Dergiler / Communications Faculty of Sciences University of Ankara Series C Biology / 2021 / Cilt: 30 - Sayı: 2

IN SILICO PROOFS FOR PHLORIDZIN, NARINGENIN, AND CINNAMIC ACID AS ALPHA-AMYLASE ACTIVATORS, WHICH IS IMPORTANT IN INDUSTRIAL MICROBIOLOGY OR BIOCHEMICAL ENGINEERING

Sayfa
134–147
Yayın Tarihi
2021-12-31
DOI
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⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

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.

📌 3 Maddede Bu Makale

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Amaç & Hipotez: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.
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Temel Bulgular & Veri:This enzyme breaks down α-1,4 glycosidic bonds in amylose or amylopectin.
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Sonuç & Katkı: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.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alpha amylase · activator · phloridzin

Abstract

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.

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Bu Makaleye Atıf Yap

ALTUNER, E. M. (2021). IN SILICO 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, Cilt: 30 - Sayı: 2, 134–147. https://ajindex.com/articles/482042

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Kaynakça (11)

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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.
  11. Menshaz, A., Altuner, E.M.,