International Research Journal of - simdos.unud.ac.id · College of Veterinary Science, Assam Agricultural University, Guwauhati, India Editor-in-Chief ... Department Ganesha University

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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

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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

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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






http://ijcu.us/online/journal/index.php/irjeis/article/view/488



http://dx.doi.org/10.21744/irjeis.v3i4.488






















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

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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

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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

































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.


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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

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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



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.

References

Apriyantono, HA. 2003. Halal Paper: The Linkage between Syar'i, Technology, and Certification.

www.indohalal.com/doc-halal2.html.

Brown, EM., King, G., and Chen, JM. 1997. Model of The Helical Portion of A Type I Collagen

Microfibril. Jalca.92.1-7.

Djojowidagdo, S. 1988. Leather Buffalo Buffalo Leather, Properties, and Its Characteristics As Purwa

Leather Puppet. Dissertation. Gadjah Mada University, Yogyakarta.

Miwada, IN. S. and I N. Simpen. 2014. Production and formulation of gelatin based edible coatings from

cattle leg skin and its potential in maintaining the quality of meatballs. Competitive Grant Research

Report. Udayana University

Miwada, IN.S and IN. Simpen. 2007. Optimization of Chicken Spread Potential (Shank) RPA Waste

Result Through Modified Extraction Method to Produce Gelatin. Ranch Scientific Magazine 10(1): 5-

8.

Miwada, IN.S., IN. Simpen, M. Hartawan, A.W. Puger and NL.P. Sriyani. 2015. Characteristics of

Gelatin from the Foot of Livestock and Its Potential as an Edible Film. Ranch Scientific Magazine.

18(3) : 109-113

Miwada, INS. and Simpen, IN. 2013. Study of Acid Curing Acid Time and Combination Ratio of

Chloroform-Ethanol for Ceker Skin Protein Extraction. Ranch Scientific Magazine 16(1):28-31.

Pearson, AM. and Dutson TR. 1992. Inedible Meat by Product Advances in Meat. Research. Vol. 8.

London and New York.

Sarkar, KT. 1995. Theory and Practice of Leather Manufacture. Publ. The Author 4. Second Avenue

Mahatma Gandhi Road. Madras.

Schrieber, R. and H. Gareis. 2007. Gelatine Handbook Theory and Industrial Practice. WILEY-VCH

Verlag Gmbh & Co. KGaA, Weinheim.

Soeparno. 1998. Meat Science and Technology. Gadjah Mada University Press. Yogyakarta.

Swatland, HJ. 1984. Structure and Development of Meat Animals. 56-63. Prentice Hall. Inc. Englewood

Cliffs. New Jersey.

http://www.indohalal.com/doc-halal2.html



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


HP : 082146495250

Institution : Faculty of Animal Science Udayana University, Bukit Jimbaran-Badung,

Bali

Address : Jalan Kembang Matahari No. 8 Denpasar


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





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International Research Journal of - simdos.unud.ac.id · College of Veterinary Science, Assam Agricultural University, Guwauhati, India Editor-in-Chief ... Department Ganesha University