Purification and improvement of the functional properties of Rhizopus oryzae lipase using immobilization techniques

2014 ◽  
Vol 110 ◽  
pp. 111-116 ◽  
Author(s):  
N. Ghattas ◽  
M. Filice ◽  
F. Abidi ◽  
J.M. Guisan ◽  
A. Ben Salah
Keyword(s):  
Functional Properties ◽  
Rhizopus Oryzae ◽  
Rhizopus Oryzae Lipase ◽  
Immobilization Techniques

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.

scholarly journals Synthesis of Dietetic Structured Lipids from Spent Coffee Grounds Crude Oil Catalyzed by Commercial Immobilized Lipases and Immobilized Rhizopus oryzae Lipase on Biochar and Hybrid Support

Processes ◽  
2020 ◽  
Vol 8 (12) ◽  
pp. 1542
Author(s):  
Danyelle A. Mota ◽  
Jefferson C. B. Santos ◽  
Diana Faria ◽  
Álvaro S. Lima ◽  
Laiza C. Krause ◽  
...  
Keyword(s):  
Crude Oil ◽  
Rhizopus Oryzae ◽  
Structured Lipids ◽  
Thermomyces Lanuginosus ◽  
Spent Coffee Grounds ◽  
Lipozyme Tl Im ◽  
Rhizopus Oryzae Lipase ◽  
Lipozyme Rm Im ◽  
Coffee Grounds ◽  
Pharmaceutical Industries

The aim of this study was the valorization of coffee industry residues, namely spent coffee grounds (SCG) as a source of oil, and silverskin (CS) as a source of both oil and biomass, under the concept of the circular economy. Therefore, crude oil from SCG was used to produce low-calorie structured lipids (SL) for food and pharmaceutical industries, and CS to produce biochar by pyrolysis for biotechnological uses. SL were obtained by acidolysis with caprylic or capric acid, or interesterification with ethyl caprylate or ethyl caprate, in solvent-free media, catalyzed by immobilized sn-1,3 regioselective lipases. Silverskin biochar (BIO) was directly used as enzyme carrier or to produce hybrid organic-silica (HB) supports for enzyme immobilization. Rhizopus oryzae lipase (ROL) immobilized on Amberlite (AMB), silica (SIL), BIO or HB, and the commercial immobilized Thermomyces lanuginosus (Lipozyme TL IM) and Rhizomucor miehei (Lipozyme RM IM) lipases were tested. Lipozyme RM IM showed better results in SL production than Lipozyme TLIM or ROL on BIO, SIL or HB. About 90% triacylglycerol conversion was attained after 7 h acidolysis or interesterification. Lipozyme RM IM was more stable in interesterification (80% and 65% activity with ethyl caprylate or ethyl caprate) than in acidolysis (first-order decay) after 10 reuses.

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