SavedAdd your journal

Journals / Turkish Journal of Chemistry / 2020 / Cilt: 44 - Sayı: 5

The production of enantiomerically pure 1-phenylethanol by enzymatic kinetic resolution method using response surface methodology

Ayse BOZAN
Rahime SONGUR
Ulku MEHMETOGLU
Pages
1352–1365
Publication Date
2020-10-26
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

This is an important result considering the industrial scale perspective.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:As the enantiomers of 1-phenylethanol are valuable intermediates in several industries, the lipase catalyzed kinetic resolution of (R,S) -1-phenylethanol is a relevant research topic.
📊
Key Findings & Data:In this study, the goal was to determine the optimum reaction parameters to produce enantiomerically pure 1-phenylethanol by lipase (Novozyme 435) catalyzed kinetic resolution using response surface methodology (RSM).
💡
Conclusion & Impact:This is an important result considering the industrial scale perspective.
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:1-phenylethanol · enzymatic kinetic resolution · chiral alcohol

Abstract

As the enantiomers of 1-phenylethanol are valuable intermediates in several industries, the lipase catalyzed kinetic resolution of (R,S) -1-phenylethanol is a relevant research topic. In this study, the goal was to determine the optimum reaction parameters to produce enantiomerically pure 1-phenylethanol by lipase (Novozyme 435) catalyzed kinetic resolution using response surface methodology (RSM). Reactions were performed with 40-400 mM (R,S)-1-phenylethanol, 120-1200 mM vinyl acetate and 2-22 mg/mL biocatalyst concentrations (BCL), at 20-60 degrees C and with a stirring rate of 50-400 rpm for 5-120 min. The samples were analyzed using high performance liquid chromatography (HPLC) with a Chiralcel OB column. Optimum reaction parameters to reach 100% enantiomeric excess for the substrate (ee(s)) were determined as follows: substrate concentration (C-s): 240 mM, BCL: 11 mg/mL, at 42 degrees C with a reaction time of 75 mM. Model validation was performed using these conditions and ee s was calculated as 100%, which indicates the predicted model was efficient and accurate. When compared to the literature, it was observed that the reaction time decreased significantly. This is an important result considering the industrial scale perspective.

🔖

Cite This Article

BOZAN, A., SONGUR, R., MEHMETOGLU, U. (2020). The production of enantiomerically pure 1-phenylethanol by enzymatic kinetic resolution method using response surface methodology. Turkish Journal of Chemistry, Cilt: 44 - Sayı: 5, 1352–1365. https://ajindex.com/articles/212679

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (3)

  1. Ahmed M, 2012,
  2. TETRAHEDRON, V68, P6781, DOI 10.1016/j.tet.2012.05.049 Almeida JM, 2020, BBA-PROTEINS PROTEOM, V1868, DOI 10.1016/j.bbapap.2019.140320 Angajala G, 2016, BIOCATAL AGRIC BIOTE, V7, P257, DOI 10.1016/j.bcab.2016.07.001 Bai W, 2012, J MOL CATAL B-ENZYM, V76, P82, DOI 10.1016/j.molcatb.2011.11.005 Bezerra MA, 2008,
  3. TALANTA, V76, P965, DOI 10.1016/j.talanta.2008.05.019 Bharathi D, 2019, BIOCATAL AGR BIOTECH, V22, DOI 10.1016/j.bcab.2019.101368 Cazetta T, 2014, J MOL CATAL B-ENZYM, V109, P178, DOI 10.1016/j.molcatb.2014.08.018 Celebi N, 2008, J SUPERCRIT FLUID, V47, P227, DOI 10.1016/j.supflu.2008.07.022 CHEN CS, 1982, J AM CHEM SOC, V104, P7294, DOI 10.1021/ja00389a064 Cui CX, 2015, BIOCATAL BIOTRANSFOR, V33, P38, DOI 10.3109/10242422.2015.1018190 Cui P, 2016, J MOL CATAL B-ENZYM, V130, P25, DOI 10.1016/j.molcatb.2016.04.013 Dhake KP, 2012, J MOL CATAL B-ENZYM, V77, P15, DOI 10.1016/j.molcatb.2012.01.009 Dwivedee BP, 2017, BIORESOURCE TECHNOL, V239, P464, DOI 10.1016/j.biortech.2017.05.050 Goswami A, 2005, TETRAHEDRON LETT, V46, P4411, DOI 10.1016/j.tetlet.2005.03.147 Graber M, 2016, J BIOTECHNOL, V238, P60, DOI 10.1016/j.jbiotec.2016.09.010 Gupta SM, 2017, MOL CATAL, V440, P50, DOI 10.1016/j.mcat.2017.06.020 Habulin M, 2009, J MOL CATAL B-ENZYM, V58, P24, DOI 10.1016/j.molcatb.2008.10.007 Hara P, 2010, J MOL CATAL B-ENZYM, V67, P129, DOI 10.1016/j.molcatb.2010.07.018 Idris A, 2012, BIOTECHNOL ADV, V30, P550, DOI 10.1016/j.biotechadv.2011.10.002 Kamble MP, 2017, BIOCHEM ENG J, V117, P121, DOI 10.1016/j.bej.2016.09.007 Kirilin A, 2010, INT J CHEM KINET, V42, P629, DOI 10.1002/kin.20504 Li K, 2018, CHEM ENG J, V351, P258, DOI 10.1016/j.cej.2018.06.086 Li X, 2013, PROCESS BIOCHEM, V48, P1905, DOI 10.1016/j.procbio.2013.09.001 Malyemez AS, 2017, TURK J BIOCHEM, V42, P600, DOI 10.1515/tjb-2016-0299 Melais N, 2016, CR CHIM, V19, P971, DOI 10.1016/j.crci.2016.05.002 Mukherjee J, 2015, INT J BIOL MACROMOL, V81, P544, DOI 10.1016/j.ijbiomac.2015.08.033 Pascoal A, 2018, PHYSIOL MOL PLANT P, V104, P119, DOI 10.1016/j.pmpp.2018.08.003 Rios AP, 2012, GREEN CHEM, V14, P1584, DOI DOI 10.1039/C2GC35196J Seddigi ZS, 2017, COORDIN CHEM REV, V348, P54, DOI 10.1016/j.ccr.2017.08.008 Shivaprasad P, 2018, CHEM ENG PROCESS, V132, P56, DOI 10.1016/j.cep.2018.08.012 Song LJ, 2020, J CONTROL RELEASE, V324, P156, DOI 10.1016/j.jconrel.2020.05.019 Soyer A, 2010, PREP BIOCHEM BIOTECH, V40, P389, DOI 10.1080/10826068.2010.525433 Sureshkumar M, 2009, J MOL CATAL B-ENZYM, V60, P