OPTIMASI DAN KARAKTERISASI a-AMILASE DARI ISOLAT AKTINOMISETES YANG BERASAL DARI KALIMANTAN TIMUR

Yati Sudaryati Soeka
10.14203/beritabiologi.v10i3.751
| Abstract views: 841 | PDF views: 4567

Abstract

Forty-one actinomycetes isolates from East Kalimantan held in Microbiology Division Collection-UPI, and their ability to produce a-amylase has been assessed. Those 41 number of actinomycetes isolates performed amylolytic activity as shown by clear zone areal after being poured with iodium solution. The bacteria produced high a-amylase when was grown in media containing starch soluble 2% the a-amylase activity in media containing 8.24 U/ml. The isolate (number 7) was the most active compared to another (number 100) and it was identified as Nocardia; the activity of this enzyme obtained was 12.93 U/ml (one unit activity is defined as mol of glucose produced per ml per minute). The maximum temperature for enzyme reaction was 40°C, optimum pH was pH 7.5 the a-amylase activity were 15.76 U/ml and 31.11 U/ml, respectively. From kinetic characterization study, it was found that enzyme showed Km and Vmax value of 7.62 % (b/v) and 71.10- umol/ml/minute respectively at condition of temperature 40°C, pH 7.5 and incubation time 10 minute.

Keywords

amilase, aktinomisetes/actinomycetes, karakterisasi/characterization, Nocardia, Streptomyces.

Full Text:

PDF

References

Alam R, Y Teramoto dan S Hayashida. 1989. Characteristic of raw starch digestible saccharifying a-amylase from Bacillus substilis 3018. Annual Report of ICBiotech. Osaka University, Japan.

Bansode SD. 2010. Screening of nutritional components for a- amylase production in submerged fermentation by Bacteria Isolated from soil using Plackett-Burman Design. International Journal of Pharmacy and Pharmaceutical Sciences 2(1), 91-98.

Bernfeld O. 1995. Amylases a & B. In: Methods in Enzymology and Related of Biochemistry 1. SP Colowick and NO Kaplan (Eds). Academic Press, New York.

Jamilah I, A Meryandini, I Rusmana, A Suwanto and NR Mubarik. 2009. Activity of proteolilytic and amylolytic enzymes from Bacillus spp. isolated from shrimp ponds. J. Microbiology Indonesia 3(2), 67-71.

Kim CH. 1995. Characterization and substrate specificity of an endo-B-l,4-D-glucanase I (Avicelase I) from an extracellular multienzyme complex of Bacillus circulans. Appl Environ Microbial 61, 959-965.

Kiran O, U Comlekcloglu and B Arihan. 2005. Effects of carbon sources and various chemicals on the production of a novel amylase from thermophillic Bacillus sp. K-12. Turk J.Biol. 29, 99-103.

Madigan MT, JM Martiko and J Parker. 2003. Biology of Microorganisms. Tenth Edition. Pearson Education, Inc. USA.

Mangunwardoyo W, M Takano and I Shibasaki. 1982. Preservation and Utilization of a Concentrated Seed Culture for Bacterial Amylase Production. Annual Reports of ICME 5, Osaka University, Osaka, Japan.

Naiola E. 2001. Karakterisasi amilase dari isolat bakteri yang berasal dari Bali dan Lombok. Jurnal Biologi Indonesia 3(1), 32-42.

Nigam P and D Singh. 1995. Enzyme and microbial system involved in starch processing. Enzyme Microb Technol 17, 770-778.

Nikolov Z and PJ Reilly. 1993. Enzymatic depolymerization of starch. In: JS Dordick (Ed.). Biocatalysists for Industry, 37-62. Plenum, New York.

Nurkanto A. 2007. Identifikasi aktinomisetes tanah hutan pasca-kebakaran Bukit Bangkirai, Kalimantan Timur dan potensinya sebagai pendegradasi selulosa dan pelarut fosfat. J. Biodiversitas 8(4), 314-319.

Nurkanto A, M Rahmansyah dan A Kanti, 2008. Teknik lsolasi Aktinomisetes. LIPI-Press.

Sadikin M. 2002. Biokimia Enzim. Widya Medika, Jakarta.

Thontowi A, Puspaningsih, S Hadi, Purkan, Ni'mahtuzahroh dan B Irawan. 2002. Pencirian produksi amilase oleh Saccharomyces cerevisiae W303A rekombinan. J. Biologi Indonesia 3(3), 169-174.

Vihinen M and P Manstala. 1989. Critical Reviews in Biochemistry and Moleculer Biology 24, issue 4. Departement of Biochemistry. University of Turku. Turku.

Volk WA and MF Wheeler. 1988. Mikrobiologi Dasar. Jilid 1. S Adisoemarto (Ed.). Erlangga, Jakarta. Terjemahan dari Basic Microbiology 5* Ed.

DOI: https://doi.org/10.14203/beritabiologi.v10i3.751

Refbacks

  • There are currently no refbacks.