Curious Cases of the Enzymes / Neobiča Istorija Enzima

Open access


Life as we know it heavily relies on biological catalysis, in fact, in a very nonromantic version of it, life could be considered as a series of chemical reactions, regulated by the guarding principles of thermodynamics. In ancient times, a beating heart was a good sign of vitality, however, to me, it is actually the presence of active enzymes that counts… Though we do not usually pay attention, the history of enzymology is as old as humanity itself, and dates back to the ancient times. This paper is dedicated to these early moments of this remarkable science that touched our lives in the past and will make life a lot more efficient for humanity in the future. There was almost always a delicate, fundamentally essential relationship between mankind and the enzymes. Challenged by a very alien and hostile Nature full of predators, prehistoric men soon discovered the medicinal properties of the plants, through trial and error. In fact, they accidently discovered the enzyme inhibitors and thus, in crude terms, kindled a sparkling area of research. These plant-derivatives that acted as enzyme inhibitors helped prehistoric men in their pursuit of survival and protection from predators; in hunting and fishing… Later in history, while the underlying purposes of survival and increasing the quality of life stayed intact, the ways and means of enzymology experienced a massive transformation, as the ‘trial and error’ methodology of the ancients is now replaced with rational scientific theories.

1. Kleczkowski M, Garncarz M. The role of metal ions in biological oxidation - the past and the present. Pol J Vet Sci 2012; 15: 165-73.

2. Setlow P. Summer meeting 2013-when the sleepers wake: the germination of spores of Bacillus species. J Appl Microbiol 2013; 115: 1251-68.

3. Büttner J. Evolution of Clinical Enzymology. J. Clin. Chcm Clin Biochem 1981; 19: 529-38.

4. Robertson JB. The Early History of Catalysis. Platinum Metals Rev 1975; 19: 64-9.

5. D'Alessandro A, Giardina B, Gevi F, Timperio AM, Zolla L. Clinical metabolomics: the next stage of clinical biochemistry. Blood Transfus 2012; 10: 19-24.

6. Kohler RE. The Enzyme theory and the origin of biochemistry. Chic J 1973; 64: 181-96.

7. Jovičić S, Ignjatović, S, Majkić-Singh N. Biochemistry and metabolism of vitamin D. J Med Biochem 2012; 31: 309-15.

8. Lazarević D, Ðorđević VV, Ćosić V, Vlahović P, Toŝić- Golubović S, Ristić T, et al. Increased lymphocyte caspase-3 activity in patients with schizophrenia. J Med Biochem 2011; 30: 55-61.

9. Karaman K, Tirnaksiz MB, Ulusu N, Dincer N, Sener B, Gulmez D, et al. Effects of dexamethasone on ischemia reperfusion injury following pringle maneuver. Hepatogastroenterology 2011; 58: 465-71.

10. Tandogan B, Guvenc A, Calis I, Ulusu NN. In vitro effects of isoorientin, forsythoside B, and verbascoside on bovine kidney cortex glutathione reductase. Int Chem Kinet 2013; 45: 574-9.

11. Tandogan B, Sengezer C, Ulusu NN. In vitro effects of imatinib on glucose-6-phosphate dehydrogenase and glutathione reductase. Folia Biol (Praha) 2011; 57: 57-64.

12. Tandogan B, Kuruüzüm-Uz A, Sengezer C, Güvenalp Z, Demirezer LÖ, Ulusu NN. In vitro effects of rosmarinic acid on glutathione reductase and glucose 6-phosphate dehydrogenase. Pharm Biol 2011; 49: 587-94.

13. Tandogan B, Ulusu NN. Comparative in vitro effects of some metal ions on bovine kidney cortex glutathione reductase. Prep Biochem Biotechnol 2010; 40: 405-11.

14. Tandogan B, Ulusu NN. A comparative study with colchicine on glutathione reductase. Protein J 2010; 29: 380-5.

15. Tandogan B, Ulusu NN. Inhibition of purified bovine liver glutathione reductase with some metal ions. J Enzyme Inhib Med Chem 2010; 25: 68-73.

16. Khare Sagar D, Fleishman Sarel J. Emerging themes in the computational design of novel enzymes and proteinprotein interfaces. FEBS Lett 2013; 587: 1147-54.

17. Gerlt JA, Allen KN, Almo SC, Armstrong RN, Babbitt PC, Cronan JE, et al. The Enzyme Function Initiative. Biochem 2011; 22: 9950-62.

18. Roncada P, Piras C, Soggiu A, Turk R, Urbani A, Bonizzi L. Farm animal milk proteomics. J Proteomics 2012; 19: 4259-74.

19. He H, Qin Y, Chen G, Li N, Liang Z. Two-step purification of a novel b-glucosidase with high transglycosylation activity and another hypothetical b-glucosidase in Aspergillus oryzae HML366 and enzymatic characterization. Appl Biochem Biotechnol 2013; 169: 870-84.

20. Natarajan P, Ray KK, Cannon CP. High-density lipoprotein and coronary heart disease: current and future therapies. J Am Coll Cardiol 2010; 30: 1283-99.

21. Reay Tannahill, editors, Food in history. (1973) New York Three Rivers Press p. 16, 68, 69.

22. Mithen SJ, Finlayson B, Smith S, Jenkins E, Najjar M, Maričević D. Göbekli tepe: An 11 600 year-old communal structure from the Neolithic of southern Jordan. Antiquity 2011; 85: 350-64.

23. Fox PF, editors, Cheese: An overview. Cheese: Chemistry, Physics and Microbiology, 2ed. Chapman and Hall, London (1993), pp. 1-36.

24. Salimei E, Fantuz F. Equid milk for human consumption. Int dairy J 2012; 24: 130-42.

25. Rosell JM. Yoghourt and kefir in their relation to health and therapeutics. Can Med Assoc J 1932; 26: 341-5.

26. Copeland Robert A, editor. Enzymes, A. Practical Introduction to Structure, Mechanism, and Data Analysis. John Wiley & Sons, Inc., 2000: 2-10.

27. McGovern PE, Zhang J, Tang J, Zhang Z, Hall GR, Moreau RA, et al. Fermented beverages of pre- and proto-historic China. Proc Natl Acad Sci USA 2004; 21: 17593-8.

28. Bamforth CW, editors, Food, Fermentation and Microorganisms, Blackwell Science: Oxford, UK, 2005: 143-153.

29. Kawakish S, Namiki K, Nishimur H, Namiki M. Effects of .gamma.-irradiation on the enzyme relating to the development of characteristic odor of onions. J Agric Food Chem 1971; 19: 166-9.

30. Xu Y, Zhang Z, Wang M, Wei J, Chen H, Gao Z, et al. Identification of genes related to agarwood formation: transcriptome analysis of healthy and wounded tissues of Aquilaria sinensis. BMC Genomics 2013; 8: 1-16.

31. Li Q, Korzan WJ, Ferrero DM, Chang RB, Roy DS, Buchi M, et al. Synchronous evolution of an odor biosynthesis pathway and behavioral response. Curr Biol 2013; 7: 11-20.

32. Fischer-Tenhagen C, Tenhagen BA, Heuwieser W. Short communication: Ability of dogs to detect cows in estrus from sniffing saliva samples. J Dairy Sci 2013; 96: 1081-4.

33. Wells DL. Dogs as a diagnostic tool for ill health in humans. Altern Ther Health Med 2012; 18: 12-7.

34. Agostinucci W, Cardoni AA, Rosenberg P. Effect of papain on bee venom toxicity. Toxicon 1981; 19: 851-5.

35. Ross Jr EV, Badame AJ, Dale SE. Meat tenderizer in the acute treatment of imported fire ant stings. J Am Acad Dermatol 1987; 16: 1189-92.

36. Baker EL, Baker WL, Cloney DJ. Resolution of a phytobezoar with Aldoph's Meat Tenderizer. Pharmacotherapy 2007; 27: 299-302.

37. Surico N, Codecà C, Caccia S. Medical humanities in gynecology and obstetrics. Minerva Ginecol 2012; 64: 447-53.

38. Philippe G, Angenot L, Tits M, Frédérich M. About the toxicity of some Strychnos species and their alkaloids. Toxicon 2004; 15: 405-16.

39. Norman G. Bisset War and hunting poisons of the New World. Part 1. Notes on the early history of curare. J Ethnopharmacol 1992; 36: 1-26.

40. Bliss CL, Novy FG. Action of formaldehyde on enzymes and on certain pboteids. J Exp Med 1899; 1: 47-80.

41. Cao L. Immobilised enzymes: science or art? Current Opinion in Chemical Biology 2005; 9: 217-26.

42. Pelkonen O, Abass K, Wiesner J. Thujone and thujonecontaining herbal medicinal and botanical products: Toxicological assessment. Regul Toxicol Pharmacol 2013; 65: 100-7.

43. Abass K, Reponen P, Mattila S, Pelkonen O. Metabolism of a-thujone in human hepatic preparations in vitro. Xenobiotica 2011; 41: 101-11.

44. Holstege CP, Baylor MR, Rusyniak DE. Absinthe: return of the Green Fairy. Semin Neurol 2002; 22: 89-93.

45. Bonkovsky HL, Cable EE, Cable JW, Donohue SE, White EC, Greene YJ, et al. Porphyrogenic properties of the terpenes camphor, pinene, and thujone (with a note on historic implications for absinthe and the illness of Vincent van Gogh). Biochem Pharmacol 1992; 43: 2359-68.

46. Jones PJ. Cleopatra's cocktail. Class World 2010; 103: 207-20.

47. Schmaltz F. Neurosciences and research on chemical weapons of mass destruction in Nazi Germany. J Hist Neurosci 2006; 15: 186-209.

48. Jokanović M, Prostran M. Pyridinium oximes as cholin - esterase reactivators. Structure-activity relationship and efficacy in the treatment of poisoning with organophosphorus compounds. Curr Med Chem 2009; 16: 2177-88.

49. Kuca K, Juna D, Musilek K. Structural requirements of acetylcholinesterase reactivators. Mini Rev Med Chem 2006; 6: 269-77.

50. Kitada M, Kume S, Takeda-Watanabe A, Kanasaki K, Koya D. Sirtuins and renal diseases: relationship with aging and diabetic nephropathy. Clin Sci (Lond) 2013; 124: 153-64.

51. Farris PK. Innovative cosmeceuticals: sirtuin activators and anti-glycation compounds. Semin Cutan Med Surg 2011; 30: 163-6.

52. Lebeda FJ, Cer RZ, Mudunuri U, Stephens R, Singh BR, Adler M. The zinc-dependent protease activity of the botulinum neurotoxins. Toxins (Basel) 2010; 2: 978-97.

53. Cartee TV, Monheit GD. An overview of botulinum toxins: past, present, and future. Clin Plast Surg 2011; 38: 409-26.

54. Dodick DW, Diener HC, Degryse RE, Turkel CC, Lipton RB, Silberstein SD. OnabotulinumtoxinA for chronic migraine: efficacy, safety, and tolerability in patients who received all five treatment cycles in the PREEMPT clinical program. Acta Neurol Scand 2014; 129: 61-70.

55. Tomatsu M, Shimakage A, Shinbo M, Yamada S, Taka - hashi S. Novel angiotensin I-converting enzyme inhibitory peptides derived from soya milk. Food Chem 2013; 15: 612-6.

56. Goyal N. Novel approaches for the identification of inhibitors of leishmanial dipeptidylcarboxypeptidase. Expert Opin Drug Discov 2013; 8: 1127-34.

57. Tanaka Y, Nanamiya H, Yano K, Kakugawa K, Kawamura F, Ochi K. rRNA (rrn) operon-engineered Bacillus subtilis as a feasible test organism for antibiotic discovery. Antimicrob Agents Chemother 2013; 57: 1948-51.

58. Clardy J, Fischbach M, Currie C. The natural history of antibiotics. Curr Biol 2009; 19: 437-41.

59. Jacomella V, Corti N, Husmann M. Novel anticoagulants in the therapy of peripheral arterial and coronary artery disease. Curr Opin Pharmacol 2013; 13: 294-300.

60. Leung E, Hanna MY, Tehami N, Francombe J. Isolated unilateral tongue oedema: the adverse effect of angiotensin converting enzyme inhibitors. Curr Drug Saf 2012; 1: 382-3.

61. Kujawa A, Szponar J, Szponar E, Zapalska-Pozarowska K, Kostek H. The harmfulness of drugs and slimming substances - a toxicologist's point of view. Przegl Lek 2012; 69: 548-51.

62. Patrono C, Rocca B. Aspirin and other COX-1 inhibitors. Handb Exp Pharmacol 2012; 210: 137-64.

63. Aggarwal M, McKenna R. Update on carbonic anhydrase inhibitors: a patent review (2008-2011). Expert Opin Ther Pat 2012; 22: 903-15.

64. Pavlović S, Zukić B, Stojiljković Petrović M. Molecular genetic markers as a basis for personalized medicine. J Med Biochem 2014; 33: 8-21.

65. Sanders MA, Brahemi G, Nangia-Makker P, Balan V, Morelli M, Kothayer H, et al. Novel inhibitors of Rad Ubiquitin Conjugating Enzyme: Design, synthesis, identification and functional characterization. Mol Cancer Ther 2013; 12: 373-83.

66. Brophy JM, Costa V. Statin wars following coronary revascularization - evidence-based clinical practice? Can J Cardiol 2006; 22: 54-8.

67. Tuncay E, Seymen AA, Tanriverdi E, Yaras N, Tandogan B, Ulusu NN, et al. Gender related differential effects of Omega-3E treatment on diabetes-induced left ventricular dysfunction. Mol Cell Biochem 2007; 304: 255-63.

68. Pekiner B, Ulusu NN, Das-Evcimen N, Sahilli M, Aktan F, Stefek M, et al. In vivo treatment with stobadine prevents lipid peroxidation, protein glycation and calcium overload but does not ameliorate Ca2+ -ATPase activity in heart and liver of streptozotocin-diabetic rats: comparison with vitamin E. Biochim Biophys Acta 2002; 9: 71-8.

69. Ulusu NN, Ercil D, Sakar MK, Tezcan EF. Abietic acid inhibits lipoxygenase activity. Phytother Res 2002; 16: 88-90.

70. Guz G, Demirogullari B, Ulusu NN, Dogu C, Demirtola A, Kavutcu M, et al. Stobadine protects rat kidney against ischaemia/reperfusion injury. Clin Exp Pharmacol Physiol 2007; 34: 210-6.

71. Ulusu NN, Sahilli M, Avci A, Canbolat O, Ozansoy G, Ari N, et al. Pentose phosphate pathway, glutathionedependent enzymes and antioxidant defense during oxidative stress in diabetic rodent brain and peripheral organs: effects of stobadine and vitamin E. Neurochem Res 2003; 28: 815-23.

72. Tandogan B, Guvenc A, Çalıs¸ I, Ulusu NN. In vitro effects of compounds isolated from Sideritis brevibracteata on bovine kidney cortex glutathione reductase. Acta Bio - chim Pol 2011; 58: 471-5.

73. Schechter I. Mapping of the active site of proteases in the 1960s and rational design of inhibitors/drugs in the 1990s. Curr Protein Pept Sci 2005; 6: 501-12.

74. Sohier JS, Laurent C, Chevigné A, Pardon E, Srinivasan V, Wernery U, Steyaert J, Galleni M. Allosteric inhibition of VIM metallo-lactamases by a camelid nanobody. Biochem J 2013; 15: 477-86.

75. Ulusu NN, Tandogan B. Purification and kinetics of sheep kidney cortex glucose-6-phosphate dehydrogenase. Comp Biochem Physiol B Biochem Mol Biol 2006; 143: 249-55.

76. Ulusu NN, Tandogan B, Tezcan FE. Kinetic properties of glucose-6-phosphate dehydrogenase from lamb kidney cortex. Biochimie 2005; 87: 187-90.

77. Ulusu NN, Kus MS, Acan NL, Tezcan EF. A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens. Int J Biochem Cell Biol 1999; 31: 787-96.

78. Ulusu NN, Tandogan B. Purification and kinetic properties of glutathione reductase from bovine liver. Mol Cell Biochem 2007; 303: 45-51.

79. Tandogan B, Ulusu NN. Purification and kinetics of bovine kidney cortex glutathione reductase. Protein Pept Lett 2010; 17: 667-74.

80. Bradshaw RA, Hancock CC, Krege N. 100 years of chemistry of life. 1 ed. Columbia, Maryland 1999, 3pp.

81. Copeland RA. A Brief History of Enzymology. In Enzymes- A Practical Introduction to Structure. New York, Wiley- VCH, Inc. 2000: 1-11.

82. Tipton K, Boyce S. The history of enzyme nomenclature system. Bioinformatics 2000; 16: 34-40.

83. Ben Kilani Cö Batis H, Chastrette M. Development of the ideas concerning catalysis at the beginning of the XIXth century. Actual Chim 2001; 7-8: 44-50.

84. Schadewaldt H. Nutrition and individual defense - historical considerations. Zentralbl Hyg Umweltmed 1991; 191: 302-6.

85. Pavy FW, Siau RL. An experimental enquiry upon glyco - lysis in drawn blood. J Physiol 1902; 31: 451-6.

86. Stirling W. On the Ferments or Enzymes of the Digestive Tract in Fishes. J Anat Physiol 1884; 18: 426-35.

87. Warren G. A vital assay. Nat Rev Mol Cell Biol 2012; 13: 754.

88. Madeira VM. Overview of mitochondrial bioenergetics. Methods Mol Biol 2012; 810: 1-6.

89. Kohler RE. The reception of Eduard Buchner’s discovery of cell-free fermentation 1972, 5: 327-53.

90. Henri V. General theory of the action of some glycoside hydrolases. CR Acad Sci Paris 1902; 135: 919.

91. Harden A, Macfadyen A. Enzymes in tumour. The Lancet 1903; 162: 224-5.

92. Michaelis L, Menten ML, Johnson KA, Goody RS. The original Michaelis constant: translation of the 1913 Michaelis-Menten paper. Biochem 2011; 4: 8264-9.

93. Harden A, Norris RV. The enzymes of washed zymin and dried yeast (Lebedeff). II. Reductase. Biochem J 1914; 8: 100-6.

94. Hartridge H. An improved spectrophotometer. J Physiol 1915; 24: 101-13.

95. Sherman HC, Thomas AW, Hinck CF. Studies on amylases. VIII. The influence of certain acids and salts upon the activity of malt amylase. JACS 1915; 37: 623-43.

96. Mack E, Villars DS. Synthesis of urea with the enzyme urease. JACS 1923; 45: 501-5.

97. Bastedo WA. The use and utility of digestive enzymes in therapeutics: A summary of the replies to a questionnaire submitted to the members of the American gastroenterological association. JAMA 1925; 85: 743-4.

98. Sumner JB. The isolation and crystallization of the enzyme urease: Preliminary paper. J Biol Chem 1926; 69: 435-41.

99. Madeira VM. Overview of mitochondrial bioenergetics. Methods Mol Biol 2012; 810: 1-6.

100. Roskelley RC, Mayer N, Horwitt BN, Salter WT. Studies in cancer. VII. Enzyme deficiency in human and experimental cancer. J Clin Invest 1943; 22: 743-51.

101. Young A. Effects on plasma glucose and lactate. Adv Pharmacol 2005; 52: 193-208.

102. Marcus M. A contribution to the history of favismo. Harefuah 1948; 15: 24

103. Thompson A. The c-terminal residue of lysozyme. Nature 1952; 169: 495-6.

104. Thompson EO. The N-terminal sequence of carboxypeptidase. Biochim Biophys Acta 1953; 10: 633-4.

105. Marks PA. A newer pathway of carbohydrate metabolism; the pentose phosphate pathway. Diabetes 1956; 5: 276-83.

106. Koshland DE, Jr. Enzyme flexibility and enzyme action. J Cell Comp Physiol 1959; 54: 245-58.

107. Wróblewski F, Ross C, Gregory K. Isoenzymes and myocardial infarction.N Engl J Med 1960; 15: 531-6.

108. Viswanatha T, Lawson WB, Witkop B. The action of Nbromosuccinimide on trypsinogen and its derivative. Biochimica et Biophysica Acta 1960; 40: 216-24.

109. Smyth DG, Stein WH, Moore S. On the sequence of residues 11 to 18 in bovine pancreatic ribonuclease. J Biol Chem 1962; 237: 1845-50.

110. Stanford Jr RH, Marsh RE, Corey RB. Structure of lysozyme: An x-ray investigation of lysozyme chloride crystals containing complex ions of niobium and tantalum: Three-dimensional fourier plot obtained from data extending to a minimum spacing of 5. Å.1962; 196: 1176-8.

111. Smyth DG, Stein WH, Moore S. The Sequence of Ami - no Acid Residues in Bovine Pancreatic Ribo nuclease: revisions and confirmations. J Biol Chem 1963; 238: 227-34.

112. Changeux JP. Allostery and the Monod-Wyman- Changeux model after 50 years. Annu Rev Biophys 2012; 41: 103-33.

113. Guilbault GG. Fluorometric system employing immobilized cholinesterase for assaying anticholinesterase compounds. Anal Chem 1965; 37: 1675-80.

114. Kiefer HC, Congdon WI, Scarpa IS, Klotz IM. Catalytic accelerations of 10-fold by an enzyme-like synthetic polymer. Proc Natl Acad Sci USA 1972; 69: 2155-9.

115. Brady RO. The lipid storage diseases: new concepts and control. Annals of Internal Medicine 1975; 82: 257-61.

116. Kinderlerer J, Ainsworth S, Gregory RB. Computer programs for use in enzyme kinetic studies. Biochem Soc Trans 1980; 8: 652-52.

117. Cech TR, Zaug AJ, Grabowski PJ. In vitro splicing of the ribosomal RNA precursor of Tetrahymena: involvement of a guanosine nucleotide in the excision of the intervening sequence. Cell 1981; 27: 487-96.

118. Vadgama P. Enzyme electrodes as practical biosensors. J Med Eng Technol 1981; 5: 293-8.

119. Pollack SJ, Jacobs JW, Schultz PG. Selective chemical catalysis by an antibody. 1986; 234: 1570-3.

120. Harley CB, Futcher AB, Greider CW. Telomeres shorten during ageing of human fibroblasts. Nature 1990; 345: 458-60.

121. Kay AC, Saven A, Garver P, Thurston DW, Rosenbloom BF, Beutler E. Enzyme replacement theraphy in type-I Gaucher disease. Trans Assoc Am Physicians 1991; 14: 258-64.

122. Breaker RR, Joyce GF. A DNA enzyme that cleaves RNA. Chem Biol 1994; 1: 223-9.

123. Changeux JP, Stuart ES. Conformational selection or induced fit? 50 years of debate resolved. F1000 Biol Rep 2011; 3: 19-24.

124. Gonzalez MJ, Miranda M, JR, Duconge J, Riordan NH, Ichim T, Quintero-Del-Rio AI, Ortiz N. The bio-energetic theory of carcinogenesis. Medical Hypotheses 2012; 79: 433-9.

125. Weller CE, Pilkerton ME, Chatterjee C. Chemical strategies to understand the language of ubiquitin signaling. Biopolymers 2014; 101: 144-55.

126. Kim JH, Nam DH, Park CB. Nanobiocatalytic assemblies for artificial photosynthesis. Current Opinion in Biotechnology 2014; 28: 1-9.

127. Breithaupt H. The hunt for living gold. The search for organisms in extreme environments yields useful enzymes for industry. EMBO reports 2001; 21: 968-71.

128. Wallerstein L. Enzymes in the fermentation industries JFI 1917; 183: 531-56.

129. Blagoveschenski AV, Sossiedov MP. On the changes of wheat proteins under the action of flour and yeast enzymes. Biochem J 1935; 29: 805-10.

130. Bommarius AS, Blum JK, Abrahamson MJ. Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst. Current Opinion in Chemical Biology 2011; 15: 194-200.

131. Smythe CV. Microbiological production of enzymes and their industrial applications 1951; 5: 126-144.

132. Demain AL, Phaff HJ. Cucumber curing, softening of cucumbers during curing. J Agr Food Chem 1957; 5: 60-4.

133. Göthe CJ, Westlin A, Sundquist S. Air-borne B. subtilis enzymes in the detergent industry. Internationales Archiv für Arbeitsmedizin 1972; 29: 201-8.

134. Shahani KM, Arnold RG, Kilara A, Dwivedi BK. Role of microbial enzymes in flavor development in foods. Biotechnol Bioeng 1976; 18: 891-907.

135. Miwa T. Saccharides from starch hydrolysis and their derivatives for foodstuffs. Yuki Gosei Kagaku Kyokaishi/J Synthetic Org Chem 1984; 42: 597-601.

136. Liu P, Tian GL, Ye YH. Progress in the Study on Peptide Synthesis Catalyzed by Immobilized Enzyme. Chem J Chinese U 2001; 22: 1347-8.

137. Mason P. Basic concepts in clinical testing. Pharm J 2004; 272: 384-6.

138. Liu XG, Ju XR, Mao XD, Zhang Z. Studies on enzymic extraction of essential oil from pine needles. Linchan Huaxue Yu Gongye/Chem Ind Forest Prod 25 (3), pp. 101-114, 2005.

139. Mlichová Z, Rosenberg M. Current trends of b-galactosidase application in food technology (Review). J Food Sci Nutr 2006; 45: 47-54.

140. Hsieh YHP, Ofori JA. Innovations in food technology for health. Asia Pac J of Clin Nut 2007; 16: 65-73.

141. Selimoğlu M, Karabiber H. Celiac disease: Prevention and treatment (Review) J Clin Gastroenterol 2010; 44: 4-8.

142. Sreedhar RP, Jhansi RD, Sulthana S. Amylases as a tool for industrial application: A review (Review). J Pure Appl Microbiol 2011; 5: 167-71.

143. Galonde N, Nott K, Debuigne A, Deleu M, Jerôme C, Paquot M, et al. Use of ionic liquids for biocatalytic synthesis of sugar derivatives (Review). J Chem Technol Biot 2012; 8: 451–71.

144. Hadden JA, French AD, Woods RJ. Unraveling cellulose microfibrils: A twisted tale. 2013; 99: 746–56.

145. Adelakun OE, Metcalfe D, Tshabalala P, Stafford B, Oni B. The effect of pectinase enzyme on some quality attributes of a Nigerian mango juice. Nutr Food Sci 2013; 43: 374–83.

146. Dettmer A, Dos APS, Gutterres M. Special review paper: Enzymes in the leather industry. J Am Leather Chem Assoc 2013; 108: 146–58.

147. Li Z, Gao Y, Nakanishi H, Gao X, Cai L. Biosynthesis of rare hexoses using microorganisms and related enzymes. Beilstein J Org Chem 2013; 12: 2434–45.

148. Khawla BJ, Sameh M, Imen G, Donyes F, Dhouha G, Raoudha EG, et al. Potato peel as feedstock for bioethanol production: A comparison of acidic and enzymatic hydrolysis. Ind Crop Prod 2014; 52: 144–9.

149. Tabita FR, Hanson TE, Satagopan S, Witte BH, Kreel NE. Phylogenetic and evolutionary relationships of RubisCO and the RubisCO-like proteins and the functional lessons provided by diverse molecular forms. Philos Trans R Soc Lond B Biol Sci 2008; 27: 2629–40.

150. Cavallini M, Gazzola R, Metalla M, Vaienti L. The role of hyaluronidase in the treatment of complications from hyaluronic Acid dermal fillers. Aesthet Surg J 2013; 1: 1167–74.

Journal of Medical Biochemistry

The Journal of Society of Medical Biochemists of Serbia

Journal Information

IMPACT FACTOR 2017: 1.378
5-year IMPACT FACTOR: 0.704

CiteScore 2017: 1.05

SCImago Journal Rank (SJR) 2017: 0.307
Source Normalized Impact per Paper (SNIP) 2017: 0.532

Cited By


All Time Past Year Past 30 Days
Abstract Views 0 0 0
Full Text Views 170 170 24
PDF Downloads 52 52 5