Publications – Binay Enzyme Recognition Center


  • Alpdağtaş, S., Yücel, S., Kapkaç, H. A., Liu, S., Binay, B. 2018. “Discovery of an acidic, thermostable and highly NADP+ dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929”, Biotechnology Letters, 40, 7, 1135-1147.
  • Çakar M. M., Mangas-Sanchez J., Birmingham W. R., Turner N. J., Binay B. 2018. “Discovery of a new metal and NAD+-dependent formate dehydrogenase from Clostridium ljungdahlii”, Preparative Biochemistry and Biotechnology, 48, 4, 327-334.
  • Altaş, N., Aşkın, A. S., Karataş, E., Chronopoulou, E., Labrou, N. E., Binay, B. 2017. "Heterologous production of extreme alkaline thermostable NAD+-dependent formate dehydrogenase with wide-range pH activity from Myceliophthora thermophila", Process Biochemistry, 61, 110- 118.
  • Aslan, S.A., Valjakka, J., Ruupunen, J., Yildirim, D., Turner, N. J., Turunen, O., Binay, B. 2017. "Chaetomium thermophilum formate dehydrogenase has high activity in the reduction of hydrogen carbonate (HCO3-) to formate", Protein Eng. Des. Select., 30, 47-55.
  • Alagöz, D., Çelik, A., Yildirim, D., Tükel, S.S., Binay B. 2016. “Covalent immobilization of Candida methylica formate dehydrogenase on short spacer arm aldehyde group containing supports”, Journal of Molecular Catalysis B: Enzymatic, 130, 40-47.
  • Yu, T., Wang, Y., Anbarasan, S., Telli, K., Aslan, A., Su, Z., Zhou, Y., Zhang, L., Iivonen, P., Havukainen, S., Mentunen, T., Hummel, M., Sixta, H., Binay, B., Turunen, O., Xiong, H. 2016. “Expression of a hyperthermostable Thermotoga maritima Xylanase XYN10B in Pichia pastoris and its stability and tolerance to ionic liquids”, Extremophiles, 20, 515-524.
  • Albuquerque, T., Rueda, N., dos Santos, J. C.S., Barbosa, O., Ortiz, C., Binay, B., Özdemir, E., Gonçalves, L. R. B., Fernandez-Lafuente, R. 2016. “Easy stabilization of interfacially activated lipases using heterofunctıonal divinylsulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment”, Process Biochemistry, 51, 865-874.
  • Aslan, S.A., Birmingham, W.R., Karagüler, N.G., Turner, N.J., Binay, B. 2016. “Semirational design of Geobacillus stearothermophilus lactate dehydrogenase to access various chiral α-hydroxy acids”, Applied Biochem and Biotech., 179, 474-484.
  • Rowles, I., Groenendaal, B., Binay, B., Malone, K.J., Willies, S.C., Turner, N.J. 2016. "Engineering of Phenylalanine Ammonia Lyase from Rhodotorula graminis for the Synthesis of Unnatural L-Amino Acids", Tetrahedron, 72, 7343-7347.
  • Alagoz, D.,  Binay, B., Yildirim, D., Celik, A., Tukel, S. S.,  2016. “Improving of stability of formate dehydrogenase from Candida methylica by immobilization onto Eupergit C 250 L”, Biotekhnologiya, 32, 37-42.
  • Binay, B., Alagöz, D., Yildirim, Y., Çelik, A., Tükel, S.S. 2016. “Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts in situ regeneration of NADH”, Beilstein Journal of Organic Chemistry, 12, 271-277.
  • Özgün, G., Karagüler, N.G., Turunen, O., Turner, N.J., Binay, B. 2015. "Characterization of a new acidic NAD+-dependent formate dehydrogenase from thermophilic fungus Chaetomium thermophilum", Journal of Molecular Catalysis B: Enzymatic, 122, 212-217.
  • Binay, B., Sessions, R. B., Gül-Karagüler, N. 2013. “A double mutant of highly prufied Geobacillus stearothermophilus LDH recognizes mandelic acid as a subsbstrate”. Enzyme and Microbial Technology, 52, 393-399.
  • Binay, B., Shoemark, D.K., Sessions, R.B., Clarke, A.R., Karaguler, N.G. 2009. “Increasing the substrate specificity of the lactate dehydrogenase from Bacillus stearothermophilus by DNA shuffling”, Biochemical Engineering Journal, 48, 118-123.
  • Karagüler, N.G., Binay, B., Ordu, E.B., Clarke, A.R. 2007. “Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH”, Biochem. Soc. Trans., 35, 1610-1615.
  • Binay, B., Karagüler, N.G. 2007. “Attempting to remove the substrate inhibition of L-lactate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis”, Appl. Biochem. Biotechnol., 141, 265-272.