A novel Bacillus sp. isolated from rotten seaweed: Identification and characterization alginate lyase its produced

DEWI SESWITA ZILDA (Research Center for Marine and Fisheries Product Processing and Biotechnology, Jl.KS Tubun Petamburan VI, 10260, Central Jakarta, Indonesia Indonesia)
YULIYANTI YULIANTI (Program of Biotechnology, Universitas Teknologi Sumbawa. Jl. Raya Olat Maras, Sumbawa 84371, West Nusa Tenggara, Indonesia)
RIZKY FAUZIYAH SHOLIHAH (Research Center for Marine and Fisheries Product Processing and Biotechnology. Jl.KS Tubun Petamburan VI, 10260, Central Jakarta, Indonesia Indonesia)
SUBARYONO SUBARYONO (Research Center for Marine and Fisheries Product Processing and Biotechnology. Jl.KS Tubun Petamburan VI, 10260, Central Jakarta, Indonesia Indonesia)
YUSRO NURI FAWZYA (Research Center for Marine and Fisheries Product Processing and Biotechnology. Jl.KS Tubun Petamburan VI, 10260, Central Jakarta, Indonesia Indonesia)
HARI EKO IRIANTO (Research Center for Marine and Fisheries Product Processing and Biotechnology. Jl.KS Tubun Petamburan VI, 10260, Central Jakarta, Indonesia Indonesia)

Biodiversitas Journal of Biological Diversity
Vol. 20 No. 4 (2019)

Abstract. Zilda DS, Yulianti Y, Sholihah RF, Subaryono S, Fawzya YN, Irianto HE.2019. A novel Bacillus sp. isolated from rotten seaweed: identification and characterization alginate lyase its produced. Biodiversitas 20: 1166-1172. Alginate lyase has been known as potential biocatalyst not only for industrial but also medicinal application especially for the production of oligosaccharides which have distinct bioactivities. An alginate lyase, AlgT513, has been isolated from rotten seaweed bacterium strain T513 and characterized. The bacterium showed low similarity (95%) with Bacillus tequilensis strain 10b based on 16S rDNA sequence indicating that AlgT513may be a novel Bacillus species. The bacterium forms a clear zone on solid medium with 0.5% sodium alginate addition. The optimum temperature and pH were 50ºC and 8 respectively. AlgT513 maintained stability at board pHs of 4-9 and temperature of 45ºC. Metal ions Mg2+, Ca2+ and K+ increase the activity of the enzyme while Zn2+, Co2+ and Li+ strongly inhibit it. NaCl inhibits AlgT513 activity where most of the alginate lyases need it to reach maximum activity. AlgT513 is suggested as a serine metalloenzyme due to inhibition of ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF).