karakterisasi kondisi kerja optimal lipase berada pada suhu 40oC, pH 8 dan konsentrasi minyak zaitun optimal 1,5%. Lipase diaktivasi oleh ion Ca2+, K+ , Mg2+ dan dihambat oleh ion Ba2+. Lipase stabil dalam pelarut etanol dan terganggu stabilitasnya pada pelarut eter dan n-heksana.

Review

This study presents an investigation into extracellular lipases produced by endophytic bacteria isolated from *Macaranga hullettii* leaves. The work successfully identifies bacterial isolates capable of lipase production, followed by a characterization of the optimal working conditions for one selected lipase. Lipases, particularly those from microbial sources like endophytes, are highly valuable biocatalysts with broad applications in various industries, including food, pharmaceutical, and chemical sectors. Exploring novel sources for these enzymes, as demonstrated here, is crucial for discovering enzymes with unique properties that could offer advantages for specific industrial processes. The methodology involved a screening process using nutrient agar supplemented with olive oil and rhodamine B, leading to the identification of six promising endophytic bacterial isolates. Further characterization of one selected lipase revealed its optimal activity at 40°C and pH 8, with an optimal olive oil concentration of 1.5%. The lipase production was observed over 72 hours. Importantly, the study also identified specific ions that activate (Ca2+, K+, Mg2+) and inhibit (Ba2+) the enzyme's activity. Furthermore, its stability profile in different organic solvents was assessed, showing good stability in ethanol but instability when exposed to ether and n-hexane. Overall, this research provides a foundational characterization of a potentially valuable lipase from a novel endophytic source. The identification of optimal temperature, pH, and substrate concentration, along with ion effects and solvent stability, are critical initial steps in understanding the enzyme's potential. To enhance the impact of this work, future studies should focus on the genetic identification of the producing bacterium, purification of the lipase to homogeneity, determination of its specific activity and kinetic parameters, and further exploration of its stability under various industrial conditions. Such detailed characterization would greatly strengthen the potential for this lipase to be utilized in practical applications, contributing to the growing field of sustainable biocatalysis.

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