Articles

PURIFICATION AND CHARATERIZATION OF PROTEASE FROM PATHOGENIC BACTERIA PSEUDOMONAS AERUGINOSA Baekhari, Ace; Suhartono, Maggy T; Palupi, Nurheni Sri; Nurhayati, Tati
Jurnal Teknologi dan Industri Pangan Vol. 19 No. 1 (2008): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

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Abstract

In the last decade, concern on protease as medical target for overcoming bacterial diseases and viral diseases has been rapidly increased because of the obvious involvement of this enzyme in the molecular of the diseases. The purpose of this research was to purify and characterize protease from pathogenic bacteria Pseudomonas aeruginosa. The bacteria were grown in media containing triptone 1%, NaCl 1% and Yeast extract 0.5%. protease of Pseudomonas aeruginosa was purified using column chromatography with Sephadex G-100 gel. There were three peaks of enzyme protein, which were detected on fractions 14,17 and 30. the optimum pH of the extracelluler protease from Pseudomonas aeruginosa was 8. The optimum temperature of Pseudomonas aeruginosa was 300C. Fe3+ (1dan 5 mM) was strong activator and Co 2+ was strong inhibitor. Study on the effect of metals ion and specific inhibitors indicated that protease from Pseudomonas aeruginosa was serin metaloprotease. The apparent moleculer weights, as determined by SDS-PAGE and zymogram technique, 36 kD and 42 kD. Key word : Protease, characterization, purification, pathogenic bacteria P. aeruginosa
THE HISTOLOGICAL, EXTRACTION AND CHARACTERIZATION COLLAGENS YELLOW-PIKE CONGER MUARENESOX TALABON Gadi, Dewi Setiyowati; Trilaksani, Wini; Nurhayati, Tati
Jurnal Ilmu dan Teknologi Kelautan Tropis Vol. 9 No. 2 (2017): Elektronik Jurnal Ilmu dan Teknologi Kelautan Tropis
Publisher : Department of Marine Science and Technology, Faculty of Fisheries and Marine Science, IPB University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29244/jitkt.v9i2.19300

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By product Muarenesox talabon swim bladders can be used as a raw material for desperately needed in the food, biomedical, pharmaceutical, and cosmeceuticals industries. The aims of the research were to observed the histological and determine chemical characteristics of swim bladder including proximate and amino acids; extraction of acid soluble collagen and determine the characteristics of collagen including proximate, pH, heavy metals, microbial, amino acids, functional groups, molecular weights, and thermal stability. The morphology of cunang swim bladder consists of outer, middle, and inner layers containing collagen fibers; 33.67±0.71%wb and protein whichwere dominated by three amino acids that were glycine, proline, and alanine. Pretreatment by 0.1 M NaOH for 8 hours (K1T4) and acid extraction by 0.25 M acetic acid for 72 hours (M1T3) was the best treatment yielding 14.51± 0.43% of collagen; having 12.12±0.04% wb of moisture; 88.54 ± 0.08% wb of protein; 1.31±0.23% wb of fat; 0.17±0.03% wb of ash. Not detected any heavy metals (Pb, Hg, As, Cd). Acidity pH was 4.31 and negative of E. coli and Salmonella. The main amino acids detected were glycine 241.06 mg/g; proline 88.73mg/g; and alanine 86,98 mg/g; FTIR spectra were revealed the presence of triple helix structures; electrophoresis patterns consisted of 136 kDa of mol weight of ?1 and 117 kDa of mol weight of ?2 were characterisedto be type I collagen; which had Tmax of 195.59ºC and ?H 7.8113 J/g. Keywords: acid extraction, swim bladder, collagens, thermal stability
AKTIVITAS ANTIBAKTERI PROTEIN KAPANG XYLARIA PSIDII KT30 TERHADAP ESCHERICHIA COLI DAN BACILLUS SUBTILIS [ANTIBACTERIAL ACTIVITY OF PROTEIN FUNGUS XYLARIA PSIDII KT30 ESCHERICHIA COLI AND BACILLUS SUBTILIS] Munandar, Aris; Mustopa, A. Zaenal; Tarman, Kustiariyah; Nurhayati, Tati
Jurnal Teknologi dan Industri Pangan Vol. 25 No. 2 (2014): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (397.636 KB) | DOI: 10.6066/jtip.2014.25.2.146

Abstract

Previous research shows that extracellular protein of an algicolous fungus Xylaria psidii KT30 inhibited Bacillus pumilus, Listeria sp., Salmonella typhi, Staphylacoccus aureus, and Pseudomonas sp. with an average clear zone diameter of 7 mm. To enhance the potent antibacterial activity of extracellular protein from Xylaria psidii KT30, the present research demonstrated fungal growth optimization and purification of its secreted extracellular protein. The fungal growth optimization was performed following NaCl concentration and harvest day variations. The protein was precipitated using ammonium sulphate at 60%-90% saturation range and was purified through gel chromatography filtrationusing Sephadex G-50, eluted with 30% aq methanol. The active fraction possesing antibacterial activity was then determined resulting supernatant, pellet, and protein fraction.The fungal was optimally obtained after 15 days cultivation using freshwater.The highest protein yield was 1.67%, resulted over 90% saturation. Fractions 11 and 12 were the most active against Escherichia coli dan Bacillus subtiliswith clear zone diameter of 8 mm.Three bands of those fractions were detected through SDS-PAGE analysis, revealing molecular weights of 23.42, 20.09, and 14.33 kDa.  
EKSTRAKSI DAN KARAKTERISASI PARSIAL EKSTRAK KASAR ENZIM KATEPSIN DARI IKAN PATIN [EXTRACTION AND PARTIAL CHARACTERIZATION OF CRUDE ENZYMES CATHEPSIN FROM CATFISH] Fikri, Muhammad Zakiyul; Nurhayati, Tati; Salamah, Ella
Jurnal Teknologi dan Industri Pangan Vol. 25 No. 1 (2014): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (491.049 KB) | DOI: 10.6066/jtip.2014.25.1.119

Abstract

EKSTRAKSI DAN KARAKTERISASI PARSIAL EKSTRAK KASAR ENZIM KATEPSIN DARI IKAN PATIN [Extraction and Partial Characterization of Crude Enzymes Cathepsin from Catfish] Muhammad Zakiyul Fikri*, Tati Nurhayati dan Ella SalamahDepartemen Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu Kelautan, Institut Pertanian Bogor, Bogor Diterima 02 Juli 2013 / Disetujui 30 Mei 2014ABSTRACT Decomposition of protein by enzymatic process will lead to changes in odor, texture, and appearance of fish. The enzymes that play a role in the enzymatic process is primarily proteolytic enzymes. Cathepsin is one of the proteolytic enzymes found in animal tissue that hydrolyzes peptide bonds of proteins. This study aims to extract the cathepsin, characterize the crude extract derived from catfish. The stages of this research consist of the extraction and characterization of the cathepsin from catfish. Result of the extraction was crude extract of cathepsin with activity of 0.278 U/mL. The enzyme had optimum temperature of 50°C, pH 6 and substrate concentration of 2%. The activity of the cathepsin was inhibited by metal ions of Fe3+, Cu2+, Ca2+, but increased by metal ions of Mg2+.  
INFLUENCE OF GLUCOSE AND YEAST EXTRACT TOWARD PRODUCTION OF PSEUDOMONAS AERUGINOSA-PROTEASE INHIBITOR FROM CHROMOHALOBACTER SP. 6A3 (BACTERIA ASSOCIATED WITH SPONGE XETOSPONGIA TESTUDINARIA) Nurhayati, Tati; Thenawidjaja, Maggy; Nuraida, Lilis; Poerwanto, Sri Budiarti
Journal of Agroindustrial Technology Vol. 19 No. 2 (2009): Jurnal Teknologi Industri Pertanian
Publisher : Department of Agroindustrial Technology, Bogor Agricultural University

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Abstract

One way to inhibit protease activity is search is compound which can inhibit the enzyme known as protease inhibitor. The bacteria associated with sponge Xetospongia testudinaria, Chromohalobacter sp. 6A3, as producer Pseudomonas aeruginosa-protease inhibitor. Because the compound is important, determination medium composition for producing is very important to be conducted.  The purpose of this research was to determinate the glucose and yeast extract consentration accurately so protease inhibitor would be produced in a short time.  The accurate medium composition for producing the protease inhibitor were 0.1%(w/v) yeast extract; 0.05% (w/v) glucose;  0.5%(w/v) special peptone; 0.2%(v/v) trace element; and 2%(w/v) NaCl at pH 7.Keywords: Chromohalobacter sp., protease inhibitor, sponges.
PURIFIKASI KOLAGENASE DARI USUS BANDENG (CHANNOS CHANNOS, FORSKAL) Yuniarti, Tatty; Nurhayati, Tati; Jacoeb, Agoes Mardiono
Biota : Jurnal Ilmiah Ilmu-Ilmu Hayati Vol 15, No 3 (2010): October 2010
Publisher : Universitas Atma Jaya Yogyakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24002/biota.v15i3.2593

Abstract

Collagenase was purified from intestines of milkfish (Chanos chanos, Forskal) by extraction,ammonium precipitation, ion exchange chromatography on DEAE Sephadex A-50 and gelfiltration on a Sephadex G-100 column. The purification and yields were 114.731 fold and1.26% when compared to those in the starting-crude extract. The molecular mass of milkfishserine collagenase was estimated to be 14.63 kDa and 27.46 kDa.
PEMANFAATAN DNA BARCODING UNTUK KETERTELUSURAN LABEL BERBAGAI PRODUK OLAHAN IKAN BERBASIS SURIMI KOMERSIAL Abdullah, Asadatun; Sativa, Hana Aulia; Nurhayati, Tati; Nurilmala, Mala
Jurnal Pengolahan Hasil Perikanan Indonesia Vol. 22 No. 3 (2019): Jurnal Pengolahan Hasil Perikanan Indonesia
Publisher : Masyarakat Pengolahan Hasil Perikanan Indonesia (MPHPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (313.683 KB) | DOI: 10.17844/jphpi.v22i3.28950

Abstract

Surimi-based processed products are prone to mislabeling using raw materials that are not in accordance with food safety requirements. There were cases reporting use of toxic fish tissue in commercial seafood products. This study was aimed to identify and determine the raw materials used in various processed surimi products using cytochrome oxidase I (COI) gene marker. The experiment consisted of DNA isolation, DNA amplification using several target primers namely full-length barcodes, mini-barcodes, as well as specific species primers against poisonous puffer fish Lagocephalus lunaris and genetic analysis. The results of bioinformatics analysis revealed that S1 samples were Coryphaena hippurus or mahi-mahi fish, S2 and S3 samples were Nemipterus bathybius or curated fish and CS samples were Evynnis cardinalis or kuro fish. Detection of samples with species specific primers of puffer fish Lagocephalus lunaris with annealing temperatures of 54°C, 57°C, and 60°C showed no DNA bands in the six samples analyzed.
ENHANCEMENT OF TEXTURAL QUALITY FROM DAGGERTOOTH PIKE CONGER FISH SURIMI WITH SODIUM TRIPOLYPHOSPHATE AND TRANSGLUTAMINASE ACTIVATOR Laksono, Untung Trimo; Suprihatin, Suprihatin; Nurhayati, Tati; Romli, Muhammad
Jurnal Pengolahan Hasil Perikanan Indonesia Vol. 22 No. 2 (2019): Jurnal Pengolahan Hasil Perikanan Indonesia
Publisher : Masyarakat Pengolahan Hasil Perikanan Indonesia (MPHPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (581.379 KB) | DOI: 10.17844/jphpi.v22i2.27373

Abstract

Dagger-tooth pike conger fish (Muraenesox cinerus) is known to have high edible portions and white meat, thus can be used as a surimi raw materials. However, the textural quality of this fish meat is relatively poor after washing process of surimi. This reserch was aimed to analyze the effects of TGase activator and STPP addition to increase the textural quality of surimi malong. The method used is a factorial experiment with the addition of activator TGase 0.2; 0.4 and 0.6 and STPP at concentrations 0; 0.2; 0.5 and 0.8. Parameters observed were texture profile analysis (TPA), water holding capacity (WHC) folding test, bite test, and scanning electron microscopy (SEM). The results showed that the addition of STPP and activator TGase (Ca) has significant effect on increasing the hardness, fracturability, chewiness, gumminess, bite test and the folding test. Furthermore, microscopies structure (SEM) of malong surimi showed smooth and solid surfaces.
AKTIVITAS INHIBITOR PROTEASE DARI EKSTRAK KARANG LUNAK, ASAL PERAIRAN PULAU PANGGANG KEPULAUAN SERIBU Nurhayati, Tati; Fikri, Muhammad; Desniar, Desniar
ILMU KELAUTAN: Indonesian Journal of Marine Sciences Vol 15, No 2 (2010): Ilmu Kelautan
Publisher : Marine Science Department Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1308.369 KB) | DOI: 10.14710/ik.ijms.15.2.59-65

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Beberapa komponen bioaktif dihasilkan oleh karang lunak, salah satunya inhibitor protease. Tujuan penelitian ini adalah mendapatkan karang lunak yang berpotensi sebagai penghambat aktivitas kerja enzim protease (inhibitor protease) pada beberapa bakteri patogen penghasil enzim protease serta mengetahui Minimum Inhibitory Concentration (MIC) dari ekstrak karang lunak tersebut.  Hasil penelitian menunjukkan bahwa pelarut metanol  lebih  potensial  untuk  mengekstrak  inhibitor  protease  dari  karang  lunak.  Karang  lunak  jenis Sarcophyton sp. dan Sinularia sp. mampu menghambat 100% aktivitas protease bakteri Staphylococus aureus dengan MIC 0,04% lebih kecil dari pada MIC EDTA (0,16%), sedangkan Xenia sp. menghambat protease bakteri S. aureus dengan MIC 0,08%. Karang lunak Nephthea sp. menghambat protease bakteri Pseudomonas aeruginosa dengan MIC 0,28%. Kata kunci : inhibitor protease, karang lunak, MIC Several bioactive compounds were produced by soft corals, including protease inhibitor.The aim of this study was to obtain softcorals which potency as inhibitor toward protease enzyme activity on pathogenic bacterial that produced protease enzyme and to study Minimum Inhibitory Concentration (MIC) from the softcorals. This research shown that ethanol is more potential for extracting protease inhibitor from softcorals. Sarcophyton sp. and Sinularia sp. are capable of inhibiting protease enzyme activity against Staphylococus aureus as 100% by MIC 0.04%, while that EDTA had MIC toward the protease as 0.16%.  Xenia sp. was capable of inhibiting protease from S. aureus by MIC 0.08%.  In the otherhand Nephtea sp. inhibited protease from Pseudomonas aeruginosa by MIC 0.28%. Key words: protease inhibitor, soft coral, MIC.
RECOVERY ENZIM KATEPSIN DARI LIMBAH CAIR SURIMI Nurhayati, Tati; Novanti, Hani; Jacoeb, Agoes M
Asian Journal of Innovation and Entrepreneurship Vol 4, No 01 (2015): January 2015
Publisher : UII

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20885/ajie.vol4.iss1.art4

Abstract

Surimi processing waste liquid that still contains high sarcoplasmic proteins that can still be used, one of which is an cathepsin enzyme. The purpose of the study was to determine the parameters of pH and temperature in recovery of  enzyme cathepsin from surimi wastewater. The results showed that the best recovery of cathepsin enzyme  is obtained at pre-treated  pH 5 and heating at a temperature of 60 °C. In these conditions, cathepsin enzyme has a specific activity 17.90 U / mg and a multiple of 117 times the purity of surimi wash water. Keywords: cathepsin, enzyme recovery, pH, surimi wastewater, temperature
Co-Authors . Desniar . Uju A. Zaenal Mustopa Ace Baehaki Ace Baekhari Agoes M Jacoeb, Agoes M Agoes Mardiono Jacoeb Alfi Hamdan Zamzami AMALIA, ELIN Andriyani, Pitria Aprilia, Bintang Efrata Aris Munandar Ary Apriland Asadatun Abdullah Aulia Andhikawati Azizah Nuraini Bagus Sediadi Bandol Utomo, Bagus Sediadi Bandol Barokah, Giri Rohmad Bunga, Selvanda Moreine Bustami Ibrahim Dedi Soedarma Desniar Desniar Djailani, Fernandy Eko Muhammad Isa Ekowati Chasanah Ella Salamah Febrina Olivia Akerina, Febrina Olivia Fitriany Podunge, Fitriany Fransiskayana, Andika Gadi, Dewi Setiyowati Hani Novanti, Hani Hefni Effendi Ifah Munifah Ika Astiana Indah Rahayu Widadi Iriani Setyaningsih Irman Febrian Jacoeb, Agoes Jacoeb, Agoes Komariah Tampubolon Kustiariyah Tarman LAKSMI AMBARSARI Laksono, Untung Trimo LILIS NURAIDA Made Suhandana Maggy T Suhartono Maggy T. Suhartono Maggy Thenawidjaja MAGGY THENAWIDJAJA SUHARTONO Maglory Siburian Mala Nurilmala Manteu, Shindy Hamidah masdudi masdudi, masdudi Merdekawati, Dewi Merdekawati, Dewi Mohammad Irfan Mohammad Zaenuri, Mohammad Muhammad Fikri Muhammad Romli Muhammad Zakiyul Fikri MUJIZAT KAWAROE nico Dynnar Ninik Purbosari Nugroho, Teguh Setyo Nur?aenah, Nani Nurfajrin Nisa, Nurfajrin Nurheni Sri Palupi Nurhikma, Nurhikma Nurjanah . Nurjanah Nurjanah Nurlisa Butet, Nurlisa Pasaribu, Ewi Pipih Suptijah Pratitis, Asri Putalan, Reinal Rahmawati, Mutiara Rina Rina Rini Suwardinni Roni Nugraha Roskananda, Rieska Ruddy Suwandi Rukmana, Evi Oktaviani S Nurul Janah, S Nurul Saeful Bahri safrina dyah hardiningtyas Santhy Wisuda Sidauruk Saputra, Dede Saputra, Dede Sari, Sharah Novita Sativa, Hana Aulia Sri Budiarti Poerwanto Sri Purwaningsih Sugeng Heri Suseno Suprihatin Suprihatin Syefri Rusyadi, Syefri Taufik Hidayat Trilaksani, Win Uju Uju Uzainah Aremhas Wini Trilaksani Yenni Yenni Yulia Oktavia Yuniarti, Tatty Yuniarti, Tatty Yusro Nuri Fawzya ZAKARIA, RIJAN