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TABLE OF CONTENTS
No Title Page
1 The Implementation of Education National Standard in the
Instrument of School Accreditation of Bali Province Education
Authority Wayan Maba http://dx.doi.org/10.21744/irjeis.v3i4.488
1
2 Community Power as a Driving Force for Sustainable Local
Development Antonio Vázquez Pérez, María Rodríguez Gámez, Carlos Gustavo Villacreces Viteri,Alcira Magdalena Velez Quiroz http://dx.doi.org/10.21744/irjeis.v3i4.489
7
3 The Effect of Health Education towards Knowledge and Teenager
Attitudes in Consuming Liquor, Kupang City in 2016 Christine Ekawati, N Adiputra, Raka Sudewi, Dyah Pradnya Paramita Duarsa http://dx.doi.org/10.21744/irjeis.v3i4.495
18
4 Problems Faced by Teachers in Designing and Implementing
Authentic Assessment in Science Teaching I Wayan Suastra, Ni Putu Ristiati http://dx.doi.org/10.21744/irjeis.v3i4.496
24
5 Bruner’s Cognitive Stages and Their Effects on the Understanding
of Fraction Concept
NLM Dwijayanti, I Gusti Putu Suharta, Sariyasa http://dx.doi.org/10.21744/irjeis.v3i4.497
33
6 Ethnomathematics of Balinese Traditional Houses I Gusti Putu Suharta, I Gusti Putu Sudiarta, I Wayan Puja Astawa http://dx.doi.org/10.21744/irjeis.v3i4.501
42
7 Health Behavior and Status Related to Mother's Death in Timor-
Leste Feliciano Pinto, I Ketut Suwiyoga, I Gde Raka Widiana, I Wayan Putu Sutirta Yasa http://dx.doi.org/10.21744/irjeis.v3i4.505
51
IRJEIS Impact Factor: 5.211 ISSN: 2454-2261
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Scopus ID: 9F46766090560E8E; Impact Factor [SJIF 2016 = 5.211]
International Research Journal of Engineering, IT and Scientific Research
8 Developing Instructional Material for Sepak Takraw Playing
Technique Course Completed with Smart Audiovisual to Improve
Competencies of the Students of Sport & Health Education
Department Ganesha University of Education I Ketut Budaya Astra, I Wayan Artanayasa http://dx.doi.org/10.21744/irjeis.v3i4.506
59
9 Continuous Time H-Infinity Filter with Asymptotic Convergence Swetha Amit, Raol Jitendra R. http://dx.doi.org/10.21744/irjeis.v3i4.507
69
10 The Production and Quality of Mott Grass (Pennisetum Purpureum
CV. Mott) that Intercropped with Legume in the First Pruning Yan Tonga, I Nyoman Kaca, Luh Suariani, I Gede Sutapa, Ni Made Yudiastari, Ni Ketut Etty Suwitari http://dx.doi.org/10.21744/irjeis.v3i4.509
79
11 Reusing the Coconut Clay (Brick) as Construction Material Wilter Enrique Ruíz Párraga, Marcos A. Chica Párraga, Mario J. Vega Salazar, Juan J. Howland Albear http://dx.doi.org/10.21744/irjeis.v3i4.512
92
12 Amino Acid Profile on Shank Skin of Livestock and Antibacterial
Potential Study
IN. Sumerta Miwada, IK. Sukada, W. Sayang Yupardhi, SA. Lindawati http://dx.doi.org/10.21744/irjeis.v3i4.516
99
13 Aquifer Hydraulics Parameters Determination regarding One Well
Base on Geolistric Data (A Case Study in Bugbug Karangasem Bali) I Nengah Simpen, I Nyoman Sutarpa Sutama, I Wayan Redana, Siti Zulaikah http://dx.doi.org/10.21744/irjeis.v3i4.520
105
ISSN: 2454-2261 Impact Factor: 5.211 IRJEIS
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Scopus ID: 9F46766090560E8E; Impact Factor [SJIF 2016 = 5.211]
International Research Journal of Engineering, IT and Scientific Research
International Research Journal of Engineering, IT & Scientific Research (IRJEIS)
Available online at http://ijcu.us/online/journal/index.php/irjeis
Vol. 3 Issue 4, July 2017, pages: 99~104
ISSN: 2454-2261 Impact Factor: 5.211 | Thomson Reuters: K-4290-2016
: http://dx.doi.org/10.21744/irjeis.v3i4.516
99
Amino Acid Profile on Shank Skin of Livestock and
Antibacterial Potential Study
IN. Sumerta Miwada a
IK. Sukada b
W. Sayang Yupardhi c
SA. Lindawati d
Article history: Abstract
Received: 10 February 2017
Revised: 15 June 2017
Approved: 20 July 2017
Published: 28 July 2017
The objective of this study is to identify amino acids in the skin
character shank of livestock i.e. broiler chicken, cattle and goat
which has been hydrolyzed to gelatin. Besides that, also to observe
morphology gelatin product with the approach of Scanning Electron
Microscope (SEM) and identify potential gelatin-based on livestock
against shank skin as the antibacterial ability on the type of
Salmonella typhii, Escherichia coli and Staphylococcus aureus. The
results showed that the gelatin of the broiler chicken, cattle and goat
were dominated by a kind of essential amino acid histidine and
arginine. While the type of non-essential amino acids was
dominated by glutamic and serine. Morphology analysis of the
surface of gelatin with SEM approach showed that the surface
structure of the gelatin molecule extraction chicken shank skin was
more smooth and flat. While at the shank of the extracted skin of
cattle and goat were still many bundles detectable binding collagen
protein extracted was not perfect. Potential skin gelatin of various
livestock shank was conducted testing of potential anti-bacterial.
The results showed that the gelatin of the broiler chicken, cattle and
goat had no ability as pathogen antibacterial against Salmonella
typhii, Escherichia coli and Staphylococcus aureus. The conclusion
of the study that the dominant gelatin amino acid profile is detected
the essential amino acid histidine and arginine as well as types of
non-essential amino acid glutamic acid and serine type. Gelatin
morphology analysis with SEM approach is going on a smooth
surface on the broiler chicken. Gelatin test results on the ability of
pathogenic bacteria inhibition showed negative results (not found
inhibitory zone).
Keywords:
SEM;
Gelatin;
Amino Acid;
Shank Skin of Livestock;
2454-2261© Copyright 2017 The Author. Published by International
Journal of College and University. This is an open access article under the
CC-BY-SA license (https://creativecommons.org/licenses/by/4.0/)
All rights reserved.
a Faculty of Animal Science, Udayana University, Bukit-Jimbaran, Badung, Bali, Indonesia. b Faculty of Animal Science, Udayana University, Bukit-Jimbaran, Badung, Bali, Indonesia. c Faculty of Animal Science, Udayana University, Bukit-Jimbaran, Badung, Bali, Indonesia. d Faculty of Animal Science, Udayana University, Bukit-Jimbaran, Badung, Bali, Indonesia.
Impact Factor: 5.211 ISSN: 2454-2261
IRJEIS Vol. 3 Issue 4, July 2017, pages: 99~104
100
Author correspondence:
IN. Sumerta Miwada,
Faculty of Animal Science, Udayana University, Bukit-Jimbaran,
Badung, Bali, Indonesia., Email address: [email protected]
1. Introduction
Shank skin of livestock are by product of their slaughter and during years their potentiality is not used
maximally yet. For example, shank skin of broiler chicken, goat, and cattle where all their histology
structure is sesame, compose of epidermis and corium. This corium is the main component of the skin
particularly on livestock shank skin and dominated by collagen protein (Brown et al., 1977), although in
different percentage (Miwada and Simpen, 2014). Djoyowidagdo (1988) said that the older the animals,
their skin composition particularly collagen protein and fat concentrations are higher, but their ash
concentration is getting lower. Soeparno (1998) said that amount and collagen physical strengthen can
increase as the increases of animal age. Swatland (1984) explained that diameter collagen fiber is 1 – 12
µm, but parallel fibril connection that composes it is 20 – 100 nm. Furthermore, it is said that growth rate
of collagen fiber is getting decreases until a certain constant age is richer. Sarkar (1995) reported that
collagen small animal is about 30 – 33% (dry weight/dw), calf skin (84% dw), steers (87.2% dw) and
bulls (91.1% dw).
During years, there is no any study about protein potential on livestock shank skin of Broiler chicken,
cattle and goat particularly about profile amino acid that compose protein on animal shank skin which
was hydrolyzed become gelatin product. This study is important due to the potential of collagen protein
hydrolysis become gellatin is a potential product which is determined by its amino acid compositor.
Miwada et al. (2015) explained that advantages of livestock shank skin are as gellatin and its uses as
adible to increase the extra value of this by product. This matter is supported by Apriantono (2003) that
gelatin can be made from materials rich in collagen i.e. skin. Furthermore, he said that the advantages of
gelatin are very flexible, can be functioned as material content of drug capsule, emulsion, binder,
depositor, to increase nutritive value and to form an elastic thin layer and also to form transparent film
layer, strong and high digestibility. The objective of the study is to identify the character of amino acid on
shank skin of Broiler chicken, cattle and goat which were hydrolyzed became gelatin. Besides that, it is
also observed the morphology of gelatin product that was resulted with SEM approach and identify
gelatin potential base on livestock shank skin to their ability as an antibacterial on Salmonella typhii,
Escherichia coli and Staphylococcus aureus.
2. Research Methods
Materials
The main materials used in this study were shanked skin of broiler chicken, shank skin of goat and shank
skin of cattle for 1 kg each. Chemicals matter were including acetic acid (1.5%), ethanol, buffer pH 4.00,
7.00, 9.00 and distilled water. Test matter of microbiology including gelatin nutrient, PDA and others
were deionized water, ordinary filter paper, Whatman 42 filter paper.
Method
The first step of study implementation is started with made 1.5% concentration of the acetic acid solution.
Furthermore, shank skin of Broiler chicken, goat, and cattle that were provided with a method of
conventional skinned and protein hydrolysis of livestock shank skin with Miwada and Simpen
modification methods (2007 and 2013) including steps of curing with 1.5% concentration acetic acid with
1: 8 ratio. Curing was conducted for 3 days, then it was continued with minimalized of fat content with
using 65% ethanol solution (gelatine: ethanol ratio i.e. 1: 2) soaked for 1 hour. The result of fat
minimalization was continued with extraction i.e. additional of water distillation (1: 1 ratio) then morm up
performed in a water bath at a temperature of 61oC – 65oC for 1 hour, then continued for washing up,
filtering, evaporating of extract solution for congealing gelatin product that was obtained. Gelatin
characteristic examination of different skin matter was performed through HPLC method, gelatin
morphology observation (with SEM approach) and obstruct ability test to Salmonella typhii, Escherichia
coli, and Staphylococcus aureus.
3. Results and Analysis
Activities of the study were begun with profile determination of amino acid in gelatin of some
livestock shank skin production. This production process was performed with Miwada dan Simpen
methods (2007 and 2013) with a little modification. The result of dry gelatin production, in this case, their
IRJEIS ISSN: 2454-2261 Impact Factor: 5.211
Amino Acid Profile on Shank Skin of Livestock and Antibacterial Potential Study
(IN. Sumerta Miwada, IK. Sukada, W. Sayang Yupardhi, SA. Lindawati)
101
amino acids were examined with HPLC method each. Description of each amino acid in every gelatin of
livestock shank skin is presented as follows.
Figure 1.Amino Acid Profile of Broiler Chicken
Shank Skin Gelatin
Figure 2. Amino Acid Profile of Cattle Shank Skin
Gelatin Acid
Figure 3. Amino Acid Profile of Goat Shank Skin
Gelatin Acid
Figure 4. Standard of Amino Acid Profile
Quantitatively, amino acid component figure in gelatin of various livestock shank skin can be presented
in Table 1 as follows.
Table 1. Profile of Gelatin Amino Acid of Various Livestock Shank Skin
Number
Amino Acid
Various Livestock Shank skin References
Schrieber
and Gareis
(2007)
Gelatin of
Broiler
Chicken
Shank Skin
Gelatin of
Cattle Shank
Skin
Gelatin of
Goat shank
Skin
1 Aspartic Acid 3.018 3.038 3.668 2.900
2 Glutamic 10.169 10.796 11.782 4.800
3 Serine 9.470 9.604 9.903 3.500
4 Histidine 11.185 11.553 11.775 0.400
5 Glycine 2.754 3.019 3.205 33.000
Impact Factor: 5.211 ISSN: 2454-2261
IRJEIS Vol. 3 Issue 4, July 2017, pages: 99~104
102
6 Threonine 6.353 6.777 6.947 1.800
7 Arginine 6.094 6.508 6.815 4.900
8 Alanine 1.387 1.359 1.450 11.200
9 Tyrosine 1.486 1.682 1.801 0.260
10 Methionine 1.205 1.471 1.545 0.360
11 Valine 1.553 1.498 1.492 2.600
12 Phenylalanine 1.111 1.111 1.165 1.400
13 Isoleusine 3.114 3.156 2.871 1.00
14 Leucine 12.554 11.472 12.351 -
15 Lysine 7.516 7.336 7.117 2.700
Results of the study showed that gelatin of the ssb, ssc and ssg were dominated by essential amino acid
i.e. histidine and arginine. On the other hand that non-essential amino acid was dominated by glutamic
and serine. Pearson and Dutson (1992) reported that at curing process, change happen as result of skin
collagen protein and some certain amino acids denaturation changed chemically. But, an interesting
matter that found in this study (Table 1), essential and non-essential amino acids detected same high on
the broiler chicken, cattle and goat compare to references of Cshrieber and Gareis (2007).
Morphology analysis of gelatin surface as result of extraction with acetic acid (1.5% concentration)
was studied for 3 days through SEM approach. Results of analysis can be seen in Figure 1 completely.
Base on SEM test showed that gelatin molecule surface structure of shank skin Broiler chicken extract is
softer and flate. But, on shank skin cattle extraction, there is still many bundles of collagen protein
detected not extracted completely. Collagen protein extraction of goat shank skin in Figure 1 tends more
vicious, and even it is soaked in 1.5% acetic acid concentration for 3 days it still not is able to rich
maximum amount of gelatin from shank skin of goat for extracting completely. Result of gelatin surface
analysis on shank skin of livestock with SEM approach and this also support by Miwada et al. (2015) that
livestock shank skin extract with acetic acid curing method (1.5%) for 3 days resulted in the highest
gelatin extraction volume of collagen protein on Broiler chicken shank skin then followed by cattle and
goat respectively.
(a) (b) (c)
Figure 1. Scanning Electron Microscope Gelatin of The Broiler Chicken Shank Skin (a), Cattle (b) and Goat
(c) with 1000 Times Magnificence
Gelatin potential of various livestock shank skin was tested to their anti bacteria potential. The result of
the study showed that gelatin of shank skin of the broiler chicken shank, cattle and goat were had no
ability as pathogen antibacterial to Salmonella typhii, Escherichia coli, and Staphylococcus aureus. Those
approved by Miwada and Simpen (2014) that bacteria and total colly from Meatballs are still high during
their preserves in natural packed (edible coating) of this gelatin type and as an indication that there is no
potency to pursue bacteria growth rate.
4. Conclusion
The result of the study showed that dominant profile of amino acid detected on gelatin of shank skin
of Broiler chicken, cattle and goat were essential amino acid i.e. histidine and arginine and non-essential
amino acid i.e. glutamic and serine. The result of gelatin morphology analysis with SEM approach
produced a soft surface on the gelatin of broiler chicken shank skin. While gelatin of the cattle shank skin
IRJEIS ISSN: 2454-2261 Impact Factor: 5.211
Amino Acid Profile on Shank Skin of Livestock and Antibacterial Potential Study
(IN. Sumerta Miwada, IK. Sukada, W. Sayang Yupardhi, SA. Lindawati)
103
was seen no extracted completely yet, and the gelatin of goat shank skin was seen more viscous. The
result of gelatin test to pursue ability of pathogen bacteria showed negative (no pursue zone).
Acknowledgements
In this opportunity, we would like to express our gratitude to Udayana University and Dirjen Dikti, for
their help in financial support on the competitive present that caused the study activities could be
performed as usual.
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Sarkar, KT. 1995. Theory and Practice of Leather Manufacture. Publ. The Author 4. Second Avenue
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Swatland, HJ. 1984. Structure and Development of Meat Animals. 56-63. Prentice Hall. Inc. Englewood
Cliffs. New Jersey.
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IRJEIS Vol. 3 Issue 4, July 2017, pages: 99~104
104
Biography of Authors
Address : Banjar Pangkung, Pejaten, Kediri, Tabanan, Bali
E-mail : [email protected]
HP : 085857026532 Institution : Faculty of Animal Science Udayana University, Bukit Jimbaran-Badung,
Bali
Address : Jalan Segara Madia. No.2, Lingkungan Tanjung Benoa, Kelurahan Tanjung
Benoa, Kecamatan Kuta Selatan, Kabupaten Badung
E-mail : [email protected]
HP : 082146495250
Institution : Faculty of Animal Science Udayana University, Bukit Jimbaran-Badung,
Bali
Address : Jalan Kembang Matahari No. 8 Denpasar
E-mail : [email protected]
HP : 08179774658
Institution : Faculty of Animal Science Udayana University, Bukit Jimbaran-Badung, Bali
Address : Jalan Tegal Wangi II gang Cempaka Sari 8A Denpasar Bali E-mail : [email protected]
No HP : 081337325477
Institution : Faculty of Animal Science Udayana University, Bukit Jimbaran-Badung,
Bali