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EXPRESSION OF LON-LIKE PROTEASE GENE FROM LACTOBACILLUS PLANTARUM IIA-1A5 IN ESCHERICHIA COLI BL21(DE3) Mega, Olfa; Sumantri, Cece; Arief, Irma Isnafia; Budiman, Cahyo
Jurnal Agripet Vol 19, No 2 (2019): Volume 19, No. 2, Oktober 2019
Publisher : Agricultural Faculty

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (835.803 KB) | DOI: 10.17969/agripet.v19i2.14904

Abstract

Proteases are one of most important and abundant enzymes produced by the biotechnology industry, for scientific, physiological and industrial application and dominates of the whole enzyme market. Lactobacillus plantarum IIA-1A5 is an Indonesian lactic acid bacteria (LAB) isolated from beef Peranakan Ongole cattle. Preliminary analysis on its whole genome sequence indicated that this strain harbours some genes involved in protein degradation and might be promising to be further applied. This study aims to optimize the gene sequence of a lon-like protease of L. plantarum IIA-1A5 for heterologous expression system. The Lon-like gene expression system is made using genes that have been optimized first in silico.  pET-28a(+), E. coli BL21(DE3), Nde1 and BamH1 were used in this study as a expression vector, a host and retriction enzyme, respectively.  Molecular weight was validated using SDS-PAGE and expasy.org software. The results showed that optimization increased codon adaptation index value (CAI) and GC content to 0.97 and 56.57%, respectively, which were suitable for the E. coli expression system. The Lon-like IIA gene was successfully expressed in the cell cytoplasm by induction of 1 mM Isopropyl ?-D-1-thiogalactopyranoside (IPTG) at 37 °C.  As many as 88% of Lon-like IIA codons were distributed in the 91-100 quality group. Lon-like IIA was successfully expressed in a host cell induced with 1 mM IPTG at 37oC . IPTG induction was performed at the 3rd hour of incubation with OD600 0.59. In addition, Lon-like IIA molecular weight was detected approximately 43 kDa.
ISOLASI LISOZIM ALBUMIN TELUR AYAM RAS DENGAN METODE KROMATOGRAFI PENUKAR ION Wulandari, Zakiah; Fardiaz, Dedi; Thenawijaya, Maggy; Yuliana, Nancy Dewi; Budiman, Cahyo
Jurnal Teknologi dan Industri Pangan Vol. 29 No. 2 (2018): 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 (321.654 KB) | DOI: 10.6066/jtip.2018.29.2.155

Abstract

Lysozyme is one of the proteins found in hen egg albumin. Besides known as antimicrobial agents, lysozyme hydrolysis products can also function as antioxidants and as angiotensin converting enzyme (ACE) inhibitors. The lysozyme is also known to have lysine and arginine that can give a sweet taste. The research aimed to isolate lysozyme from commercial laying hen eggs. The isolation and purification of the eggs lysozyme was done by preparative and analytical separation technique using cation exchange resins.  The preparative separation was carried out by centrifugation of a large sample size of 205 g by centrifuga-tion, while the analytical separation only used only 3.16 g sample with a column measuring 13 cm in length and 3 cm in diameter. The number of samples isolated by preparative separation is greater than that with analytical method. The preparative separation was conducted in order to obtain the pure isolated lysozyme in higher quantity for further testing purposes. The purity of the isolated lysozyme from preparative separa-tion was 68.62% and the purity of isolated lysozyme from analytical separation was 63.03%. 
The Ghrelin Receptor (Ghsr) Gene Polymorphism in Indonesian Local Chicken and Crossbreed Is Associated With Carcass Traits Khaerunnisa, Isyana; Jakaria, Jakaria; Arief, Irma Isnafia; Budiman, Cahyo; Sumantri, Cece
ANIMAL PRODUCTION Vol 19, No 2 (2017)
Publisher : Universitas Jenderal Soedirman, Faculty of Animal Science, Purwokerto-Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (943.521 KB) | DOI: 10.20884/1.jap.2017.19.2.596

Abstract

Ghrelin receptor (GHSR) gene is candidate gene for growth performance in chicken by modulating growth hormone release from the pituitary by binding to its ligand of ghrelin. Ghrelin gene, or growth hormone secretagogue (GHS) gene, is well known as feed intake and energy homeostasis regulator in mammals and birds. The objectives of this study were to identify the polymorphism of the T1857C GHSR locus in Indonesian local chicken and to evaluate its effects on carcass traits. The gene polymorphism was identified using polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) using Hin6I restriction enzyme. Effect of genotype on carcass composition was analyzed using SAS General Linear Model (GLM) procedure. The genotyping was performed on 343 individuals including Merawang, Pelung, Sentul, Kampung, broiler (strain Cobb, parent stock), F1 crossbred of Kampung x broiler (strain Cobb, parent stock), and F2 crossbred of Kampung x broiler (strain Cobb, parent stock). All individuals were successfully amplified and were resulted in a 470 bp PCR product. This locus was polymorphic with two alleles (T and C) and three genotypes (TT, CT, and CC). The T allele and TT genotype were predominant in all populations. Individuals with CT genotype were significantly had higher live weight at 26w, carcass weight, commercial cuts weights, and muscles weights than TT genotype in F2 crossbred of Kampung x broiler population. Association of the T1857C GHSR locus-polymorphism with chicken carcass composition has been described in Indonesian chicken, providing evidence that GHSR might be an important candidate gene for chicken carcass traits.
CHARACTERISTIC OF LAMB SAUSAGES FERMENTED BY INDONESIAN MEAT-DERIVED PROBIOTIC, LACTOBACILLUS PLANTARUM IIA-2C12 AND LACTOBACILLUS ACIDOPHILUS IIA-2B4 Sulaiman, Noraimah Binti; Arief, Irma Isnafia; Budiman, Cahyo
Media Peternakan Vol. 39 No. 2 (2016): Media Peternakan
Publisher : Faculty of Animal Science, Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (703.841 KB) | DOI: 10.5398/medpet.2016.39.2.104

Abstract

Probiotic is a group of microorganism, mainly from lactic acid bacteria (LAB), widely used to increase functionality of various foodstuffs, including lamb which was limited by its goaty odor and short life issue. This study aimed to evaluate the characteristic of lamb sausages fermented by either Lactobacillus plantarum IIA-2C12 or L. acidophilus IIA-2B4 isolated from local cattle in Indonesia, and stored for 21 days at low temperature (4oC). Fermented lamb sausages were made with the addition of L. plantarum IIA-2C12 and L. acidophilus IIA-2B4 with three replications. The result showed that pH value, protein, and cholesterol contents of the sausages with addition of L. acidophilus IIA-2B4 were higher (P<0.05) than that of L. plantarum IIA-2C12. Meanwhile, the sausage fermented with L. plantarum IIA-2C12 had higher titratable acid (TA) value, texture, and the content of fat, carbohydrate, tyrosine, lysine, myristoleic (C14:1), pentadecanoic (C15:0), heneicosanoic (C21:0) and cis-11-eicosatrienoic (C20:1) as compared to that of  L. acidophilus 2C12-2B4. Final population of LAB in the sausage fermented by L. plantarum IIA-2C12 was also higher than that of L. acidophilus IIA-2B4, yet both can be categorized as a probiotic. The differences between characteristics of the physicochemical traits and microbiological quality of the sausage fermentation associated with the addition of L. plantarum IIA-2C12 or L. acidophilus IIA-2B4. The 21 days of storage at cold temperatures with probiotics addition could extend shelf life and maintain quality of fermented sausage.
PURIFICATION OF EGG WHITE LYSOZYME FROM INDONESIAN KAMPUNG CHICKEN AND DUCKS Wulandari, Zakiah; Fardiaz, Dedi; Budiman, Cahyo; Suryati, Tuti; Herawati, Dian
Media Peternakan Vol. 38 No. 1 (2015): Media Peternakan
Publisher : Faculty of Animal Science, Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (829.373 KB) | DOI: 10.5398/medpet.2015.38.1.18

Abstract

Egg white lysozyme (EWL) has considerably a wide functional protein exhibiting antibacterial activity mainly against Gram-positive bacteria. The EWL is widely applied in food industry and is considerably safe. Despite its high potency, EWL of Indonesian poultry has never been studied and exploited. This study was aimed to purify EWL from two Indonesian poultry: kampung chicken and Cihateup duck, and compared to egg of commercial laying hens. The eggs in this study were obtained from field laboratory of Faculty of Animal Science, Bogor Agricultural University (IPB) and classified in AA quality based on the interior quality. First attempt to purify the EWL was performed by using ethanol precipitation yielding purified EWL which was still contaminated by other proteins, hence designated as partially purified EWL. Final concentrations of partially purified EWL of kampung chicken, commercial laying hens, and Cihateup duck were about 5800, 5400, and 5500 ?g/mL, respectively. To confirm whether the use of ethanol in the purification affecting EWL antibacterial activities, the activities were examined against Staphylococcus aureus. It demonstrated that the partially purified EWL exhibited ability to inhibit S. aureus at 6 and 26 h suggesting that the method was feasible as it did not interfere EWL antibacterial activities. Yet, based on SDS-Page, purity was the issue in ethanol precipitation method. Further attempt using ion exchange chromatography at pH 10 successfully purified lysozyme as indicated by a single band corresponding to lysozyme size (~14 kD) free from bands of other proteins. Altogether, a single step of ion exchange chromatography is sufficient and promising to isolate EWL from Indonesian poultry for various industrial purposes.Key words: Indonesian poultry, lysozyme, egg, kampung chicken, Cihateup duck
PHYSICOCHEMICAL CHARACTERISTICS AND MICROBIOLOGICAL QUALITY OF THE TOPSIDE AND LONGISSIMUS DORSI OF INDONESIAN LOCAL BUFFALO MEAT Sulaiman, Noraimah Binti; Sumantri, Cece; Arief, Irma Isnafia; Budiman, Cahyo
Buletin Peternakan Vol 44, No 2 (2020): BULETIN PETERNAKAN VOL. 44 (2) MAY 2020
Publisher : Faculty of Animal Science, Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (401.888 KB) | DOI: 10.21059/buletinpeternak.v44i2.45544

Abstract

The physicochemical characteristics and microbiological quality of buffalo meat are influenced by differences in muscle type. This study aimed to evaluate the physiochemical characteristic and microbiological quality of the topside (active muscle) and longissimus dorsi (passive muscle) of Indonesian local buffalo meat. Samples used in this study were buffalo meat from local swamp buffalo, aged more than four years old on the topside and longissimus dorsi. This study used a completely randomized design, with three repetitions in each treatment. All data were analyzed using analysis of variance (ANOVA). The result of the study on the topside and longissimus dorsi area showed a significant difference in the pH and cholesterol levels of the buffalo meat. The longissimus dorsi area had a lower level of pH and cholesterol compared to the topside area. Furthermore, this longissimus dorsi meat has a higher color, protein, ash, fat, essential amino acid, and lactic acid bacterial (BAL) content than the topside meat. However, the topside meat had higher carbohydrate, essential fatty acid, Escherichia coli (E. coli) and Staphylococcus aureus (S. aureus) content compared to the longissimus dorsi meat. Longissimus dorsi meat had better physicochemical characteristics and microbiological quality than the topside meat