Effect of the structural chemical composition of mesoporous materials on the adsorption and activation of the Rhizopus oryzae lipase-catalyzed trans-esterification reaction in organic solvent

2008 ◽  
Vol 10 (2) ◽  
pp. 165-168 ◽  
Author(s):  
Mozaffar Shakeri ◽  
Koei Kawakami
Keyword(s):  
Chemical Composition ◽  
Organic Solvent ◽  
Mesoporous Materials ◽  
Rhizopus Oryzae ◽  
Esterification Reaction ◽  
Rhizopus Oryzae Lipase

Biodiesel fuel production from plant oil catalyzed by Rhizopus oryzae lipase in a water-containing system without an organic solvent

1999 ◽  
Vol 88 (6) ◽  
pp. 627-631 ◽  
Author(s):  
Masaru Kaieda ◽  
Taichi Samukawa ◽  
Takeshi Matsumoto ◽  
Kazuhiro Ban ◽  
Akihiko Kondo ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Rhizopus Oryzae ◽  
Biodiesel Fuel ◽  
Fuel Production ◽  
Plant Oil ◽  
Rhizopus Oryzae Lipase

Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastoris

2001 ◽  
Vol 86 (1) ◽  
pp. 59-70 ◽  
Author(s):  
Stefan Minning ◽  
Alicia Serrano ◽  
Pau Ferrer ◽  
Carles Solá ◽  
Rolf D. Schmid ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Rhizopus Oryzae ◽  
Rhizopus Oryzae Lipase ◽  
High Level ◽  
Level Production

scholarly journals Transcriptional response of P. pastoris in fed-batch cultivations to Rhizopus oryzae lipase production reveals UPR induction

2007 ◽  
Vol 6 (1) ◽  
pp. 21 ◽  
Author(s):  
David Resina ◽  
Mónika Bollók ◽  
Narendar K Khatri ◽  
Francisco Valero ◽  
Peter Neubauer ◽  
...  
Keyword(s):  
Rhizopus Oryzae ◽  
Transcriptional Response ◽  
Lipase Production ◽  
Fed Batch ◽  
Rhizopus Oryzae Lipase

scholarly journals Truncated Prosequence of Rhizopus oryzae Lipase: Key Factor for Production Improvement and Biocatalyst Stability

Catalysts ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 961 ◽  
Author(s):  
Josu López-Fernández ◽  
Juan J. Barrero ◽  
M. Dolors Benaiges ◽  
Francisco Valero
Keyword(s):  
Amino Acids ◽  
Ionic Strength ◽  
Rhizopus Oryzae ◽  
Lipase Production ◽  
Biochemical Properties ◽  
Mature Sequence ◽  
Rhizopus Oryzae Lipase ◽  
Batch Cultures ◽  
Production Improvement ◽  
Key Factor

Recombinant Rhizopus oryzae lipase (mature sequence, rROL) was modified by adding to its N-terminal 28 additional amino acids from the C-terminal of the prosequence (proROL) to obtain a biocatalyst more suitable for the biodiesel industry. Both enzymes were expressed in Pichia pastoris and compared in terms of production bioprocess parameters, biochemical properties, and stability. Growth kinetics, production, and yields were better for proROL harboring strain than rROL one in batch cultures. When different fed-batch strategies were applied, lipase production and volumetric productivity of proROL-strain were always higher (5.4 and 4.4-fold, respectively) in the best case. rROL and proROL enzymatic activity was dependent on ionic strength and peaked in 200 mM Tris-HCl buffer. The optimum temperature and pH for rROL were influenced by ionic strength, but those for proROL were not. The presence of these amino acids altered lipase substrate specificity and increased proROL stability when different temperature, pH, and methanol/ethanol concentrations were employed. The 28 amino acids were found to be preferably removed by proteases, leading to the transformation of proROL into rROL. Nevertheless, the truncated prosequence enhanced Rhizopus oryzae lipase heterologous production and stability, making it more appropriate as industrial biocatalyst.

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