Malaysian
Journal of Analytical Sciences Vol 20 no 5 (2016): 1104 - 1111
DOI:
http://dx.doi.org/10.17576/mjas-2016-2005-16
ZETA POTENTIAL AND ENVIRONMENTAL
SCANNING ELECTRON MICROSCOPY ANALYSIS IN DEPROTEINISATION OF NATURAL RUBBER
LATEX
(Analisis Keupayaan Zeta dan Pengimbas Persekitaran Mikroskopi
Elektron di dalam Penyahprotein Lateks Getah Asli)
Nurulhuda
Abdullah*, Asrul Mustafa, Mok Kok Lang
Technology and
Engineering Division,
Malaysian Rubber
Board, 47000 Sungai Buloh, Selangor Darul Ehsan, Malaysia
*Corresponding author: nurulhuda.a@lgm.gov.my
Received: 10
June 2015; Accepted: 21 July 2016
Abstract
This paper describes the effect of
protein denaturants namely, urea and sodium dodecyl sulphate (SDS) in the deproteinisation
of high ammonia natural rubber latex (HA-NRL). It had been shown that latex
proteins were reduced more in the presence of urea alone (48%) than in the
presence of SDS (18%). The synergistic effect when both urea and SDS were used
in the latex deproteinisation attributed to the higher protein removal efficacy
(55%). Higher zeta potential value was observed when only SDS was used,
suggesting higher colloidal stability. Environmental Scanning Electron
Microscopy (ESEM) revealed that without SDS, the use of urea single-handedly in
the deproteinisation process promoted aggregation of latex particles, possibly due
to the dismissal of latex proteins which helped to stabilise latex colloidal.
Thus, it is most likely that urea serves as a protein unfolding agent during
latex deproteinisation process, while SDS functions as a latex stabiliser with
no significant effects on latex proteins discharge.
Keywords: urea, sodium dodecyl sulphate,
deproteinisation, zeta potential, environmental scanning electron microscopy
Abstrak
Kertas kerja ini menghuraikan kesan bahan-bahan
pengubah sifat protein iaitu urea dan natrium dodekil sulfat (NDS) dalam penyahprotein
lateks getah asli tinggi ammonia (HA-NRL). Ia telah menunjukkan bahawa protein lateks
lebih banyak dikurangkan dengan kehadiran urea sahaja (48%) berbanding dengan
kehadiran NDS sahaja (18%). Keberkesanan penyingkiran protein yang lebih tinggi
(55%) mungkin telah disebabkan oleh kesan sinergi apabila kedua-dua urea dan
NDS digunakan di dalam penyahprotein lateks. Nilai keupayaan zeta yang tinggi
diperhatikan apabila hanya NDS digunakan, menunjukkan kestabilan koloid yang
lebih tinggi. Pengimbas Persekitaran Mikroskopi Elektron (ESEM) menunjukkan
bahawa tanpa NDS, penggunaan hanya urea dalam proses penyahprotein menyumbang
kepada kesan pengagregatan zarah lateks, kemungkinan disebabkan oleh
penyingkiran protein lateks yang membantu dalam kestabilan koloid lateks. Oleh
yang demikian, besar kemungkinan fungsi utama urea semasa proses penyahprotein
lateks adalah sebagai ejen pembuka protein manakala NDS berfungsi sebagai
penstabil lateks tanpa kesan ketara pada penyingkiran protein lateks.
Kata kunci: urea, natrium dodekil sulfat, penyahprotein,
keupayaan zeta, pengimbas persekitaran mikroskopi elektron
References
1.
Hasma
H. and Subramaniam A. (1986). Composition of lipids in latex of Hevea
brasiliensis clone RRIM 501, Journal
Natural Rubber Research, 1(1):30 – 40.
2.
Aprem
A. S. and Pal S. N. (2002). Latex allergy and recent developments in
deproteinisation of natural rubber latex Journal
of Rubber Research, 5(2): 94 – 134.
3.
Sansatsadeekul,
J., Sakdapipanich, J. and Rojruthai, P. (2011). Characterization of associated
proteins and phospholipids in natural rubber latex. Journal of Bioscience and Bioengineering, 111(6): 628 – 634.
4.
Ma'zam
Md Said, Ng, K. P., Hasma, H., Mok, K. L., Asrul, M., Lai, P. P. and Saadiah,
S. (2004). Low protein natural rubber lattices. Journal of Rubber Research, 7(1): 30 – 55.
5.
Amnuaypornsri,
S., Sakdapipanich, J., Toki, S., Hsiao, B. S., Ichikawa, N. and Tanaka, Y.
(2008). Strain-induced crystallization of natural rubber: effect of proteins
and phospholipids. Rubber Chemistry and
Technology, 81(5): 753 – 766.
6.
Nor-Hidayaty,
K., Shamsul, K., Asrul, M. and Ahmad-Nazir, K. (2011). Comparisons of some
properties of deproteinised natural rubber vulcanisates and observations on
dynamic load analysis. Journal of Rubber
Research, 14(3): 129 – 138.
7.
Othman,
A. and Hasma, H. (1988). Influence of Hevea proteins and amino-acids on
properties of natural rubber, Proceedings
International Rubber Technology Conference: 166 – 177.
8.
Burfield,
D. R. (1986). Storage hardening of natural rubber: An examination of current
mechanistic proposals. Journal of Natural
Rubber Research, 1(3): 202 – 208.
9.
Sakdapipanich,
J. T. (2007). Structural characterization of natural rubber based on recent
evidence from selective enzymatic treatments. Journal of Bioscience and Bioengineering, 103(4): 287 – 292.
10.
Sakdapipanich,
J. T. and Rojruthai, P. (2012). Molecular structure of natural rubber and its
characteristics based on recent evidence. InTech publisher: pp. 159 – 172.
11.
Creighton,
T. E. (1995). Protein folding: An
unfolding story. Current Biology, 5(4):353-356
12.
Creighton,
T. E. (1979). Electrophoretic analysis of the unfolding of proteins by urea. Journal of Molecular Biology, 129: 235 –
264.
13.
Yamamoto,
Y., Kawahara, S., Chaikumpollert, O. and Nghia, P. T. (2013). Protein- free
natural rubber, latex thereof, and method for manufacturing said rubber and US Patent 8476348 B2
14.
Kawahara, S., klinklai, W., Kuroda, H. and Isono, Y. (2004).
Removal of proteins from natural rubber with urea. Polymer Advance Technology, 15:181 – 184.
15.
Rossky,
P. J. (2008). Protein denaturation by urea: Slash and bond. PNAS, 105(44): 16825 – 16826.
16.
Canchi,
D. R., Paschek, D. and García, A. E. (2010). Equilibrium study of protein
denaturation by urea. Journal of the
American Chemical Society, 132(7): 2338 – 2344.
17.
Bennion,
B. J. and Daggett, V. (2003). The molecular basis for the chemical denaturation
of proteins by urea. PNAS, 100 (9): 5142
– 5147.
18.
Ruiz,
C. C. (1999). Micelle formation and microenvironmental properties of sodium
dodecyl sulphate in aqueous urea solution Colloids
and Surfaces A: Physicochemical and Engineering Aspects, 147: 349 – 357.
19.
Otzen,
D. E. (2002). Protein unfolding in detergents: Effect of micelle structure,
ionic strength, pH, and temperature. Biophysical
Journal, 83: 2219 – 2230.
20. Kemp, A. R. and Straitiff, W. G. (1940). Hevea Latex:
Effect of proteins and electrolytes on colloidal behavior. Rubber Chemistry and
Technology, 13(4): 705 – 721.
21.
Chen,
S. F. (1981). Adsorption of sodium dodecyl
sulfate on natural rubber latex particles and determination of specific surface
area of the particles. Rubber Chemistry
and Technology, 54(1): 124 – 133.
22.
Jacso,
T., Bardiaux, B., Broecker, J., Fiedler, S., Baerwinkel, T., Mainz, A., Fink,
U., Vargas, C., Oschkinat, H., Keller, S. and Reif, B. (2013). The mechanism of
denaturation and the unfolded state of the α-helical membrane-associated
protein Mistic. Journal of the American
Chemical Society, 135(50): 18884 – 18891.
23.
Junoi, S.,
Chisti, Y. and Hansupalak, N. (2015). Optimal conditions for deproteinizing
natural rubber using
immobilized alkaline protease Journal of Chemical Technology and Biotechnology, 90: 185 – 193.
24.
Wei,
L. K., Ing, W. K., Badri, K. H. and Ban, W. C. (2013). Formation of protein
complex with the aid of polyethylene glycol for deproteinized natural rubber
latex AIP Conference Proceedings 1571:
871