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Characterization of Thermostable Chitin Deacetylase from Bacteria Strain Pancuran Tujuh, Baturaden, Center of Java Siswa Setyahadi; Tatit K Bunasor; Deuxianto Hendarsyah
Jurnal Teknologi dan Industri Pangan Vol. 17 No. 1 (2006): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

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Chitin deacetylase is the enzymes that has important role in converting chitin to chitosan. In nature, chitin is the second most abundant natural biopolymer after cellulose. Generally, chitin easily obtained from outer shell of crustaceans, arthropods, and also detectable on cell wall of some type of fungal (Zygomycetes). The chitin deacetylase was isolated from Bacillus sp PT2-3. It was found that the highest specific activity was attained at pH 8 60C. The addition of 5 mM Zn2+ and 5 mM Mn2+ increased the specific activity of the enzyme, 4.39% and 7.8%, respectively, and the increase was only 2.19% when the addition was 2 mM Mn2+. On the contrary the addition of Ca2+, Mg2+ and Fe2+ decrease the specific activity 46.83%, 41.22% and 47.32%, respectively. The enzyme activity was relatively stable at 600C for 60 minutes, while lengthen the time to 90 minutes, decreased the activity 15.05 %, and the decrease was 26.13% at temperature of 700C for 180 minutes. Key words: chitin deacetylase, Bacillus, thermostabil

Screening of Lactic Acid Bacteria for the Purpose of Chitin Recovery Processing SISWA SETYAHADI
Microbiology Indonesia Vol. 1 No. 1 (2007): April 2007
Publisher : Indonesian Society for microbiology

Lactic acid fermentation has been studied as an alternative method of chitin recovery from the natural chitin compounds, such as shrimp waste. The purpose of this research was to identify a potential lactic acid bacterium which can produce large amount of lactic acid and has the ability to release chitin (demineralization) from shrimp-shell-waste. Among 11 bacteria tested, strain 15 was the strongest lactic acid producer yielding 1.09% (v/v) lactic acid in the media with a pH of 4.15 after 6 days incubation at 37 oC. After that, strains 17 and 23 produced 0.79 and 0.74% of lactic acid respectively. These three strains were selected for further experiments on various kinds of media using two-day incubation periods. No strains produced lactic acid well in MRS media containing lactose. The best medium for lactic acid production by strains 15 and 17 was MRS containing glucose, molasses or mixture of molasses and shrimp shell waste. Fermentation of shrimp shell waste using strain 15 caused an increase of viscosity reflecting an increase of soluble chitin in the media..

Effect of pH, Temperature and Medium Composition on Xylanase Production by Bacillus sp. AQ-1 and Partial Characterization of the Crude Enzyme BUDIASIH WAHYUNTARI; NISA RACHMANIA MUBARIK; SISWA SETYAHADI
Microbiology Indonesia Vol. 3 No. 1 (2009): April 2009
Publisher : Indonesian Society for microbiology

Bacillus sp. AQ-1 was isolated from household aquarium sediment. The isolate produced extracellular xylanolytic enzymes on xylan containing agar medium. Based on morphological, and physiological analysis, the isolate was identified as Bacillus sp. AQ1. The effect of temperature and pH on isolate growth and xylanase production were observed. The best condition observed for the enzyme production in Luria Broth supplemented with 0.5% oat spelt xylan medium was at 40 °C pH 7. The maximum enzyme production was 0.23 U mL-1 after 20 h of fermentation. Two different medium compositions (A and B) were examined for xylanase production. The maximum growth of the isolate and the xylanase production was better in A medium. Replacing oat spelt xylan in medium A with fruitless oil palm bunch in the medium caused the growth slightly slower than that of in the original formula. However, the xylanase production was 3 times higher in fruitless oil palm bunch medium. Optimum activity of the crude enzyme was observed at 60 °C and pH 7. Each ml of the crude enzyme contained 55.21 U xylanase, 8.12 U amylase and 0.50 U carboxymethylcellulase

Production and Purification of Xylanase From Indonesian Isolate Bacillus sp. AQ-1 Grown on Bunch Palm Oil PUJI RAHAYU; SISWA SETYAHADI; . HARMITA
Microbiology Indonesia Vol. 3 No. 1 (2009): April 2009
Publisher : Indonesian Society for microbiology

Xylanase (endoxylanase, EC 3.2.1.8) is a commercial enzyme that has been applied in the industrial production of fuel, food, textiles and paper. Xylanase was isolated from the culture supernatant of Bacillus sp. AQ-1 grown on Nakamura medium containing 0.5% powder bunch palm oil. The optimum pH and temperature of xylanase activity were pH 7.0 and 60 °C, respectively. The enzyme was purified by anion exchange chromatography using DEAE-Sepharose-Fast-Flow column and gel filtration chromatography using Sephacryl S-300 column. The results showed that purification of xylanase produced two forms of xylanase, which were identified as xylanase A and xylanase B. Xylanase A can be separated from xylanase B by ultrafiltration using a 30 kDa polyethersulfone membrane. The molecular weight of xylanase A and B were 15.7 and 57.7 kDa, respectively.

Selection of Methods for Microbiological Extraction of Chitin from Shrimp Shells JUNIANTO JUNIANTO; BUDIASIH WAHYUNTARI; SISWA SETYAHADI
Microbiology Indonesia Vol. 7 No. 2 (2013): June 2013
Publisher : Indonesian Society for microbiology

Chitin extraction from shrimp shells involves two processing steps that are demineralization followed by deproteination process. Lactobacillus acidophilus FNCC 116 and Bacillus licheniformis F11.1 were used in demineralization and deproteination respectively. The overall objectives of this experiment were to determine fermentation systems which resulted in the highest mineral and protein removal. The demineralization experiments consisted of three different batch fermentation designs: batch fermentation (Am ); subsequent batch fermentation 1, in which 100% medium was replaced with fresh medium after 24 h fermentation (Bm ); and subsequent batch fermentation 2, in which 50% medium was replaced with the same amount of fresh medium after 24 h fermentation (Cm ). The demineralization was conducted at 30±2 °C, 50 rpm for 60 h. The deproteination experiments consisted of 3 different batch fermentation designs: batch fermentation 1, inoculum was added once at the beginning of the fermentation (A p); batch fermentation 2, inoculum was added twice, at the beginning and after 24 h fermentation (Bp ); and subsequent batch fermentation, 100% medium was replaced with fresh medium after 24 h fermentation (Cp ). The deproteination was carried out at 55 °C, pH 7.8-8.0, aeration 2.3 vvm, and agitation 275 rpm for 96 h. The experimental results showed that in the demineralization process, fermentation design B gave the highest ash removal. Ash removed in the fermentation design A , B , and C was 97.19, 99.69, and 97.69%, respectively. The protein removed in the fermentation design A , B , and C was 94.42, 94.51, and 95.37%, respectively.

PURIFIKASI DAN KARAKTERISASI ENZIM KOLAGENASE DARI Bacillus sp. KUB BPPT CC DENGAN MENGGUNAKAN SUBSTRAT KOLAGEN DARI KULIT CEKER AYAM Melia Febrina; Siswa Setyahadi; Churiyah
CERATA Jurnal Ilmu Farmasi Vol 13 No 1 (2022): Cerata Jurnal Ilmu Farmasi
Publisher : UNIVRSITAS MUHAMMADIYAH KLATEN

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Kolagenase merupakan endopeptidase yang dapat memecah domain triple helix dari kolagen. Sumber utama substrat kolagen yang digunakan pada penelitian ini adalah kulit ceker ayam, untuk memanfaatkan limbah dari Rumah Potong Ayam dengan jumlah cukup banyak. Ceker ayam merupakan salah satu bagian dari tubuh ayam yang kurang diminati, terdiri atas komponen kulit, otot dan tulang dengan kandungan kolagen yang tinggi pada bagian kulit. Karakteristik kolagen dari sumber yang berbeda menghasilkan karakteristik enzim kolagenase yang berbeda pula. Sehingga dibutuhkan informasi mengenai karakteristik enzim dan aktivitas enzim yang optimum. Penelitian ini bertujuan untuk ekstraksi kolagen, penentuan berat molekul kolagen, karakterisasi kolagen, produksi kolagenase, pemurnian enzim kolagenase, karakterisasi enzim kolagenase crude dan murni. Produksi kolagenase dengan menggunakan media Luria Bertani Broth (LB) cair dan menambahkan 5% kulit ceker ayam. Fermentasi dengan Bacillus sp. KUB BPPT CC dengan variasi waktu 24, 36 dan 48 jam. Waktu produksi optimum adalah 36 jam dengan aktivitas kolagenase 0,1001 U/ml. Pemurnian enzim dilakukan dengan presipitasi amonium sulfat mulai dari konsentrasi 0 hingga 80%, dimana hasil aktivitas optimum dengan presipitasi amonium sulfat 60% (b/v), dilanjutkan dengan kromatografi kolom DEAE Sephadex A-50. Pengendapan dengan amonium sulfat mengakibatkan pemurnian 2,43 kali lipat. Setelah pemurnian dengan kolom DEAE Sephadex A-50, enzim dimurnikan 11,21 kali lipat. Berat molekul enzim kolagenase 42 kDa. Aktivitas optimum kolagenase crude dan murni pada suhu 50oC. Enzim crude memiliki pH optimum 10, sedangkan enzim yang dimurnikan pada pH 7. Pada pengujian aktivitas kolagenase digunakan substrat yang berasal dari kulit ceker ayam. Metode ekstraksi kolagen tergolong kedalam kolagen larut asam dengan uji kolagen yaitu Nilai rendemen kolagen 9,475%, Nilai pH 6,8, Kadar air 5%, Kadar Abu 0,6%, Kadar protein 0,425 mg/ml dan Berat molekul kolagen 130 kDa .

PURIFIKASI DAN KARAKTERISASI ENZIM KOLAGENASE DARI Bacillus sp. KUB BPPT CC DENGAN MENGGUNAKAN SUBSTRAT KOLAGEN DARI KULIT CEKER AYAM Melia Febrina; Siswa Setyahadi; Churiyah
CERATA Jurnal Ilmu Farmasi Vol 13 No 1 (2022): Cerata Jurnal Ilmu Farmasi
Publisher : Universitas Muhammadiyah Klaten

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.61902/cerata.v13i1.454

Kolagenase merupakan endopeptidase yang dapat memecah domain triple helix dari kolagen. Sumber utama substrat kolagen yang digunakan pada penelitian ini adalah kulit ceker ayam, untuk memanfaatkan limbah dari Rumah Potong Ayam dengan jumlah cukup banyak. Ceker ayam merupakan salah satu bagian dari tubuh ayam yang kurang diminati, terdiri atas komponen kulit, otot dan tulang dengan kandungan kolagen yang tinggi pada bagian kulit. Karakteristik kolagen dari sumber yang berbeda menghasilkan karakteristik enzim kolagenase yang berbeda pula. Sehingga dibutuhkan informasi mengenai karakteristik enzim dan aktivitas enzim yang optimum. Penelitian ini bertujuan untuk ekstraksi kolagen, penentuan berat molekul kolagen, karakterisasi kolagen, produksi kolagenase, pemurnian enzim kolagenase, karakterisasi enzim kolagenase crude dan murni. Produksi kolagenase dengan menggunakan media Luria Bertani Broth (LB) cair dan menambahkan 5% kulit ceker ayam. Fermentasi dengan Bacillus sp. KUB BPPT CC dengan variasi waktu 24, 36 dan 48 jam. Waktu produksi optimum adalah 36 jam dengan aktivitas kolagenase 0,1001 U/ml. Pemurnian enzim dilakukan dengan presipitasi amonium sulfat mulai dari konsentrasi 0 hingga 80%, dimana hasil aktivitas optimum dengan presipitasi amonium sulfat 60% (b/v), dilanjutkan dengan kromatografi kolom DEAE Sephadex A-50. Pengendapan dengan amonium sulfat mengakibatkan pemurnian 2,43 kali lipat. Setelah pemurnian dengan kolom DEAE Sephadex A-50, enzim dimurnikan 11,21 kali lipat. Berat molekul enzim kolagenase 42 kDa. Aktivitas optimum kolagenase crude dan murni pada suhu 50oC. Enzim crude memiliki pH optimum 10, sedangkan enzim yang dimurnikan pada pH 7. Pada pengujian aktivitas kolagenase digunakan substrat yang berasal dari kulit ceker ayam. Metode ekstraksi kolagen tergolong kedalam kolagen larut asam dengan uji kolagen yaitu Nilai rendemen kolagen 9,475%, Nilai pH 6,8, Kadar air 5%, Kadar Abu 0,6%, Kadar protein 0,425 mg/ml dan Berat molekul kolagen 130 kDa .

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