A Biochemical Study of α-Amylase Activity in Saliva of Some Libyan Cigarette Smokers

Authors

  • Khaled S. Al salhen Departmentof Chemistry Faculty of Science, Omar Al-Mukhater University, El-Beida, Libya
  • Omalsaad E. I. Omar Biochemistry Department, Faculty of Medicine, El-Beida, Libya
  • Latefa A. Aljradmi Departmentof Chemistry Faculty of Science, Omar Al-Mukhater University, El-Beida, Libya

DOI:

https://doi.org/10.54172/mjsc.v35i3.295

Keywords:

Cigarette Smokers, Salivary α-Amylase, Kinetic Parameters, Optimum Conditions

Abstract

Tobacco consumption alters many biological parameters, including α-amylase activity. This study reports the effect of cigarette smoking on salivary α-amylase activities of some male heavy smokers (100) in apparent good health compared with (40) male non-smokers as control. The salivary α-amylase activity was assayed using the standard colorimetric method. The α-amylase enzyme was characterized from the saliva samples collected from healthy adult smokers and non-smokers (control) to determine the effects of temperature, pH, and substrate concentration on the kinetic parameters of the enzyme. The analysis of the saliva samples showed that there were significant increases (P<0.05) in the α-amylase activity values in the saliva of cigarette smokers when compared with non-smokers at optimum conditions (2.74±0.37 nmol/min/mg-protein and 2.01±0.16 nmol/min/mg-protein, respectively). The Michaelis constant (Km) values of 0.5±0.02 mM and 1.12±0.08 mM observed for non-smokers and smokers were obtained from the double reciprocal plot of initial velocity (1/V) and substrate concentration (1/[S]). The maximum activities obtained at an optimum temperature of 37ºC, and an apparent pH of 7.0 for both subjects were 31.25±8.24 nmol/min/mg protein and 18.10±4.06 nmol/min/mg protein for non-smokers and smokers respectively. Measurements of salivary α-amylase activity could be useful in the early detection and diagnosis of parotitis. Subsequent studies are required to specify the mechanisms responsible for such a risk.

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...

References

Abd El-Samad, M., & Hanafi, H.A. (2017). Analysis of toxic heavy metals in ciga-rettes by instrumental neutron activation analysis. Journal of Taibah University for Science,11,822-829. DOI: https://doi.org/10.1016/j.jtusci.2017.01.007

Aysun, A. , Ozge, D., Ebru, H. B, & Yuksel, B. (2009). Evaluation of the relationship between passive smoking and salivary electrolytes, protein, secretory IgA, sialic acid and amylase in young children. Archives of Oral Biology, 54 (5), 457-463. DOI: https://doi.org/10.1016/j.archoralbio.2009.01.017

Bodade, G.R., Chandarahas, N. K., & Arfeen, S.A. (2010). Optimization of culture conditions for glucose oxidase produc-tion by a Penicillium chrysogenum SRT 19 strain. Engineering and Life Science, 10(1), 35-39. DOI: https://doi.org/10.1002/elsc.200900030

Bradford, M. M. (1976). A rapid and sensitive method for quantitation of microogram qualities of protein utilizing the principle of protein dye binding, Analytical Biochemistry, 7(72), 248-254. DOI: https://doi.org/10.1016/0003-2697(76)90527-3

Callegari, C., & Lami, F., (1984). Cigarette smoking and salivary amylase activity. Gut, 25, 909. DOI: https://doi.org/10.1136/gut.25.8.909

Caruso, R.V., O'Connor, R.J., Stephens, W.E., Cummings, K.M., & Fong, G.T. (2014). Toxic metal concentrations in cigarettes obtained from U.S. smokers in 2009: results from the International Tobacco Control (ITC) United States survey co-hort. International Journal of Environ-mental Research and Public Health, 11, 202-217. DOI: https://doi.org/10.3390/ijerph110100202

Da Costa, E., & Sylva, V.L. (2005). Health consequences of the tobacco epidemic in West African French-speaking countries and current tobacco control. Promot Educ, 4(7), 54.

Enemchukwu, B.N., Ubaoji, K.I., Igwilo, I.O., & Udedi, S.C. (2013). Effects of Tem-perature, pH and substrate concentration on the kinetics of salivary alpha-amylase activity among cigarette smokers in Awka, Anambra State, Nigeria, The Bioscientist Journal, 1(1),108-113.

Enemchukwu, B.N., Emeh, K.I., & Ubaoji, I.O. (2011). Salivary α--amylase activity among cigarette smokers in Awka, Anambra state, Nigeria, Biochemistry An Indian Journal, 5(5), 306-309.

Gomina, M., Badirou, L., & Akpona, S. A. (2013). Activity of Serum and Salivary α-Amylase in Habitual Adult Tobacco Consumers. Biochem Anal Biochem, 2,140. DOI: https://doi.org/10.4172/2161-1009.1000140

Hadrich, F., Bouallagui, Z., Junkyu, H., Isoda, H., & Sayadi, S. (2015). The α-Glucosidase and α-amylase enzyme in-hibitory of hydroxtyrosol and oleuropein, The Journal of Oleo Science, 64(8), 835-843. DOI: https://doi.org/10.5650/jos.ess15026

Heberd, A., Razali, A., Mahalingam, S.R., Tiong, C. S., & Arshad, K. (2015). As-sessment of Salivary Biomarkers Asso-ciated with Occupational Stress. Inter-national Academic Research Journal of Social Science, 1(2),107-111.

Kennedy, J.F., Melo, E.H.M., & Jumel, K. (1989). Immobilized biosystems in re-search and industry. Biotechnology and Genetic Engineering Reviews, 7(1), 297-314. DOI: https://doi.org/10.1080/02648725.1989.10647863

Kivelä, J., Parkkila, S., Metteri, J., Parkkila, A., K., Toivanen, A., & Rajaniemi, H. (1997). Salivary carbonic anhydrase VI concentration and its relation to basic characteristics of saliva in young men. Acta Physiol Scand, 161(2), 221-225. DOI: https://doi.org/10.1046/j.1365-201X.1997.00217.x

Levitzki, A., & Steer, M. L. (1974). The allo-steric activation of mammalian alpha-amylase by chloride. European Journal of Biochemistry, 41(1),171-180. DOI: https://doi.org/10.1111/j.1432-1033.1974.tb03257.x

Maier, H., Jarczyk, L., Scherer, G., & Born, I. A. (1991). Effects of acute nicotine ad-ministration on the function of the human parotid gland. Laryngo-Rhino-Otologie, 70(1),24-26. DOI: https://doi.org/10.1055/s-2007-997978

Miller, G. L. (1959). Use of dinitrosalicylic acid reagent for determination of reducing sugars. Analytical Chemistry, 31(3), 426-428. DOI: https://doi.org/10.1021/ac60147a030

Mohammed. B. J., AL-Thwani, A.N., & Kannan R. (2016). Demographic and genetic study for a sample of Iraqi smokers. Cancer Biology, 6(4),16-27.

Myers, D.K., Lawlor, D.T., & Attfield, P.V. (1997). Influence of invertase activity and glycerol synthesis and retention on fermentation of media with a high sugar concentration by Saccharomyces cere-visiae. Applied and Environmental Mi-crobiology, 63(1),145-150. PMCID: PMC168312. DOI: https://doi.org/10.1128/aem.63.1.145-150.1997

Nagaya, T., Okuno, M. (1993). No effect of smoking on drinking habits on salivary amylase. Toxicology Letters, 66 (3),257-261. DOI: https://doi.org/10.1016/0378-4274(93)90006-J

Nagler, R., Lischinsky, S., Diamond, E., Drigues, N., Klein, I., & Reznick, A.Z. (2000). Effect of cigarette smoke on sal-ivary proteins and enzyme activities. Archives of Biochemistry and Biophys-ics, 379(2), 229-236. DOI: https://doi.org/10.1006/abbi.2000.1877

Nasrallah, S. M., & Martin, D. M. (1983). Se-rum isoamylase as a test for pancreatic insufficiency. Gut, 24(2),161-4. DOI: https://doi.org/10.1136/gut.24.2.161

Nater, U.M., Rohleder, N., Schlotz, W., Ehlert, U., & Kirschbaum, C. (2007). Determi-nants of the diurnal course of salivary alpha-amylase. Psychoneuroendocri-nology, 32 (4), 392-401. DOI: https://doi.org/10.1016/j.psyneuen.2007.02.007

Onyesom, I., Osioma, E., Ifie, E.J., & Oweh O.T. (2012). Activities of alpha amylase in serum and saliva of some Nigerian cigarette smokers. Advances in Life Sci-ences, 2(1), 28-30. DOI: https://doi.org/10.5923/j.als.20120201.04

Rudeekulthamrong, P., Kaulpiboon, J. (2012). Kinetic inhibition of human salivary al-pha-amylase by a novel cellobiose-containing tetrasaccharide. Journal of the Medical Association of Thailand, 95 Suppl 1,S102-8. PMID: 23964451.

Tatah, V.S., Otitoju, O. (2015). Characterization of immobilized post-carbohydrate meal salivary α-amylase. African Journal of Biotechnology, 14(31), 2472. DOI: https://doi.org/10.5897/AJB2015.14510

Weiner, D., Khankin, E. V., Levy, Y., & Rez-nick, A. Z. (2009). Effects of cigarette smoke borne reactive nitrogen species on salivary alpha-amylase activity and protein modifications. J Physiol Phar-macol, 60 Suppl 5, 127-132. PMID: 20134053.

WHO (World Health Organization) Report on the Global Tobacco Epidemic. (2017). Tobacco Free Initiative (TFI), Switzer-land, Geneva.

Yi, T.C., & Moochhala, S. (2013). Mini-Review Article - Current opinion on salivary bi-omarkers as a measurement for stress and fatigue. The Open Biomarkers Journal, 6,9-14. DOI: https://doi.org/10.2174/1875318301306010009

Yoon, S.H., & Robyt, J.F. (2003). Study of the inhibition of four alpha amylases by acarbose and its 4IV-alphamaltohexaosyl and 4IV- alpha-maltododecaosyl analogues. Carbohydrate Research, 338(19), 1969-1980. DOI: https://doi.org/10.1016/S0008-6215(03)00293-3

Zappacosta, B., Persichilli, S., Mordente, A., Minucci, A., Lazzaro, D., Meucci, E., & Giardina, B. (2002). Inhibition of sali-vary enzymes by cigarette smoke and the protective role of glutathione. Hu-man and Experimental Toxicology, 21(1),7-11. DOI: https://doi.org/10.1191/0960327102ht202oa

Downloads

Published

2020-09-30

How to Cite

Al salhen, K. S. ., Omar, O. E. I. ., & Aljradmi, L. A. . (2020). A Biochemical Study of α-Amylase Activity in Saliva of Some Libyan Cigarette Smokers. Al-Mukhtar Journal of Sciences, 35(3), 195–204. https://doi.org/10.54172/mjsc.v35i3.295

Issue

Section

Research Articles

Categories

Most read articles by the same author(s)

Obs.: This plugin requires at least one statistics/report plugin to be enabled. If your statistics plugins provide more than one metric then please also select a main metric on the admin's site settings page and/or on the journal manager's settings pages.