95, Ciputat, Jakarta 15412, Indonesia, Telp. Publisher Department of Chemistry, Faculty of Science and Technology, Syarif Hidayatullah Jakarta State Islamic University, Identification of marker peptides in digested gelatins by high performance liquid chromatography/mass spectrometry. Zhang GF, Liu T, Wang Q, Lei JD, Ma GH, Su ZG. Extensive deuterium back-exchange in certain immobilized pepsin columns used for H/D exchange mass spectrometry. Journal of Pharmaceutical and Biomedical Analysis I. Differentiation of bovine from porcine gelatins using polyclonal anti-peptide antibodies in indirect and competitive indirect ELISA. Journal of Pharmaceutical and Biomedical Analysis. Differentiation of bovine and porcine gelatins using principal component analysis. Nemati M, Oveisi MR, Abdollahi H, Sabzevari O. Memahami Gelatin, didownload dari 7 Juni 2012. Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution. Journal of Food Composition and AnalysisI.
GELATINE BOVINE ADALAH SKIN
Effect of gelatins on calcium phosphate precipitation: a possible application for distinguishing bovine bone gelatin from porcine skin gelatin. Differentiation of bovine and porcine gelatin based on spectroscopic and electrophoretic analysis. Potential use of fourier transform infrared spectroscopy for differentiation of bovine and porcine gelatins. Hashim DM, Che Man YB, Norakasha R, Shuhaimi M, Salmah Y, Syahariza YB. Chemical and functional properties of bovine and porcine skin gelatin. Hafidz RN, Yaakob CM, Amin I, Noorfaizan A. Porous chitosan gelatin scaffold containing plasmid DNA encoding transforming growth factor-α1 for chrondrocytes proliferation. Guo T, Zhao J, Chang J, Ding Z, Hong H, Chen J, Zhang J.
Gelatine-Based Biomaterials and Their Biocompatibility: Review and Perspectives, Biomaterials Applications for Nanomedicine, Prof. International Food Research Journal 19 (3): 1175-1180.
Differentiation of bovine and porcine gelatins in processed products via Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) and principal component analysis (PCA) techniques. Kinetics and mechanism of pepsinogen activation. Based on the results,each of the samples were tested contain of bovine gelatin respectively.Īl-Janabi J, JA Hartsuck, et al. Similar results were obtained on a sample of hard capsules with bands of protein fragments that were identical to bovine gelatinstandard. The results showed there were of specific bands of bovine gelatin with a molecular weight of 11,4 kDa 34 kDa 47kDa and specific bands of pork gelatin with a molecular weight of 24.7 kDa 28 kDa and 60 kDa. Hydrolysis time optimization throught applied to identify the source of hard gelatin capsules in the samples obtained from market and compared with the simulation of hard gelatin capsules.
Identification of gelatin hydrolyzate fragments were carried by molecular weight.
Gelatin hydrolyzateswere analyzed by SDS-PAGE to determine the optimal hydrolysis time. In the early stages, optimization of standards bovine and pork gelatin were hydrolyzed by pepsin at pH 4.5 and 60☌ for 1 hour, 2 hours, and 3 hours. The main of study is determine the source of gelatin used in hard capsules by using SDS-PAGE ( Sodium Dodecyl Sulphate Gel electrophoresis Poly Acrylamide) method. One of gelatin source is came from collagen of the skin and bones of bovine or pork. Most of gelatin production remains largely derived from non-halal materials. Gelatin as the main ingredient of capsules is still a problem for a moslem.
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