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All Journal International Journal of Biosciences and Biotechnology Jurnal Ilmu Dasar IPTEK Journal of Proceedings Series BERKALA SAINSTEK Biogenesis: Jurnal Ilmiah Biologi Biotropika Pelita Perkebunan Journal of Mathematical and Fundamental Sciences Jurnal Biodjati BIOSFER : Jurnal Biologi dan Pendidikan Biologi JATI EMAS (Jurnal Aplikasi Teknik dan Pengabdian Masyarakat) Journal of Natural Sciences
Kahar Muzakhar
Department Of Biology, Faculty Of Mathematics And Natural Science, University Of Jember, Indonesia
Agriculture, Biological Sciences & Forestry Humanities Astronomy Biochemistry, Genetics & Molecular Biology Chemistry Computer Science & IT Control & Systems Engineering Earth & Planetary Sciences Education Engineering Environmental Science Immunology & microbiology Mathematics Physics Public Health Other

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Purification and Characterization of Cellulase of Mold Isolated from Vermicomposting Process of Palm Oil Empty Fruit Bunches Rosita Fitrah Dewi; Kahar Muzakhar
Jurnal Biodjati Vol 3 No 1 (2018): May
Publisher : UIN Sunan Gunung Djati Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15575/biodjati.v3i1.2292

Abstract

In previous investigation of vermicomposting process of palm oil empty fruit bunches, five cellulase-producing microorganisms had been isolated. An isolated VTM1 identified as Aspergillus sp. as a cellulase producing mold, and proven produced extracellular cellulase in solid state fermentation of palm oil empty fruit bunches. The obtaining crude cellulase was purified to homogeneity by ammonium sulfate precipitation, gel filtration on Sephadex G-100 chromatography, and finally purified on ion exchange chromatography on DEAE Cellulofine A-500. The yield and purification fold were 12.89% and 107.50, respectively. The purified cellulase was easily released glucose when 5% CMC applied as substrate, as shown by TLC analysis. The purified cellulase had an optimal pH and temperature at 4.0 and 45°C, and was stable at pH 3-7 and 30-50°C, respectively.
Activity of an A-L-Rhamnosidase Produced by Aspergillus niger During Solid State Fermentation of Coffee Pulp Wastes Kahar Muzakhar; Rudju Winarsa
Jurnal Biodjati Vol 4 No 1 (2019): May
Publisher : UIN Sunan Gunung Djati Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15575/biodjati.v4i1.4411

Abstract

 An α-L-Rhamnosidase released by Aspergillus niger during solid-state fermentation (SSF) using coffee pulp (CP) wastes media has been investigated. The activity of α-L-Rhamnosidase based on reducing sugar production against 2% CP alkali extract substrate in 50 mM acetate buffer pH 5. The maximum activity of α-L-Rham-nosidase was obtained in sixth-day SSF with reducing sugar pro-duction of 13 μg/mL. The enzyme is actively hydrolyzed 0.1% p-ni-trophenyl-α-L-rhamnopyranoside (PNP-Rha) to 95% from initial concentration. Purification using DEAE-Toyopearl 650M increased hydrolysis activity ten times against the substrate, reaching 134 μg/mL of reducing sugar. Optimum enzyme activity at pH 4.5 and 50°C, while stable at pH and temperature in a pH range of 3.5-7 and below 50°C. 
An Extracellular Pectinase from ISH16 Bacteria Isolated Induced by Coffee Pulp Waste Substrate Kahar Muzakhar; Farah Salma Elida; Ramdhan Putrasetya; Siswoyo Siswoyo; Rudju Winarsa; Hidayat Teguh Wiyono
Jurnal Biodjati Vol 7 No 2 (2022): November
Publisher : UIN Sunan Gunung Djati Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15575/biodjati.v7i2.20279

Abstract

An α-1,4-glycosidic bonds galactoses pectin, mainly composed of a D-galacturonic acid chain, are important biomaterial widely used in industries. Utilizing this material, a bioprocess, including the biocatalysis pectinase, is often needed. Pectinase production was optimized in 7 days SSF at 37°C, and the pectinase activities were daily measured by the method of Somogy-Nelson. The optimum pectinase production was 0.166 U/ml on the fourth day SSF. Purification using open column ion exchange chromatography DEAE cellulose DE-52 resulted in 1030.9 folds of pectinase purity with a yield of 25.9%. The enzyme was at optimal activity at pH six and attended stable in the pH range of 5.5-8, while optimal activity at a temperature of 50°C and was stable in the range of 30-45°C. The pectinase activity increased by 120% with the addition of 10 mM Mg2+, and 95% retained when 10 mM Ca2+ was added. The presence of 10 mM Na+, K+, and Fe2+ resulted in a slight effect of activity at 85%, 83%, and 78%. However, it was strongly inhibited by 10 mM Al3+ and retained 25%. Based on the results above, the microbial utilization of coffee pulp waste by ISH16 bacteria pectinolytic is one opportunity to produce valuable pectinase with low-cost production, so comprehensive examination in large-scale production is needed too. In this paper, all research detail steps were described.
Co-Authors AA Sudharmawan, AA Agus Subekti Ahmad Bukhari Saragih Alya, Fathia Anisa Azhari, Fitri Esti Utarti Farah Salma Elida Gatot Kusiyanto Hidayat Teguh Wiyono Kartika Senjarini Khafiyya, Nida An Khofiya, Zunairoh Nidaan Khofiya, Zunairoh Nidaan Kusumah, Maulana S. Nuryatmaja Gora Pawana Purwatiningsih Purwatiningsih Purwatiningsih Purwatiningsih Purwatiningsih Purwatiningsih Ramdhan Putrasetya Reza Billa Afifuddin Rosita Fitrah Dewi Rosyanda Fisel Kosaya S Siswanto Sattya Arimurti Siswanto Siswanto Siswoyo Siswoyo Sururin, Fahma Wardah Sutoyo S Sutoyo Sutoyo Ummi Wasilah Winarsa, Rudju