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Purification and Properties of Extracellular Lipases with Transesterification Activity and 1,3-Regioselectivity from Rhizomucor miehei and Rhizopus oryzae.

Authors
  • Takó, Miklós1
  • KotogÁn, Alexandra1
  • Papp, TamÁs1, 2
  • Kadaikunnan, Shine3
  • Alharbi, Naiyf S3
  • VÁgvölgyi, Csaba1
  • 1 Department of Microbiology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Közép fasor 52, Hungary. , (Hungary)
  • 2 HAS-USZ "Momentum" Fungal Pathogenicity Mechanisms Research Group, University of Szeged, H-6726 Szeged, Közép fasor 52, Hungary. , (Hungary)
  • 3 Department of Botany and Microbiology, College of Science, King Saud University, Riyadh-11451, Saudi Arabia. , (Saudi Arabia)
Type
Published Article
Journal
Journal of microbiology and biotechnology
Publication Date
Feb 28, 2017
Volume
27
Issue
2
Pages
277–288
Identifiers
DOI: 10.4014/jmb.1608.08005
PMID: 27780957
Source
Medline
Keywords
License
Unknown

Abstract

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. SDS-PAGE 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 Vmax 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 Hg2+, Zn2+, or Mn2+, 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 n-hexane, 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.

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