In Silico Proofs for Phloridzin, Naringenin, and Cinnamic Acid as Alpha-amylase Activators, Which is Important in Industrial Microbiology or Biochemical Engineering

Ergin Murat Altuner1*

1Kastamonu University, Faculty of Science and Arts, Department of Biology, Kastamonu, Turkey
* Corresponding author: ergin.murat.altuner@gmail.com

Enzymes are commonly defined as biological catalysts, regulating particular biochemical reactions. α-Amylase (EC 3.2.1.1) is one of the industrially important enzymes, which are extensively used in starch hydrolyzing processes, such as brewing, fermentation, detergent production, food processing, etc. This enzyme breaks down α-1,4 glycosidic bonds in amylose or amylopectin. The end products from amylose are maltotriose and maltose. Maltose, glucose, and limit dextrin are formed from amylopectin. There are many studies in the literature regarding the α-amylase inhibitors, which have the potentials of being used in diabetes and obesity. However, there is a very limited number of studies in the literature about the activation of this enzyme, which could be harmful to such diseases. This study aims to support the activation activity of phloridzin, naringenin, and cinnamic acid for α-amylase, which was previously proved experimentally, with some in silico tests.
Keywords: Alpha amylase, activator, phloridzin, naringenin, cinnamic acid, in silico

How to cite: Altuner, E.M. (2021). Proofs for Phloridzin, Naringenin, and Cinnamic Acid as Alpha-amylase Activators, Which is Important in Industrial Microbiology or Biochemical Engineering. Communications Faculty of Sciences University of Ankara Series C Biology, 30(2), 134-147.

References
  • Doss, A., Anand, S.P., Purification and characterization of extracellular amylolytic enzyme from Aspergillus species, African Journal of Biotechnology, 11 (83) (2012), 14941–14945. https://doi.org/10.5897/ajb12.2542.
  • Tiwari, S.P., Srivastava, R., Singh, C.S., Shukla, K., Singh, R.K., Singh, P., Singh, R., Singh, N.L., Sharma, R., Amylases: an overview with special reference to alpha amylase, Journal of Global Sciences, 4 (1) (2015), 1886–1901.
  • Pandey, A., Nigam, P., Soccol, C.R., Soccol, V.T., Singh, D., Mohan, R., Advances in microbial amylases, Biotechnology and Applied Biochemistry, 31 (2) (2000), 135–152. https://doi.org/ 10.1042/ba19990073.
  • Souza, P.M.D., Application of microbial α-amylase in industry-A review, Brazilian Journal of Microbiology, 41 (4) (2010), 850–861. http://dx.doi.org/10.1590/S1517-83822010000400004.
  • Van Der Maarel, M.J., Van der Veen, B., Uitdehaag, J.C., Leemhuis, H., Dijkhuizen, L., Properties and applications of starch-converting enzymes of the α-amylase family, Journal of Biotechnology, 94 (2) (2002), 137–155. https://doi.org/10.1016/S0168-1656(01)00407-2.
  • Sundarram, A., Murthy, T.P.K., α-Amylase production and applications: a review, Journal of Applied & Environmental Microbiology, 2 (4) (2014), 166–175. https://doi.org/10.12691/jaem-2-4-10.
  • Gupta, R., Gigras, P., Mohapatra, H., Goswami, V. K., Chauhan, B., Microbial α-amylases: a biotechnological perspective, Process Biochemistry, 38 (11) (2003), 1599–1616. https://doi.org/10.1016/S0032-9592(03)00053-0.
  • Farooq, M.A., Ali, S., Hassan, A., Tahir, H.M., Mumtaz, S., Mumtaz, S., Biosynthesis and industrial applications of α-amylase: a review, Archives of Microbiology, (2021). https://doi.org/10.1007/s00203-020-02128-y.
  • Jamai, L., Ettayebi, K., El Yamani, J., Ettayebi, M., Production of ethanol from starch by free and immobilized Candida tropicalis in the presence of α-amylase, Bioresource Technology, 98 (14) (2007), 2765–2770. https://doi.org/10.1016/j.biortech.2006.09.057.
  • Jujjavarapu, S.E., Dhagat, S., Evolutionary trends in industrial production of α-amylase, Recent Patents on Biotechnology, 13 (1) (2019), 4–18. https://doi.org/10.2174/2211550107666180816093436.
  • Kashani-Amin, E., Yaghmaei, P., Larijani, B. and Ebrahim-Habibi, A., Xanthine derivatives as activators of alpha-amylase: Hypothesis on a link with the hyperglycemia induced by caffeine, Obesity Research & Clinical Practice, 7 (6) (2013), e487–e493. https://doi.org/10.1016/j.orcp.2012.07.007.
  • Menshaz, A., Altuner, E.M., The potential of some plant-derived compounds in inhibition of α-amylase, which is important for diabetic patients, Fresenius Environmental Bulletin, 29 (09A) (2020), 8642–8646.
  • Ramasubbu, N., Paloth, V., Luo, Y., Brayer, G.D., Levine, M.J., Structure of human salivary α-amylase at 1.6 Å resolution: implications for its role in the oral cavity, Acta Crystallographica Section D: Biological Crystallography, 52 (3) (1996), 435–446. https://doi.org/10.1107/S0907444995014119.
  • Biovia, Dassault Systèmes, Discovery Studio Visualizer v.20.1.0.19295 [Computer software], Dassault Systèmes, San Diego, 2019.
  • Morris, G.M., Huey, R., Lindstrom, W., Sanner, M.F., Belew, R.K., Goodsell, D.S., Olson, A.J., Autodock4 and AutoDockTools4: automated docking with selective receptor flexibility, Journal of Computational Chemistry, 30 (16) (2009), 2785–2791. https://doi.org/10.1002/jcc.21256.
  • O'Boyle, N.M., Banck, M., James, C.A., Morley, C., Vandermeersch, T., Hutchison, G.R., Open Babel: An open chemical toolbox, Journal of Cheminformatics, 3 (1) (2011), 1–14. https://doi.org/10.1186/1758-2946-3-33.
  • Joshi, T., Joshi, T., Sharma, P., Pundir, H., Chandra, S., In silico identification of natural fungicide from Melia azedarach against isocitrate lyase of Fusarium graminearum, Journal of Biomolecular Structure and Dynamics, (2020), 1–19. https://doi.org/10.1080/07391102.2020.1780941.
  • Tian, W., Chen, C., Lei, X., Zhao, J., Liang, J., CASTp 3.0: computed atlas of surface topography of proteins, Nucleic Acids Research, 46 (W1) (2018), W363–W367. https://doi.org/10.1093/nar/gky473.
  • Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., UCSF Chimera-a visualization system for exploratory research and analysis, Journal of Computational Chemistry, 25 (13) (2004), 1605–1612. https://doi.org/10.1002/jcc.20084.
  • Hsu, K.C., Chen, Y.F., Lin, S.R., Yang, J.M., iGEMDOCK: a graphical environment of enhancing GEMDOCK using pharmacological interactions and post-screening analysis, BMC Bioinformatics, 12 (1) (2011), 1–11. https://doi.org/10.1186/1471-2105-12-S1-S33.
  • Wallace, A.C., Laskowski, R.A., Thornton, J.M., LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions, Protein Engineering, Design and Selection, 8 (2) (1995), 127–134. https://doi.org/10.1093/protein/8.2.127.
  • Balavignesh, V., Srinivasan, E., Ramesh Babu, N. G., Saravanan, N., Molecular docking study ON NS5B polymerase of hepatitis c virus by screening of volatile compounds from Acacia concinna and ADMET prediction, International Journal of Pharmacy and Life Sciences, 4 (4) (2013), 2548-2558.
  • Yusoff, N.A., Ahmad, M., Al Hindi, B., Widyawati, T., Yam, M.F., Mahmud, R., Razak, K.N.A., Asmawi, M.Z., Aqueous extract of Nypa fruticans Wurmb. vinegar alleviates postprandial hyperglycemia in normoglycemic rats, Nutrients, 7 (8) (2015), 7012-7026. https://doi.org/10.3390/nu7085320.
  • Sharma, P., Kumar, V., Khosla, R., Guleria, P., Exogenous naringenin improved digestible protein accumulation and altered morphology via VrPIN and auxin redistribution in Vigna radiata, 3 Biotech, 10 (431) (2020), 1-14. https://doi.org/10.1007/s13205-020-02428-6.
  • Patel, K., Singh, G. K., Patel, D. K., A review on pharmacological and analytical aspects of naringenin, Chinese journal of integrative medicine, 24 (7) (2018), 551-560. https://doi.org/10.1007/s11655-014-1960-x.
  • Najafian, M., Ebrahim-Habibi, A., Yaghmaei, P., Parivar, K., Larijani, B., Core structure of flavonoids precursor as an antihyperglycemic and antihyperlipidemic agent: an in vivo study in rats, Acta Biochimica Polonica, 57 (4) (2010), 553-560. https://doi.org/10.18388/abp.2010_2443.
  • Qian, M., Haser, R., Buisson, G., Duee, E., Payan, F., The active center of a mammalian alpha-amylase structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-ANG Resolution, Biochemistry, 33 (20) (1994), 6284-6294. https://doi.org/10.1021/bi00186a031.
  • PDF