Ace Baehaki
Jurusan Teknologi Hasil Perikanan Fakultas Pertanian Universitas Sriwijaya, Indralaya, Ogan Ilir 30662 Sumatera Selatan Telp./Fax. (0711) 580934

Published : 33 Documents
Articles

Found 33 Documents
Search

KARAKTERISASI PROTEASE DARI ISOLAT BAKTERI ASAL TUMBUHAN RAWA DARI INDRALAYA Baehaki, Ace; ., Rinto
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 15, No 1 (2012): Jurnal Pengolahan Hasil Perikanan Indonesia
Publisher : Departement of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (938.914 KB)

Abstract

Proteases constitute one of the most important groups of industrial enzymes, therefore screening of these proteases from bacteria is important. The aim of this study was to characterize proteases from plant swamp bacteria. The result of  proteolytic assays revealed three isolates possesed proteolytic index >1.00 (T1P4, H1P4 and K1P4). The optimum fermentation time of each isolate was 48 hours. The optimum pH of proteases from T1P4, H1P4 and K1P4 was 8.0; 7.5; and 8.0,  respectively. The optimum temperature of T1P4, H1P4 and K1P4 protease was 50 °C; 40 °C;  and 50 °C, respectively. Metal ions (Fe, K, Mn, and Zn) inhibited T1P4 protease except Fe2+ (5 mM), H1P4 protease except  Zn2+ (5 mM),  K1P4 protease except Fe (1 and 5 mM). Effect of inhibtor specific (EDTA) shown EDTA inhibit all  proteases. Study on the effect of metals ion and spesific inhibitors indicated that all protease were  metaloprotease. The moleculer weights of T1P4, H1P4 and K1P4 proteases were determinited by using SDS-PAGE and zymography technique were 151; 138; and 127 kD, respectively.Key words:  bacteria, characterization, protease, swamp
Karakterisasi Protease dari Bakteri Aeromonas hydrophila Baehaki, Ace; Nurhayati, Tati; Suhartono, Maggy T.
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 7, No 2 (2004): Buletin Teknologi Hasil Perikanan
Publisher : Departement of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (266.87 KB)

Abstract

In the last decade, a concern on protease as medicinal target for overcoming bacterial and viral diseases has been rapidly increased because of the obvios involvement of this enzyme in the molecular of the diseases mechanism. The porpuse of this research was to characterize proteases from fish pathogenic bacteria Aeromonas hydrophila. The bacteria were grown in media containing triptone 1%, NaCl 1% and yeast extract 0,5%. The optimum production time of A. hydrophila was 48 h, the optimum pH was 7,5, the optimum temperature was 50oC. Study on the effect of metals ion and spesific inhibitors indicated that protease from A. hydrophila was serin metaloprotease.Keywords: protease, characterization, pathogenic bacteria
Karakteristik Protease dari Bakteri Patogen Staphylococcus epidermidis Baehaki, Ace; Nurhayati, Tati; Suhartono, Maggy T.
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 8, No 2 (2005): Buletin Teknologi Hasil Perikanan
Publisher : Departement of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (129.232 KB)

Abstract

Beberapa bakteri patogen memproduksi enzim hidrolitik seperti protease dan hialuronidase yang berfungsi untuk mendegradasi komponen matrik ekstraseluler sehingga dapat merusak struktur jaringan inang. Tujuan penelitian ini adalah untuk melakukan karakterisasi protease dari bakteri Staphylococcus epidermidis yang diisolasi dari koleksi Rumah Sakit Pertamina Jakarta. Bakteri ditumbuhkan pada media Luria broth (LB) yang mengandung tryptone 1 %, NaCl 1 % dan yeast extract 0,5 %. Hasil karakterisasi menunjukkan bahwa protease S. epidermidis ini memiliki pH dan suhu optimum 8 dan 50 oC. Ion logam Mn2+ (5 mM) dan Ba2+ (5 mM) merupakan aktivator kuat protease S. epidermidis yang dapat meningkatkan aktivitas protease masing-masing 3 dan 2 kali lipat dari protease kontrol, sedangkan Na+ (1 mM), K+ (1 mM), Fe3+ (1 dan 5 mM), Zn2+ (5 mM), dan Ca2+ (1 mM) merupakan inhibitor ion logam yang kuat. Protease S. epidermidis digolongkan ke dalam serin metaloprotease karena dapat dihambat secara sempurna oleh PMSF dan EDTA. Protease tersebut mempunyai berat molekul sekitar 35 kD.Kata Kunci: bakteri patogen, karakterisasi, protease, Staphylococcus epidermidis.
Karakteristik Protease dari Bakteri Patogen Staphylococcus epidermidis Baehaki, Ace; Nurhayati, Tati; Suhartono, Maggy T.
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 8, No 2 (2005): Buletin Teknologi Hasil Perikanan
Publisher : Department of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (129.232 KB) | DOI: 10.17844/jphpi.v8i2.1013

Abstract

Beberapa bakteri patogen memproduksi enzim hidrolitik seperti protease dan hialuronidase yang berfungsi untuk mendegradasi komponen matrik ekstraseluler sehingga dapat merusak struktur jaringan inang. Tujuan penelitian ini adalah untuk melakukan karakterisasi protease dari bakteri Staphylococcus epidermidis yang diisolasi dari koleksi Rumah Sakit Pertamina Jakarta. Bakteri ditumbuhkan pada media Luria broth (LB) yang mengandung tryptone 1 %, NaCl 1 % dan yeast extract 0,5 %. Hasil karakterisasi menunjukkan bahwa protease S. epidermidis ini memiliki pH dan suhu optimum 8 dan 50 oC. Ion logam Mn2+ (5 mM) dan Ba2+ (5 mM) merupakan aktivator kuat protease S. epidermidis yang dapat meningkatkan aktivitas protease masing-masing 3 dan 2 kali lipat dari protease kontrol, sedangkan Na+ (1 mM), K+ (1 mM), Fe3+ (1 dan 5 mM), Zn2+ (5 mM), dan Ca2+ (1 mM) merupakan inhibitor ion logam yang kuat. Protease S. epidermidis digolongkan ke dalam serin metaloprotease karena dapat dihambat secara sempurna oleh PMSF dan EDTA. Protease tersebut mempunyai berat molekul sekitar 35 kD.Kata Kunci: bakteri patogen, karakterisasi, protease, Staphylococcus epidermidis.
Karakterisasi Protease dari Bakteri Aeromonas hydrophila Baehaki, Ace; Nurhayati, Tati; Suhartono, Maggy T.
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 7, No 2 (2004): Buletin Teknologi Hasil Perikanan
Publisher : Department of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (266.87 KB) | DOI: 10.17844/jphpi.v7i2.1045

Abstract

In the last decade, a concern on protease as medicinal target for overcoming bacterial and viral diseases has been rapidly increased because of the obvios involvement of this enzyme in the molecular of the diseases mechanism. The porpuse of this research was to characterize proteases from fish pathogenic bacteria Aeromonas hydrophila. The bacteria were grown in media containing triptone 1%, NaCl 1% and yeast extract 0,5%. The optimum production time of A. hydrophila was 48 h, the optimum pH was 7,5, the optimum temperature was 50oC. Study on the effect of metals ion and spesific inhibitors indicated that protease from A. hydrophila was serin metaloprotease.Keywords: protease, characterization, pathogenic bacteria
KARAKTERISASI PROTEASE DARI ISOLAT BAKTERI ASAL TUMBUHAN RAWA DARI INDRALAYA Baehaki, Ace; ., Rinto
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 15, No 1 (2012): Jurnal Pengolahan Hasil Perikanan Indonesia
Publisher : Department of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (938.914 KB) | DOI: 10.17844/jphpi.v15i1.5335

Abstract

Proteases constitute one of the most important groups of industrial enzymes, therefore screening of these proteases from bacteria is important. The aim of this study was to characterize proteases from plant swamp bacteria. The result of  proteolytic assays revealed three isolates possesed proteolytic index >1.00 (T1P4, H1P4 and K1P4). The optimum fermentation time of each isolate was 48 hours. The optimum pH of proteases from T1P4, H1P4 and K1P4 was 8.0; 7.5; and 8.0,  respectively. The optimum temperature of T1P4, H1P4 and K1P4 protease was 50 °C; 40 °C;  and 50 °C, respectively. Metal ions (Fe, K, Mn, and Zn) inhibited T1P4 protease except Fe2+ (5 mM), H1P4 protease except  Zn2+ (5 mM),  K1P4 protease except Fe (1 and 5 mM). Effect of inhibtor specific (EDTA) shown EDTA inhibit all  proteases. Study on the effect of metals ion and spesific inhibitors indicated that all protease were  metaloprotease. The moleculer weights of T1P4, H1P4 and K1P4 proteases were determinited by using SDS-PAGE and zymography technique were 151; 138; and 127 kD, respectively.Key words:  bacteria, characterization, protease, swamp
Protein Hydrolysis from Catfish Prepared by Papain Enzyme and Antioxidant Activity of Hydrolyzate Baehaki, Ace; Lestari, Shanti Dwita; Romadhoni, Achmad Rizky
Jurnal Pengolahan Hasil Perikanan Indonesia Vol 18, No 3 (2015): Jurnal Pengolahan Hasil Perikanan Indonesia
Publisher : Departement of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (39.104 KB)

Abstract

The objective of this research was to make a protein hydrolysates from catfish(Pangasius pangasius) enzymatically using papain enzyme and analyzed the antioxidant activityof protein hydrolysates produced. The research used the method completely randomized designwith two replications the treatment were the difference concentration of the papain enzyme(0%, 1%, 2%, 3%, 4%, 5%, and 6%). The parameters of research were antioxidative activity usingDPPH (2,2-difenil-1–pikrilhidrazil), protein content, and molecular weight using SDS-PAGE(Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). The results showed that catfishprotein hydrolysates prepared by papain enzyme has antioxidative activity. The highest degree ofhydrolysis was 71.98% at enzyme concentration of 6%. Based on the DPPH scavenging methodcatfish protein hydrolysates has the antioxidative activity with the value 37.85-67.62%. The proteincontent of catfish protein hydrolysates were 20.86-54.47 mg/ml. The molecular weight of catfishprotein hydrolyzates were 11.90-65.20 kDa.Keywords: Antioxidant, catfish, papain enzyme, protein hydrolyzate
AKTIVITAS ANTIOKSIDAN KOMPLEKS KITOSAN MONOSAKARIDA (Chitosan Monossacharides Complex) Sari, Selly Ratna; Baehaki, Ace; Lestari, Shanti Dwita
Jurnal FishtecH Vol 2, No 1 (2013)
Publisher : Jurnal FishtecH

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (185.825 KB)

Abstract

The purpose of this research was to observe antioxidative activity of chitosan monosaccharides complex. The research was conducted in May until June 2013 at chemistry and microbiology laboratory, study program of agricultural technology. All treatment are chitosan, chitosan glucose complex, chitosan galactose complex and chitosan fructose complex using a invitro testing. The parameters were brown color analysis, analysis antioxidant activity with DPPH and reducing power method . The result showed that all chitosan monosaccharides complex demonstrated better antioxidative than chitosan. It is indicated that Maillard reaction product (MRP) exhibited antioxidant activity. The brown color analysis (0.031-0.224), antioxidant antioxidant analysis with DPPH method of IC50 (92-131 ppm) and reducing power method was 1.059-1.274. Chitosan galactose complex (A2) is the best to antioxidative from all treatments. Chitosan monosaccharides complex could be used as natural preservatives, edible packaging (film and couting) and food additive.
Pengaruh Rasio Etanol dan Air Cucian Surimi Ikan Gabus (Channa striata) Terhadap Recovery Protein Larut Air Wiranata, Nurhadi; Baehaki, Ace; Lestari, Susi
Jurnal FishtecH Vol 4, No 1 (2015)
Publisher : Jurnal FishtecH

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (297.889 KB)

Abstract

The objective of this research was to know the deposition of protein in snakehead fish (Channa striata) surimi wash water and know the effect of the ratio of ethanol and surimi wash water from snakehead fish (Channa striata) on the recovery of protein water solubility. Design was used with two factors of treatment which were repeated twice. The factors of treatment consist of surimi wash frequency and the addition of ethanol concentration. The parameters observed were water-soluble protein analysis and SDS-PAGE analysis. The highest precipitation in the treatment T2, while the lowest precipitation in treatment T0. Based on BJND test, every treatment showed different precipitated with other treatments. In each sample the water-soluble protein content (PLA) in the first washing is greater than the second washing. Based on BJND test, treatment T1, T2, and T3 were not different but significantly different with treatment T0 (without ethanol). The treatment effect of the ratio of ethanol and surimi wash water from snakehead fish effect on the percentage of water-soluble protein content. SDS-PAGE analysis showed treatment P1T0, P1T1, and P2T0 still contains albumin with a molecular weigh of 68.75 kDa. Results recovery of protein from the ratio effects of ethanol and snakehead fish surimi wash water from showed thet the use of ethanol is able to precipitate proteins. The use of ethanol is added to snakehead surimi wash water serves as a coagulant.
Analisis Mutu Ikan Lele (Clarias batrachus) Asap Produksi Rakyat di Jalan Lintas Musi II Desa Keramasan, Kertapati, Palembang Citra, Firnanda; Yuliati, Kiki; Baehaki, Ace
Jurnal FishtecH Vol 4, No 1 (2015)
Publisher : Jurnal FishtecH

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (268.846 KB)

Abstract

The purpose of this research was to analize the quality of smoked catfish sold at Musi Dua street data were obtained through and series of survey. The smoke fish processing staser were material of supply, clear of weeds, washing of fish, work with salt and furnigation. Furnigation was a process in very important because can be specific character of smoke fish in the production. The result of the microbiology smoke catfish with sampling showed average be able to 1.8x106, 1.7x106 and 1.65x107. The result of the chemistry analysis smoke catfish showed in water activity of testing was about 0.84. The result standard water of testing showed smoke catfish was about 46.8% until 48.8% for every sample.