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"Enzim peroksidase adalah enzim yang mengkatalisis reaksi oksidasi sejumlah substrat yang merupakan donor hidrogen seperti asam askorbat, benzidin , pirogalol. dan fenol oleh hidrogen perokslda. Enzim ini banyak memberikan manfaat baik dalam bidang medis maupun industri. Oleh karena itu perlu dilakukan pencarian sumber peroksidase, salah satunya adalah jamur Corttnaiias msgnivetatus. Penetitian rnr bertujuan untuk mengisolasi enzim peroksidase dan jamur Cortinarius magnivelatus dan memurnikannya secara parsial serta mengkarakterisasi enzim yang telah terisolasi tersebut. Telah dilakukan isolasi enzim peroksidase dan jamur Cortinarius magnivelatus yang menghasilkan enzim ekstrak kasar dengan nilai aktivitas spesifik 0.249 U/mg. Pemumian secara parsial dilakukan dengan cara fraksionasi dengan garam ammonium sulfat, dialisis, dan kromatografi penukar anion DEAE-Selulosa dengan pengelusi buffer fosfat 0.05 M pH 8,0; buffer fosfat 0.05 M pH 7,0; dan buffer fosfat 0.2 M pH 7,0. Tahap pemumian dengan cara Fraksionasi menggunakan ammonium sulfat (55 %) dihasilkan enzim dengan nilai aktivitas spesifik sebesar 0,626 U/mg dan tingkat kemurnian 2,514 kali. Sedangkan tahap pemumian dengan kromatografi kolom DEAE Selulosa menghasilkan enzim peroksidase dengan aktivitas spesifik sebesar 9.788 U/mg dan tingkat kemumian 39.309 kali dari ekstrak kasamya. Karakteristik dilakukan dengan menentukan pH dan suhu optimum, kinetlka reaksi enzim peroksidase dan uji kualitatif dalam mengkatallsis pembentukan senyawa polimer. Hasil pengujian karakteristik terhadap enzim peroksidase terisoiasi tersebut menunjukkan bahwa enzim peroksidase terisoiasi memiliki aktivitas maksimum pada pH 7,0; dan suhu optimum 30°C, dengan nilai Km sebesar 0.0026 M. Uji kualitatif pembentukan senyawa polimer dari guaiakol dengan katalis enzim peroksidase menunjukkan hasil positif dengan terbentukhya warna merah kecoklatan dibanding blanko."

"Produksi industri pakaian di Indonesia mengalami pertumbuhan signifikan sebesar 15,29 persen. Hal ini dapat meningkatkan risiko kerusakan lingkungan akibat limbah pewarna tekstil. Pewarna tekstil bersenyawa Azo yang digunakan industri-industri tekstil adalah limbah yang sulit terurai dan pada kadar tertentu bersifat karsinogenik (Chung K. T., 2016). Diperlukan suatu cara untuk mengolah limbah perwarna tekstil. Salah satu caranya adalah memanfaatkan mikroorganisme yang menghasilkan enzim ligninolitik. Tujuan dari penelitian ini adalah mendapatkan fraksi enzim mangan peroksidase dari kultur jamur termofilik dengan purifikasi menggunakan ammonium sulfat dan kromatografi penukar anion untuk proses dekolorisasi limbah pewarna tekstil. Isolat jamur dari penelitian sebelumnya diremajakan kembali di media Potato Dextrose Agar + filtrat daun nanas. Kultivasi kultur dilakukan di campuran media Potato Dextrose Broth, serbuk daun nanas, dan trace element. Fraksi enzim MnP didapatkan dari fraksinasi dengan ammonium sulfat pada saturasi 65% dan didialisis dengan alat MW cut-off 8000-14000 Da dan enzim MnP murni dari purifikasi dengan kromatografi penukar anion menggunakan DEAE Cellulose. Hasil menunjukkan bahwa, uji aktivitas enzim dan aktivitas speksifik Enzim MnP dari purifikasi dengan ammonium sulfat sebesar 1,008 U/mL dan 48,956 U/mg ; purifikasi dengan DEAE Cellulose sebesar 1,061 U/mL dan 51,497 U/mg. Dekolorisasi limbah pewarna tekstil dilakukan di suhu 50°C, selama 144 jam, pH 5,5, dan konsentrasi enzim-substrat sebesar 1:1.

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The production of the clothing industry in Indonesia experienced significant growth of 15.29 percent (Ministry of Industry, 2019). This can increase the risk of environmental damage due to textile dye waste. Azo compound textile dyes used by textile industries are waste that is difficult to decompose and to some extent carcinogenic (Chung K. T., 2016). A method is needed to process textile dye waste. One way is to utilize microorganisms that produce ligninolytic enzymes. The purpose of this study is  to obtain the fraction of Manganese peroxidase Enzyme from thermophilic mushroom culture by purification using ammonium sulphate and anion exchange chromatography for the decolorization process of textile dye waste. Fungal isolates from previous studies (Anas, 2022) were rejuvenated in Potato Dextrose Agar + pineapple leaf filtrate media. Culture cultivation was carried out in a mixture of Potato Dextrose Broth media, pineapple leaf powder, and trace elements.The MnP enzyme  fraction was obtained from fractionation with ammonium sulfate at 65% saturation and dialysis with MW cut-off 8000-14000 Da and pure MnP enzyme from purification by anion exchange chromatography using DEAE Cellulose. The results showed that the test of enzyme activity and spective activity of MnP Enzyme from purification with ammonium sulfate  of 1.008 U/mL and 48.956 U/mg; purification  DEAE Cellulose of 1.061 U/mL and 51.497 U/mg. Decolorization of textile dye waste was carried out at 50°C, for 144 hours, pH 5.5, and enzyme-substrate concentration of 1:1."

"Pemurnian parsial dan karakterisasi β-galaktosidase dari Lactobacillus plantarum strain D-210 belum dilaporkan. L. plantarum strain D-210 ditemukan sebagai bakteri penghasil β-galaktosidase sebagian dimurnikan dengan dialisis. Hasil penelitian menunjukkan bahwa aktivitas optimum dalam 24 jam dengan dan total protein adalah 0,454 mg/ml pada pH 6.5 aktivitas enzim 252,341 U/ml, dan suhu 45°C dengan aktivitas 0,582 U/ ml. Total aktivitas β-galaktosidase L.plantarum strain D-210 adalah 138,396 U dan endapan dengan amonium sulfat dicapai pada 40% - 50% dengan aktivitas total 87,030 U. Setelah dialisis, aktivitas total adalah 50,420 U. Penghambat β - galaktosidase adalah Hg dan Cu dengan aktivitas relatif adalah 56,82% dan1,04%, sedangkan aktivator adalah Mg, Mn, Ca, Co, Zn. Vmaks dari enzim adalah 0.093 µmol/menit dan KM enzim β-galaktosidase L. plantarum adalah 0,491 mM. Berdasarkan karakteristik β-galaktosidase, dapat disimpulkan bahwa L. plantarum strain D-210 adalah bakteri baik dan unggul yang dapat memproduksi β-galaktosidase. Studi lebih lanjut diperlukan untuk mengeksplorasi kemungkinan menggunakan bakteri ini dalam pengolahan susu pada bayi dengan intoleransi laktosa."

"ABSTRAKEnzim peroksidase merupakan enzim oksidor~duktase, yang dapat mengkatalis reaksi oksidasi oleh senyawa hidrogen peroksida (H202) dari sejumlah substrat yang merupakan donor hidrogen. Pada penelitian ini telah diisolasi enzim peroksidase dari tanaman sawi hijau (Brassica juncea) yang ada di pasaran. Pemurnian enzim dilakukan dengan teknik pengendapan bertingkat menggunakan garam amonium sulfat. Enzim peroksidase dengan aktivitas spesifik paling tinggi diperoleh pada fraksi amonium sulfat dengan tingkat kejenuhan 55-75 %, yaitu sebesar 1 ,24 kali dibandingkan ekstrak enzim kasarnya. Kondisi optimum reaksi katalisis enzim peroksidase dengan menggunakan substrat guaiakol diperoleh pada suhu 30 oc dan pH 6,0. Pada uji kestabilan, enzim peroksidase yang disimpan pada suhu 4°C selama satu bulan mengalami penurunan yang relatif kecil, yaitu sebesar 2, 79 %. Apabila enzim disimpan pada suhu 30 °C, terjadi penurunan sebesar 10,35-70,42% pada tujuh hari pertama, dan setelah satu bulan penurunannya mencapai 81,73 %. Uji homogenitas enzim peroksidase hasil dialisis dengan SD?PAGE menghasilkan pita protein di sekitar 37-50 kDa."

"Oxydoreductases are enzymes which catalyze oxidation-reduction reaction of their corresponding substrates. Oxydoreductase enzymes from many microorganisms had become major focus of research during last decades. This reaction had been utilized in biosensor (Yuhashi et al. 2005), biotransformation and biofuel (Zu et al. 2006). In the field of biosensor, glucose dehydrogenase application as self-blood glucose monitoring had evolved through several generation to enhance its sensitivity and specificity (Witarto et al. 1997). Oxydoreductase involve cofactor in their active sites. According to Anthony (1996) among several known cofactors such nicotinamide, flavonoid, and quinone, Pyrollo Quinoline Qinone (PQQ) as the member group of quinon is one of the latest known-cofactors. PQQ differs from other cofactor since it is not covalently bond to its enzyme (Oubrie et al. 1999). PQQ ubiquitously found in all organisms from prokaryote to eukaryote (Bishop et al. 1998). Bacteria is the largest group of PQQ-oxydoreductase producing microorganisms. They successfully isolated from many habitats such: soil, water (Toyama et al. 1995), fruits (Adachi et al. 2003), plants, and in human mouth (Anesti et al. 2005). However, study on PQQ-oxydoreductase producing bacteria isolation had never been reported in Indonesia. PQQ-Oxydoreductase bacteria are able to utilize organic substrates such glucose, ethanol, methanol, up to polyvinyl alcohol (Ameyama et al. 1985). One of the habitats which provides such organic substrates is Situ Agathis located in University of Indonesia Depok. Situ Agathis contain humic substances that could be degraded in to glucose, ethanol, methanol, also quinone. In this study, isolation of oxydoreductase-producing bacteria from Situ Agathis University of Indonesia, Depok and characterization of oxydroreductases of selected isolates were performed. The objectives of this research are: to investigate the presence of oxydoreductase-producing bacteria, to isolate the oxydoreductases -producing bacteria, and to partially characterize oxydoreductases from Situ Agathis University of Indonesia Depok. This is the first study on bacteria isolation performed in Situ Agathis UI, Depok. Hence, this study can provide information about the oxydoreductases- producing bacteria from Situ Agathis, which located in UI, Depok. The study consists of two part: first part describe the isolation of oxydoreductase-producing bacteria from Situ Agathis. Second part describe the partial characterization of oxydoreductases which covers enzyme activity, molecular weight, and PQQ effects on the enzymes activity. The research was carried out at the Protein Engineering Laboratory, Biotechnology Research Centre, Indonesian Institute of Science, Cibinong and the Laboratory of Microbiology, Department of Biology, University of Indonesia, Depok during February ? September 2007. The isolation of bacteria was conducted in three methods i.e : dilution, filtration using filter paper Milipore membran (0.2 μm) based on Cappucino and Sherman (2002). Isolation of oxydoreductase-producing bacteria was carried out by using selective media based on Toyama et al. (1995). The assay of oxydoreductases was performed by using Native-PAGE based on Khodijah (2002). The result showed that 83 isolates were obtained from Situ Agathis which we assumed could produce oxydoreductase enzymes. Among those isolates, 15 isolates were randomly selected for further study e.g : five isolates which could grow in glucose as sole carbon sources by producing glucose dehdyrogenase, six isolates which could grow on ethanol as sole carbon sources by producing ethanol dehydrogenase and four isolates which could grow on methanol as sole carbon sources by producing methanol dehydrogenase. The selected isolates showed various morphotypes indicating no specific morphological character in oxydoreductase-producing bacteria. Two oxydoreductases from selected isolates were selected to be analyzed further in second part this thesis. Those enzymes were examined for their possibility to have intracellular PQQ cofactor. Those enzymes were obtained from isolate G1H1D30 (glucose dehydrogenase) and isolate A1H2D60 (ethanol dehydrogenase). Native-PAGE result confirmed that crude extract fraction, dialyzed fraction and elution of open column chromatography of isolate G1H1D30 can produce glucose dehydrogenase and isolate A1H2D60 can produce ethanol dehdyrogenase. The molecular weight of glucose dehydrogenase subunit is about 46 kDa using SDS-PAGE. SDS-PAGE of ethanol dehydrogenase did not show any protein band in acrylamide gel. We assumed that the amount of protein extracted from cell cytoplasm was not sufficient enough to be detected in SDS-PAGE. Cell of isolate A1H2D60 should be treated by other destruction method such as French pressure or ultrasonicator since this isolate is Gram positive bacteria which had thicker peptydoglycan layer than isolate G1H1D30 which is Gram negative bacteria. Other characterization performed was addition of PQQ as the cofactor to investigate its effect on enzymes activity. Glucose dehydrogenase from isolate G1H1D30 was known to be PQQ dependent enzymes from its activity increased after addition of PQQ. The addition of PQQ raised the indicating no specific morphological character in oxydoreductase-producing bacteria. Two oxydoreductases from selected isolates were selected to be analyzed further in second part this thesis. Those enzymes were examined for their possibility to have intracellular PQQ cofactor. Those enzymes were obtained from isolate G1H1D30 (glucose dehydrogenase) and isolate A1H2D60 (ethanol dehydrogenase). Native-PAGE result confirmed that crude extract fraction, dialyzed fraction and elution of open column chromatography of isolate G1H1D30 can produce glucose dehydrogenase and isolate A1H2D60 can produce ethanol dehdyrogenase. The molecular weight of glucose dehydrogenase subunit is about 46 kDa using SDS-PAGE. SDS-PAGE of ethanol dehydrogenase did not show any protein band in acrylamide gel. We assumed that the amount of protein extracted from cell cytoplasm was not sufficient enough to be detected in SDS-PAGE. Cell of isolate A1H2D60 should be treated by other destruction method such as French pressure or ultrasonicator since this isolate is Gram positive bacteria which had thicker peptydoglycan layer than isolate G1H1D30 which is Gram negative bacteria. Other characterization performed was addition of PQQ as the cofactor to investigate its effect on enzymes activity. Glucose dehydrogenase from isolate G1H1D30 was known to be PQQ dependent enzymes from its activity increased after addition of PQQ. The addition of PQQ raised theindicating no specific morphological character in oxydoreductase-producing bacteria. Two oxydoreductases from selected isolates were selected to be analyzed further in second part this thesis. Those enzymes were examined for their possibility to have intracellular PQQ cofactor. Those enzymes were obtained from isolate G1H1D30 (glucose dehydrogenase) and isolate A1H2D60 (ethanol dehydrogenase). Native-PAGE result confirmed that crude extract fraction, dialyzed fraction and elution of open column chromatography of isolate G1H1D30 can produce glucose dehydrogenase and isolate A1H2D60 can produce ethanol dehdyrogenase. The molecular weight of glucose dehydrogenase subunit is about 46 kDa using SDS-PAGE. SDS-PAGE of ethanol dehydrogenase did not show any protein band in acrylamide gel. We assumed that the amount of protein extracted from cell cytoplasm was not sufficient enough to be detected in SDS-PAGE. Cell of isolate A1H2D60 should be treated by other destruction method such as French pressure or ultrasonicator since this isolate is Gram positive bacteria which had thicker peptydoglycan layer than isolate G1H1D30 which is Gram negative bacteria. Other characterization performed was addition of PQQ as the cofactor to investigate its effect on enzymes activity. Glucose dehydrogenase from isolate G1H1D30 was known to be PQQ dependent enzymes from its activity increased after addition of PQQ. The addition of PQQ raised theenzyme activity to eight fold from 0.102 U/mL to 0.94 U/mL of crude enzyme extract. In contrast, addition of PQQ did not give significant effect to EDH enzyme activity (activity of crude enzyme remain 0.082 U/mL in the presence and absence of PQQ). However, further study should be performed to analyze the real cofactor of EDH from isolate A1H2D60. EDH differs from GDH since it had disulphide ring which stabilize PQQ bound to its enzyme. Hence, PQQ could remain bound to EDH as purification procedure performed. PQQ-GDH do not have any disulphide ring which could stabilize PQQ bound. This fact implicated unstable PQQ bound to GDH while isolation and purification performed."

"Metode biodelignifikasi dengan WRF (White Rot Fungi) saat ini menjadi pilihan yang menjanjikan dalam pengolahan limbah lignoselulosa menjadi bahan baku dalam industri obat maupun kertas. Karena pretreatment pada limbah lignoselulosa yang dilakukan melalui proses kimiawi dinilai tidak ramah terhadap lingkungan, maka diperlukan pretreatment biologis dengan organisme atau enzim yang lebih strabil pada lingkungan industri yang bervariasi. Penelitian ini bertujuan untuk mendapatkan jamur termofilik dengan aktivitas ligninolitik dan mampu menghasilkan enzim ligninolitik (MnP) pada kondisi tersebut. Jamur diisolasi dari kayu yang telah lapuk yang didapatkan dari Sumber Air Panas Guci, Kabupaten Tegal. Jamur ditumbuhkan pada media PDB dan Kirk dengan serbuk daun nanas sebagai substrat, lalu aktivitas enzim MnP dilakukan secara spektrofotometri UV/Vis dengan Mn2+ sebagai substrat pada panjang gelombang 270 nm. Larutan fraksi enzim MnP didapatkan dari fraksinasi enzim, dengan teknik filtrasi, presipitasi ammonium sulfat pada tingkat saturasi 80% dan dialisis dengan MW cut-off 8000-14000 Da. Kemudian Jamur diuji pada beberapa kondisi suhu inkubasi dan beberapa pH berbeda kemudian diukur aktivitas MnP dengan metode yang sama. Hasil didapatkan suhu optimum untuk inkubasi adalah 50°C dan pH optimum aktivitas MnP pada pH 6,0-7,0. Penentuan kinetika enzim dilakukan dengan plot Lineweaver-Burk persamaan Michaelis-Menten. Didapatkan hasil kinetika enzim dengan Km 0,473 mM dan Vmax 5,257 mM/min.

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The biodelignification method with WRF (White Rot Fungi) is currently a promising option in the treatment of lignocellulosic waste into raw materials in the drug and paper industries. Because the pretreatment of lignocellulosic waste through a chemical process is considered dangerous to the environment, accordingly biological pretreatment with more stable organisms or enzymes in various industrial environments is required.

This study aims to obtain thermophilic fungi with ligninolytic activity and capable of producing ligninolytic enzymes (MnP) under these conditions. The fungus was isolated from rotting wood obtained from Guci Hot Springs, Tegal Regency. The fungus were grown on PDB and Kirk media with pineapple leaf powder as a substrate, then the MnP enzyme activity was carried out by UV/Vis spectrophotometry with Mn2+ as a substrate at a wavelength of 270 nm. MnP enzyme fraction solution was obtained from enzyme fractionation, with filtration technique, ammonium sulfate precipitation at 80% saturation level and dialysis with MW cut-off of 8000-14000 Da. Then the fungus was tested at several incubation temperature conditions and several different pH values and then measured the MnP activity with the same method.

The results obtained that the optimum temperature for incubation was 50°C and the optimum pH for MnP activity was at pH 6.0-7.0. Determination of enzyme kinetics was carried out using the Lineweaver-Burk plot of the Michaelis-Menten equation. The results of the enzyme kinetics were 0.473 mM and Vmax 5.257 mM/min."

"Industri pulp dan kertas merupakan salah satu industri besar di Indonesia. Pada pembuatan pulp dan kertas, diperlukan suatu proses delignifikasi yang bertujuan untuk memisahkan struktur lignin yang masih tersisa dalam pulp. Umumnya, pada proses delignifikasi digunakan bahan kimia seperti klorin dioksida, yang pada akhirnya akan menghasilkan limbah kimia yang lebih berbahaya. Dalam rangka mengurangi limbah kimia, maka digunakan proses biodelignifikasi menggunakan mikroorganisme, yaitu jamur. Jamur pelapuk putih diketahui dapat memproduksi berbagai enzim. Penelitian ini memfokuskan pada enzim lignin peroksidase (LiP), yaitu salah satu enzim ligninolitik yang dihasilkan oleh jamur pelapuk putih dan dapat mendegradasi lignin dengan tujuan untuk melakukan optimasi media yang menghasilkan aktivitas enzim terbaik serta mengkarakterisasi LiP dari isolat jamur hasil penelitian sebelumnya. Optimasi dilakukan pada empat media, yaitu PDB (media 1); PDB+Serbuk bambu (media 2); PDB+Serbuk bambu+serbuk daun nanas (media 3), dan glukosa+serbuk bambu (media 4). Hasil penelitian menunjukan bahwa media yang paling baik adalah media 3 dengan nilai aktivitas enzim 6,605 μmol.mL−1. Kemudian LiP yang didapat dikarakterisasi dengan melakukan pengujian terhadap suhu, pH, dan profil kinetika enzim. Suhu optimum untuk LiP adalah pada suhu 30ºC dengan aktivitas 9,874 μmol.mL−1. Sedangkan untuk pH optimum diperoleh pada pH 5,0 dengan nilai aktivitas tertinggi sebesar 6,787 μmol.mL−1. Kemudian untuk kinetika enzim LiP pada rentang konsentrasi substrat veratril alkohol paling baik adalah 0,4 mM pada media 3 dengan nilai Vmaks sebesar 34,2465 μmol.mL−1.menit−1 serta Km sebesar 1,0958 μmol.mL−1. Berdasarkan hasil tersebut maka dapat disimpulkan bahwa jamur yang diteliti berpotensi mendegradasi lignin karena memiliki aktivitas enzim yang cukup baik.

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The pulp and paper industry is one of the major industries in Indonesia. In the manufacture of pulp and paper, a delignification process is needed which aims to separate the remaining lignin structure in the pulp. In general, chemicals such as chlorine dioxide are used in the delignification process, which in turn will produce more hazardous chemical waste. In order to reduce chemical waste, a biodelignification process is used using microorganisms, namely fungi. White rot fungi are known to produce various enzymes. This research focuses on the enzyme lignin peroxidase (LiP), which is a ligninolytic enzyme produced by white rot fungi that can degrade lignin. This study aims to optimize the media that produces the best enzyme activity and to characterize LiP from fungal isolates from previous studies. Optimization was carried out on four media, namely PDB (media 1); PDB+bamboo powder (media 2); PDB + bamboo powder + pineapple leaf powder (media 3), and glucose + bamboo powder (media 4). The results showed that the best medium was media 3 with an enzyme activity value of 6.605 μmol.mL−1. Then the LiP obtained was characterized by testing the temperature, pH, and enzyme kinetics profile. The optimum temperature for LiP is 30ºC with an activity of 9.874 μmol.mL−1. Meanwhile, the optimum pH was obtained at pH 5.0 with the highest activity value of 6.787 μmol.mL−1. Then for LiP enzyme kinetics in the range of substrate concentrations veratril alcohol the best was 0.4 mM in medium 3 with a Vmax value of 34.2465 μmol.mL−1.minute−1 and Km of 1.0958 μmol.mL−1. Based on these results, it can be concluded that the fungi studied have the potential to degrade lignin because they posses good enzyme activity."

"Enzim selulase merupakan enzim hidrolase yang mengkatalisis reaksi pemecahan selulosa menjadi unit glukosa. Enzim ini akan digunakan dalam pemanfaatan limbah pertanian (dedak padi) yang kaya akan selulosa untuk dijadikan senyawa lain seperti bioetanol. Pada penelitian ini telah dilakukan isolasi dan pemurnian enzim selulase dari mikroorganisme jamur Trichoderma viride (T051) melalui fermentasi padat menggunakan dedak padi sebagai substratnya. Pemurnian ekstrak kasar enzim dengan pengendapan bertingkat (fraksinasi) menggunakan garam ammonium sulfat, menghasilkan aktivitas spesifik selulase paling tinggi pada tingkat kejenuhan ammonium sulfat 20 -50% (11,4530 mU/mg) dengan tingkat kemurnian 5,3 kali dari ekstrak kasarnya. Pemurnian lebih lanjut dengan kromatografi kolom penukar anion (DEAE-Streamline) menghasilkan 6 puncak protein dengan aktivitas CMCase. Puncak protein ke-1 memiliki aktivitas spesifik paling tinggi (85,6703 mU/mg) dengan tingkat kemurnian 39,1 kali dari ekstrak kasarnya. Aktivitas selulolitik enzim ini ditentukan sebagai aktivitas CMCase (endoglukanase) menggunakan substrat CMC (carboxymethyl cellulose). Enzim selulase hasil pemurnian parsial memiliki aktivitas optimum pada pH 5,5 dan suhu inkubasi 50oC dan enzim ini diinhibisi oleh ion-ion Mg2+, Mn2+, dan Cu2+ (konsentrasi ion logam 100 mM) dengan persen inhibisi berturut-turut sebesar 16,4; 64,2; 60,2 %.

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Cellulase is a hydrolase enzyme that catalyzes the reaction of the breakdown of cellulose into glucose units. This enzyme will be used in the utilization of agricultural waste (rice bran) that is rich in cellulose to be used as other compounds such as bioethanol. In this study has been carried out isolation and purification of the cellulase from Trichoderma viride fungal microorganisms (T051) through solid fermentation using rice bran as a substrate. Purification of crude enzyme extract with multilevel deposition (fractionation) using ammonium sulfate salt, generating the highest specific activity of cellulase (11.4530 mU / mg) at 20 -50% level of saturation of ammonium sulfate, with a purity level of roughly 5.3 times of the extract. Further purification by anion-exchange chromatography column (DEAE-Streamline) produces 6 protein peaks with CMCase activity. Peak-1 protein to have the highest specific activity (85.6703 mU / mg) with a purity level of roughly 39.1 times of the extract. Cellulolytic enzyme activity was determined as CMCase activity (endoglucanase) using the substrate CMC (carboxymethyl cellulose). Partial purification of cellulase enzyme has optimum activity at pH 5.5 and incubation temperature 50oC, and this enzyme had inhibition by ions Mg2+, Mn2+, and Cu2+ with inhibition percent respectively at 16.4, 64.2, 60. 2%."

"Selulosa adalah polimer organik berlimpah, sumber pembentukan bioproduct di berbagai industri, yang dapat diperoleh melalui proses delignifikasi biomassa lignoselulosa menggunakan metode fisik, kimia, fisikokimia dan biologis. Biodelignifikasi adalah metode delignifikasi alternatif ramah lingkungan yang menggunakan enzim ligninolitik dalam prosesnya. Mangan peroksidase (MnP) adalah enzim ligninolitik yang dalam aplikasi biodelignifikasi belum banyak dipelajari dan didalami. Review ini bertujuan untuk mengetahui kondisi produksi yaitu: metode kultivasi, sumber dan rasio karbon dan nitrogen, suhu, pH dan induser ion logam dan metode purifikasi enzim terbaik untuk memperoleh MnP dengan aktivitas tinggi dan murni. Kajian berfokus pada penelitian selama 15 tahun terakhir namun diutamakan penelitian yang diterbitkan dalam 5 tahun terakhir. Gagasan yang diperoleh dari hasil analisis pustaka adalah kondisi optimal yang dapat diterapkan untuk produksi MnP yaitu: metode kultivasi menggunakan SSF dengan substrat biomassa lignoselulosa, sumber dan rasio C:N menggunakan glukosa dan ekstrak ragi-pepton rasio 20:1, suhu 30-40°C, pH 4.5 – 5.0, dan Mn2+ konsentrasi 500 µM – 20 mM sebagai induser. Metode purifikasi yang terbaik untuk memperoleh MnP yang murni adalah menggunakan kombinasi presipitasi-dialisis, kromatografi penukar ion dan kromatografi filtrasi gel.

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Cellulose is an abundant organic polymer, source of bio-product formation in various industries, which can be obtained by delignification of lignocellulosic biomass using physical, chemical, physicochemical and biological methods. Biodelignification is an environmentally friendly alternative in delignification that uses ligninolytic enzymes in its process. Manganese peroxidase (MnP) is a ligninolytic enzyme that in biodelignification application has yet been widely studied. This review aims to determine the optimal production conditions including the cultivation method, carbon and nitrogen sources and ratio, temperature, pH, and metal ion inducer, also the purification methods to obtain high activity and pure enzyme. The study focused on researches over the past 15 years but prioritized those in the last 5 years. The ideas drawn from the result of literature analysis is that the optimal conditions that can be applied in the production of MnP, are as follows: cultivation method using SSF with lignocellulosic biomass substrate, source and ratio of C: N of glucose and yeast extract-peptone with 20:1 ratio, temperature of 30-40 °C, pH 4.5 - 5.0, and 500 µM – 20 mM Mn2+ as the inducer. The best purification method to purify MnP is to use a combination of precipitation-dialysis, ion exchange chromatography and gel filtration chromatography."