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Synthesis of collagen from Bali cattle's hide using a combination of acid and alkali on the extracting process Said, M. I.; Burhan, B.; Tensi, T.; Haerati, H.
Journal of the Indonesian Tropical Animal Agriculture Vol 43, No 3 (2018): September
Publisher : Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (276.089 KB) | DOI: 10.14710/jitaa.43.3.247-256

Abstract

The process of pre-extraction is an important stage in the process of collagen synthesis. This stage increases the sensitivity of collagen molecule chains that can affect production yields and collagen properties. The objectives of the study were to synthesize and evaluate halal collagen from Bali cattle?s hide on different -extracting processes. A total of 5 treatments applied in this study, namely: T1 = Ca(OH)2 5% (b/v) ; T2= Ca(OH)2 15% (b/v) ; T3= Ca(OH)2 5% + CH3COOH 5%(b/v) ; T4= Ca(OH)2 15% + CH3COOH 5% (b/v). Each treatment was repeated 4 times. Data were analyzed in a variety of ways using SPSS program. The observed parameters consisted of: 1) yield, 2) viscosity and 3) pH. The results showed that the difference in real pre-extracting process increased the yield and viscosity, but not the pH value. The application of T4 treatment provided the best results compared to other treatments as well as controls to increase the yield and also improve the collagen's physical properties and pH.
THE EFFECT OF CURING PROCESS IN ACETIC ACID ON THE GELATIN PROPERTIES OF BLINGON GOAT SKIN Said, M. I.; Triatmojo, S.; Erwanto, Y.; Fudholi, A.
Jurnal Ilmu dan Teknologi Peternakan Vol 3, No 2 (2014)
Publisher : Fakultas Peternakan, Universitas Hasanuddin, Makassar

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Abstract

Bligon goat is a cross between Kacang with Ettawah goat.  The skin of Bligon goat contains collagen protein compounds that have the potential to be processed into gelatin. Curing process is necessary to improve the properties of gelatin both quantitative and qualitative.  The purpose of this study was to identification of the best process time and level of acetat acid as curing materials of Blingon goat skin.  The skin of male Bligon goat age  ±1.5-2.5 years of old and acetic acid (CH3COOH 0.5 M) were used as material.  The experiment was run according to completely randomized design (CRD) with factorial pattern of 2x3 and three replications for each treatment.  Two processing time (48 and 96 hours) as first factor and three concentrations levels of acetic acid (3, 6 and 9%, v/v) as the second factor.   The data were analyzed by analysis of variance.  Yields, gel strength and viscosity were used as parameters. The results of this study showed that the processing time up to 96 hours and level of concentration up to 9% significantly affected (P<0.01 ) gel strength, but no significantly on the yields and viscosity. The combination of processing time of 96 hours with concentration level of 3% gave the best results compared to others.
ISOLATION AND IDENTIFICATION OF BACTERIA THAT HAS POTENTIAL AS PRODUCER OF PROTEASE ENZYME IN THE TANNERY INDUSTRY, PT. ADI SATRIA ABADI (ASA), YOGYAKARTA Said, M. I.; Likadja, J. C.
Jurnal Ilmu dan Teknologi Peternakan Vol 2, No 2 (2012)
Publisher : Fakultas Peternakan, Universitas Hasanuddin, Makassar

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Abstract

Bacteria are one of the microorganisms that have the potential as a producer of protease enzyme. Tannery industrial waste is one of the media predicted to contain a number of proteolytic bacteria because of the waste generated is composed largely of protein and fat which are good as growing medium for bacteria. This study aimed to isolate and identify bacteria that have the potential as a producer of protease enzyme. Research conducted at the waste water processing installation (WWPI), tannery industry of PT.Adi Satria Abadi (ASA), Sitimulyo, Bantul, Yogyakarta and Laboratory of Animal Product and Food, Faculty of Animal Science, Gadjah Mada University, Yogyakarta. Solid waste (SW), waste water (WW) and soil (S) around the industry are used as source of isolates. Random screening methods used for isolation and identification. The results obtained by isolation and identification of 1264 colonies (621 colonies from the SW, 156 of the WW and 487 of S). Thirty one colonies (2.5%) were identified as potentially proteolytic bacteria by the presence of clear zone (halo) around the colony while the 1.233 colonies (97.5%) were not potential. The third colony isolates look like a white crust, firmly attached to the medium, round, white to resemble wool and convex. Bacterial isolates from the S and SW at pH 10 and 12 were potential as a source of proteases with Proteolytic Index (PI)?3, while the one isolated from WW was less potential.
EFFECT OF TIME AND CURING CONCENTRATION ON QUANTITY AND QUALITY OF GOAT SKIN GELATIN PRODUCED BY ACID PROCESS Said, M. I.; Likadja, J. C.; Hatta, M.
Jurnal Ilmu dan Teknologi Peternakan Vol 1, No 2 (2011)
Publisher : Fakultas Peternakan, Universitas Hasanuddin, Makassar

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Abstract

Gelatin is widely used in food and non-food industries. One of its utilizations  in the food industry is as a biopolymer packaging materials to extend product shelf life. The quantity and quality of gelatin used is influenced by the production process, especially the curing period. This study aimed to determine the effect of curing time and concentration of curing agent  on the quantity and quality of gelatin produced from goat skin by acid process. Material used in this experiment was goat skin of Ettawah cross male, 1.5 to 3 years old.  The experiment was carried out in a 2x3 factorial arrangement according to completely randomized design with three replications for each treatment combination.  The first factor was curing time, i.e. 2 and 4 days and the second factor was the concentration of curing  agent, i.e. 3, 6 and 9%.  The gelatin was produced by the treatment with acetic acid (CH3COOH 0.5 M, v/v) as the curing  agent.  The results showed that application of CH3COOH 0.5 M with  concentration of 9% for 4 days yielded the best quantity and quality of gelatin, with product characteristics are yields of 16,39% and protein contents of  90.74%.