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Production and Characterization od Xylanase from Actinomyces ATG 70 Using CornCob Xylan Substrate Farrennina, Tasya Preira; Putri, Amelia Fahreza; Arimurti, Sattya; Winarsa, Rudju; Utarti, Esti
Jurnal ILMU DASAR Vol. 26 No. 2 (2025)
Publisher : Fakultas Matematika dan Ilmu Pengetahuan Alam Universitas Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.19184/jid.v26i2.53702

Abstract

Xilan is a polysaccharide that can be used as a substrate for producing xylanase. Xylan can be obtained from processing xylan-rich agricultural waste such as corn cobs, which contain 12.4% xylan. Xilan can be hydrolyzed into xylose and xylooligosaccharide (XOS) using the enzyme Xilanase. Actinomycetes have dominant xylanolytic species, Actinomyces ATG 70 has semi-qualitative xylanolytic ability with an enzyme activity index of 3.21±0.55 in xylan media. This study was conducted by extracting xylan from corn cobs, rejuvenating Actinomyces ATG 70, preparing the inoculum, creating a standard curve, producing xylanase with pH optimization of the medium, testing xylanase activity, characterizing the pH and temperature of crude xylanase, and identifying the morphology and biochemical characteristics of Actinomyces ATG 70. Optimization of the pH of the xylanase production medium was achieved at pH 8, with xylanase activity of 10.07±0.13 U/mL. The crude xylanase was characterized for pH and temperature effects, and the optimal pH for crude xylanase was found to be pH 6 with xylanase activity of 7.64±0.66 U/mL, and the optimal temperature was 50°C with xylanase activity of 11.17±0.33 U/mL. The identification results showed that Actinomyces ATG 70 belongs to Gram-positive bacteria, with a positive catalase test, white colonies, cream-colored aerial mycelium, and cream-colored pigmentation. The spore structure consists of long chains of conidia, streptococcus-shaped cells, and can form aerial mycelium, thus the isolate belongs to the genus Streptomyces.
Activity of an A-L-Rhamnosidase Produced by Aspergillus niger During Solid State Fermentation of Coffee Pulp Wastes Muzakhar, Kahar; Winarsa, Rudju
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 Muzakhar, Kahar; Elida, Farah Salma; Putrasetya, Ramdhan; Siswoyo, Siswoyo; Winarsa, Rudju; Wiyono, Hidayat Teguh
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.