E3S Web Conf.
Volume 67, 2018The 3rd International Tropical Renewable Energy Conference “Sustainable Development of Tropical Renewable Energy” (i-TREC 2018)
|Number of page(s)||6|
|Section||Multifunctional and Advanced Materials|
|Published online||26 November 2018|
The Influences of transglutaminase enzyme dosage on the meat characteristic from restructuring the animal and vegetable protein sources
Bioprocess Engineering Study Program, Departement of Chemical Engineering, Faculty of Engineering Universitas Indonesia, Depok 16424, Indonesia.
* Coresponding author: firstname.lastname@example.org
Transglutaminase (EC 18.104.22.168) catalyses an acyl-transfer reaction in which the γ-carboxamide group of peptide-bound glutaminyl residues are the acyl donors. In this research is compare the influence of transglutaminase enzyme dosage on the animal protein which is duck meat and vegetable protein which is analog meat from TSP and soy powder. The sample was tested by some instrument analysis namely pH meter, Texture Profile Analyzer (TPA). Then, the sample was analized its nutrition by Proximate test. By these tests, it could be obtained the optimum of amount transgluminase dosage in animal or vegetable protein source. The experimental variations is the enzyme dosage. The enzyme dosage for animal protein source are 0.0%; 0.3%; 0.6% and 1%, while vegetable protein source are 0.0%; 0.5%; 1,0%; 1.5% and 2% with the duration of 24 h incubation in 4°C. The result showed that the characteristic of each sample observed, increased dosage of transglutaminase enzyme affects the texture of sample as evedenced by TPA. In animal protein the optimum enzyme used is 0,6 %, while in vegetable protein the optimum enzyme is 1,5% as evedenced by TPA and acidity test level.
© The Authors, published by EDP Sciences, 2018
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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