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( Miklos Tako ),( Alexandra Kotogan ),( Tamas Papp ),( Shine Kadaikunnan ),( Naiyf S. Alharbi ),( Csaba Vagvolgyi ) 한국미생물 · 생명공학회 2017 Journal of microbiology and biotechnology Vol.27 No.2
Rhizomucor miehei NRRL 5282 and Rhizopus oryzae NRRL 1526 can produce lipases with high synthetic activities in wheat bran-based solid-state culture. In this study, the purification and biochemical characterization of the lipolytic activities of these lipases are presented. SDSPAGE indicated a molecular mass of about 55 and 35 kDa for the purified R. miehei and Rh. oryzae enzymes, respectively. p-Nitrophenyl palmitate (pNPP) hydrolysis was maximal at 40°C and pH 7.0 for the R. miehei lipase, and at 30°C and pH 5.2 for the Rh. oryzae enzyme. The enzymes showed almost equal affinity to pNPP, but the V<sub>max</sub> of the Rh. oryzae lipase was about 1.13 times higher than that determined for R. miehei using the same substrate. For both enzymes, a dramatic loss of activity was observed in the presence of 5 mM Hg<sup>2+</sup>, Zn<sup>2+</sup>, or Mn<sup>2+</sup>, 10 mM N-bromosuccinimide or sodium dodecyl sulfate, and 5-10% (v/v) of hexanol or butanol. At the same time, they proved to be extraordinarily stable in the presence of nhexane, cyclohexane, n-heptane, and isooctane. Moreover, isopentanol up to 10% (v/v) and propionic acid in 1 mM concentrations increased the pNPP hydrolyzing activity of R. miehei lipase. Both enzymes had 1,3-regioselectivity, and efficiently hydrolyzed p-nitrophenyl (pNP) esters with C8-C16 acids, exhibiting maximum activity towards pNP-caprylate (R. miehei) and pNP-dodecanoate (Rh. oryzae). The purified lipases are promising candidates for various biotechnological applications.
Rudolf Gesztelyi,Zita Wachal,Bela Juhasz,Mariann Bombicz,Evelin Csepanyi,Krisztian Pak,Judit Zsuga,Csaba Papp,Zoltan Galajda,Klara Branzaniuc,Robert Porszasz,Andras Jozsef Szentmiklosi,Arpad Tosaki,Zs 대한약학회 2013 Archives of Pharmacal Research Vol.36 No.3
A1 adenosine receptors (A1 receptors) arewidely expressed in mammalian tissues; therefore attainingproper tissue selectivity is a cornerstone of drug development. The fact that partial agonists chiefly act on tissueswith great receptor reserve can be exploited to achieve anappropriate degree of tissue selectivity. To the best of ourknowledge, the A1 receptor reserve has not been yetquantified for the atrial contractility. A1 receptor reservewas determined for the direct negative inotropic effect ofthree A1 receptor full agonists (NECA, CPA and CHA) inisolated, paced guinea pig left atria, with the use of FSCPX, an irreversible A1 receptor antagonist. FSCPXcaused an apparently pure dextral displacement of theconcentration–response curves of A1 receptor agonists. Accordingly, the atrial A1 receptor function converging toinotropy showed a considerably great, approximately80–92 % of receptor reserve for a near maximal (about91–96 %) effect, which is greater than historical atrial A1receptor reserve data for any effects other than inotropy. Consequently, the guinea pig atrial contractility is verysensitive to A1 receptor stimulation. Thus, it is worthwhileconsidering that even partial A1 receptor agonists, given inany indication, might decrease the atrial contractile force,as an undesirable side effect, in humans.