Yusro Nuri Fawzya
Balai Besar Riset Pengolahan Produk dan Bioteknologi Kelautan dan Perikanan

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PURIFICATION AND CHARACTERIZATION OF THE NEWLY THERMOSTABLE PROTEASE PRODUCED BY Brevibacillus thermoruber LII ISOLATED FROM PADANG CERMIN HOTSPRING, INDONESIA Zilda, Dewi Zeswita; Harmayani, Eni; Widada, Jaka; Asmara, Widya; Irianto, Hari Eko; Patantis, Gintung; Fawzya, Yusro Nuri
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 9, No 1 (2014): May 2014
Publisher : Research and Development Center for Marine and Fisheries Product Processing and Biotechnol

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.v9i1.91

Abstract

Thermo stability is among of the vital enzyme characteristics for industrial application. Brevibacillus thermoruber LII was obtained as a potential isolate from the previous researchwhich screened the potential thermostable protease producing bacteria from Indonesian hotspring.The newly thermostable protease produced by thermophilic Brevibacillus thermoruber LII hadbeen purified and characterized. It was predicted that the pure enzyme obtained from Brevibacillusthermoruber LII was homo hexameric, having molecular weight of 36 kDa unit protein and itsnative was 215 kDa. In addition, it was also a neutral metalo serine protease according tobiochemical tests that it was totaly inhibited by PMSF (Phenylmethanesulfonyl fluoride) and EDTA(Ethylenediaminetetraacetic acid). It showed optimum activity at pH of 8 and active in acidic buffer(up to pH of 4). All of metal ion in the form of chloride salt (2.5 mM) which were tested on theenzyme enhanced the enzyme activity but Li2+. Ca2+ion increased the activity and the stability ofenzyme against thermal. The enzyme also showed the stability against solvent. The protease LIIhad optimum temperature at 60oC without CaCl 2and 80 – 85oC with addition of 2.5 mM CaCl 2. TheK Mand V maxvalues for the purified protease LII were 27.2 mg/ml or 0.362 – 0.272 M for substrateHammersteinCasein (MM 75–100 kDa) and 261.1 µg/minute/ml, respectively.
Identification of Protease-Producing Bacteria Isolated from Banyuwedang, Bali, and Characterization of its Protease Zilda, Dewi Seswita; Fawzya, Yusro Nuri; Uria, Agustinus Robert
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 13, No 3 (2018): December 2018
Publisher : Research and Development Center for Marine and Fisheries Product Processing and Biotechnol

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.v13i3.367

Abstract

Proteases or peptidases is known as a largest group of hydrolytic enzymes and have been applied in various industries such as food, pharmacy, leather, detergent and waste treatment. Although they are also produced by plants and animals, microbes remain the main source of proteases in the world market which mostly derived from Bacillus sp. Aims of this research were to identify isolate BII-1 and study its protease. Analysis of 16Sr RNA sequencing showed the identity of BII-1 as Bacillus subtilis (99% similarity with the same species in GenBank). It was found that protease from BII-1 exhibited optimal temperature and pH of 50 oC and 8-9, respectively. It was activated by Li2+, Na2+, Mg2+ and K+. The degenerated primer for protease gene was designed, and a partial protease gene was amplified from BII-1. The sequencing result showed that this amplified gene shared 100 and 99% similarity with those from Geobacillus thermophiles and Bacillus subtilis in the GenBank, respectively.Keywords: protease, bacteria, Bacillus subtilis, Geobacillus thermophylus
Pengaruh Garam dan Enzim Transglutaminase Terhadap Sifat Fisik dan Sensori Daging Restrukturisasi Ikan Mata Goyang Fawzya, Yusro Nuri; Gunawan, Gunawan; Patantis, Gintung
Jurnal Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 6, No 1 (2011): Juni 2011
Publisher : Balai Besar Riset Pengolahan Produk dan Bioteknologi Kelautan dan Perikanan

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/jpbkp.v6i1.88

Abstract

ABSTRACTThe important thing considered in the processing of fish mince meat based products is gel forming ability, which is affected by additives applied in the processing of the products. This research was aimed at studying the effect of TGase and salt addition on the physical and sensory properties of restructured product from Priacanthus macracanthus. Salt was added into minced meat at the concentration of 0, 1 and 2%, TGase with the concentration of 0; 0.3; 0.6 and 1%. The meat dough was then filled into plastic tubes and heated at 30oC for an hour before being heated at 90oC. The restructured meat was then evaluated its sensory properties texture profile (hardness,chewiness, gumminess, cohesiveness, springiness and breaking force, deformation/distance, gel strength), and its microscopic observation under the scanning electron microscope. The result showed that addition of salt as well as TGase gave significant effect on the sensory properties related to texture, appearance and brightness; and physical properties ofthe restructured products espescially gumminess and breaking force. Based on the sensory score, addition of 2% salt wasenough to produce gel which met with panelist preference, however based on the physical/texture properties addition of 2% salt and 0.3% TGase was needed to increase the gel properties. At this treatment combination, the gel strength produced was 3,235 g cm.
Produksi dan Karakterisasi Xilanase dari Isolat Bakteri M-13.2a Asal Air Laut Manado Fawzya, Yusro Nuri; Mangunwardoyo, Wibowo; Munifah, Ifah; Patantis, Gintung
Jurnal Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 8, No 1 (2013): Juni 2013
Publisher : Balai Besar Riset Pengolahan Produk dan Bioteknologi Kelautan dan Perikanan

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/jpbkp.v8i1.53

Abstract

Isolat bakteri M-13.2A yang berasal dari laut Manado diketahui mampu menghasilkan enzim selulase dan xilanase, berdasarkan pembentukan zona bening pada media padat. Penelitian ini bertujuan untuk mendapatkan informasi lebih lanjut mengenai produksi dan sifat enzim xilanase yang dihasilkan dari isolat bakteri M-13.2A serta identifikasi isolat bakteri tersebut di atas. Sebanyak (2,4-3,3) x 108 cfu/ml inokulum dengan konsentrasi sekitar 9% (v/v) diinokulasikan dalam medium xylan broth, kemudian diinkubasi selama 6 hari pada suhu 30°C, 150 rpm. Pengambilan sampel dilakukan setiap hari dan enzim yang dihasilkan diuji aktivitasnya dengan metode asam dinitro salisilat (DNS). Hasil penelitian menunjukkan bahwa aktivitas xilanase tertinggi dihasilkan pada hari ke-2 inkubasi, sebesar 5,17 U/ml. Enzim xilanase ini bekerja optimum pada pH 8, suhu 70°C. Penambahan ion logam 10 mM memberikan pengaruh yang bervariasi terhadap aktivitas enzim. Ion Zn2+ meningkatkan aktivitas xilanase hingga 278,1%. Ion Fe3+ dan Ca2+ menurunkan aktivitas xilanase menjadi 75 dan 8,3% relatif terhadap kontrol, sedangkan ion K+ tidak memberikan pengaruh terhadap aktivitas xilanase. Hasil identifikasi bakteri menunjukkan bahwa isolat M-13.2A memiliki kemiripan 99% dengan Acinetobacter baumannii.
Karakterisasi Enzim Kitinase yang Diproduksi Oleh Isolat Bakteri Jb4 Dari Terasi Noviendri, Dedi; Chasanah, Ekowati; Fawzya, Yusro Nuri
Jurnal Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 1, No 2 (2006): Desember 2006
Publisher : Balai Besar Riset Pengolahan Produk dan Bioteknologi Kelautan dan Perikanan

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/jpbkp.v1i2.390

Abstract

Penelitian karakterisasi enzim kitinase yang diproduksi oleh isolat bakteri JB4 dari terasi telah dilakukan. Karakterisasi enzim mencakup penentuan suhu dan pH optimum, stabilitas enzim, dan pengaruh adanya ion logam terhadap aktivitas enzim. Dari hasil penelitian ini diperoleh enzim kitinase mempunyai suhu optimum 40ºC dan pH optimumnya 8,0. Enzim ini memiliki kernampuan stabilitas panas pada suhu 40ºC. Kation monovalen NH+ dan Na+ dengan konsentrasi 1,0 mM diketahui dapat berfungsi sebagai aktivator bagi enzim kitinase isolat JB4. sebaliknya kation divalen Mg2+,Cu2+ Co2+, Zn2+ , Ba2+, Ca2+ dan kation trivalen Fe3+ dengan konsentrasi akhir 1,0 mM merupakan inhibitor bagi enzim kitinase dari isolat tersebut.
Enzymatic Production of Fish Protein Hydrolysates in A Pilot Plant Scale Martosuyono, Pujoyuwono; Fawzya, Yusro Nuri; Patantis, Gintung; Sugiyono, Sugiyono
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 14, No 2 (2019): August 2019
Publisher : Research and Development Center for Marine and Fisheries Product Processing and Biotechnol

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (451.785 KB) | DOI: 10.15578/squalen.v14i2.398

Abstract

Protease enzyme produced from Bacillus sp was employed to hydrolyze fish protein hydrolysates (FPH) under controlled conditions at a batch-pilot plant scale-process. Thirty kilograms of fish meat was mincedand mixed with 60 liters of water in 100 liters stainless steel vessel and 20,000 units of protease enzyme was added per kg of fish. Hydrolysis of fish was carried out at 55 oC for 6 hours. Multi stage of filtration were done to separate the FPH from unhydrolized fish residue. Mass balance were carried out to determine the rate of hydrolysis and yields. W ithout pH adjustment, 80% of substrate hydrolyzed could be achieved in 6 hour at 55 °C. Three kinds of products were recovered from the process, i.e solid residue, liquid FPH as filtration product, and spray dried FPH. Hydrolysis of 30 kg of fish meat substrate producing 1.7-2.0 kg of unhydrolyzed residue and 70 L of liquid FPH. Afterspray drying process of liquid FPH, 13 kg of FPH powder was recovered. The proximate and amino acid analysis of spray dried FPH showed that the FPH containing 20% of protein, rich in amino acids especially lysine and leucineand the residue still had 85,36% of protein (dry basis) that could be utilized for other purpose.