Stability Of A Commercial Lipase From<i>Mucor Jav Anicus:</i>Kinetic Modelling Of Ph And Temperature Dependencies

Balcão, Victor M.; Oliveira, Teresa A.C.; Malcata, F. Xavier

doi:10.3109/10242429809040110

Cited by 16 publications

(10 citation statements)

References 18 publications

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“…javanicus (Balcao et al, 1998), and 304 kJ mol -1 for lipase from R. miehei (Noel and Combes, 2003). Our value is within the overall range reported.…”

Section: Thermal Deactivation Kinetics Of the Wool Immobilized Lipasesupporting

confidence: 85%

Characterization of tributyrin hydrolysis by immobilized lipase on woolen cloth using conventional batch and novel spinning cloth disc reactors

Feng

Patterson

Balaban

et al. 2013

Chemical Engineering Research and Design

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Optimal loading and operating conditions for a new, superior immobilization of amano lipase from P. fluorescens on woolen cloth were determined. The optimal enzyme loading was 46.8 mg g dry cloth-1 with activity of 200 U. A batch reactor was used to characterize process conditions important to industrial application of the wool immobilized lipase. The optimal pH for immobilized lipase in tributyrin hydrolysis was 7, slightly lower than that of free lipase (pH 8). The optimal temperature for both free and immobilized lipase was 45 °C. The immobilized lipase was more stable to reuse than some other lipase immobilizations, maintaining 85% of its activity after 6 long term runs and 75.8% of the original activity after storage of 40 weeks at 4 °C. The thermal stability of lipase was improved by 2.4 times after immobilization. The thermal deactivation rate of immobilized lipase followed the Arrhenius law with E d =199 kJ mol −1. The Michaelis-Menten constant (K m) of the lipase increased from 1.63 mM to 4.48 mM after immobilization. The immobilized lipase was also successfully applied for tributyrin hydrolysis in a novel enzyme process intensification technologythe spinning cloth disc reactor (SCDR): conversion increased by around 13% under similar conditions compared to a conventional batch stirred tank reactor. The SCDR is therefore key to exploiting the advantages of the wool immobilized lipase developed in this work.

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“…javanicus (Balcao et al, 1998), and 304 kJ mol -1 for lipase from R. miehei (Noel and Combes, 2003). Our value is within the overall range reported.…”

Section: Thermal Deactivation Kinetics Of the Wool Immobilized Lipasesupporting

confidence: 85%

Characterization of tributyrin hydrolysis by immobilized lipase on woolen cloth using conventional batch and novel spinning cloth disc reactors

Feng

Patterson

Balaban

et al. 2013

Chemical Engineering Research and Design

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“…Thermal stability of the cardosin A agarose(6BCL)-glutaraldehyde derivative was checked at 40, 50 and 55 • C. Following incubation for 48 h at each such temperature, the derivatives retained virtually 100% activity (results not shown); these results agree with Balcão et al [22,33] and Lamas et al [18].…”

Section: Thermal Stability Of Immobilized Cardosin Asupporting

confidence: 86%

Hydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supports

Barros

Extremina

Gonçalves

et al. 2003

Enzyme and Microbial Technology

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In the present research effort, production of derivatives of cardosin A (a plant protease) encompassing full stabilization of its dimeric structure has been achieved, via covalent, multi-subunit immobilization onto highly activated agarose-glutaraldehyde supports. Boiling such enzyme derivatives in the presence of sodium dodecyl sulfate and ␤-mercaptoethanol did not lead to leaching of enzyme, thus providing evidence for the effectiveness of the attachment procedure. Furthermore, the cardosin A derivatives prepared under optimal conditions presented ca. half the specific activity of the enzyme in soluble form, and were successfully employed at laboratory-scale trials to perform (selective) hydrolysis of ␣-lactalbumin (␣-La), one of the major proteins in bovine whey. Hydrolysates of ␣-La were assayed for by the OPA method, as well as by FPLC, SDS-PAGE and HPLC. Thermal inactivation of the immobilized cardosin A was also assessed at 40, 50 and 55 • C; at these temperatures, no thermal denaturation took place during incubation for 48 h. The highest degree of hydrolysis was attained by 5 h reaction, at 55 • C and pH 5.2. SDS-PAGE of ␣-La hydrolysates displayed bands corresponding to low molecular weight peptides. Our results suggest that cardosin A in immobilized form is a good candidate to bring about proteolysis in the dairy industry, namely in whey processing.

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“…The evolution with time of the total concentration of free fatty acids in hydrolysed bovine, ovine and caprine milkfats, incubated with each of the eleven microbial enzymes tested, is depicted in Figs 1–3. It is apparent that hydrolysis proceeded for 1–2 h, and then essentially halted – most likely due to product inhibition and/or (reversible) enzyme inactivation, because of a progressively lower pH of the reaction media (Balcão et al. , 1998c).…”

Section: Resultsmentioning

confidence: 99%

Flavour development via lipolysis of milkfats: changes in free fatty acid pool

Regado

Cristóvão

Moutinho

et al. 2007

Int J of Food Sci Tech

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Under the trade name lipolysed milkfat (LMF), concentrated cheese flavours obtained via enzymatic treatments of cheese (or other dairy substrates) have been made available in increasing numbers. In this research effort, (anhydrous) milkfats from cows, ewes and goats were used as substrates for production of cheesy flavours. Those milkfats were subjected to modifications brought about by ten different (commercial) lipases and one cutinase, and the free fatty acids released were analysed by high performance liquid chromatography. Both the degrees of hydrolysis and the free fatty acid profiles of the final products were similar to those reported for several LMF products, although specific keynotes could be pinpointed. Consequently, those milkfats may represent alternative raw materials for manufacture of cheesy flavours, while contributing to alleviate the problem derived from the increasing surplus of milkfat in Western countries.

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Stability Of A Commercial Lipase FromMucor Jav Anicus:Kinetic Modelling Of Ph And Temperature Dependencies

Cited by 16 publications

References 18 publications

Characterization of tributyrin hydrolysis by immobilized lipase on woolen cloth using conventional batch and novel spinning cloth disc reactors

Characterization of tributyrin hydrolysis by immobilized lipase on woolen cloth using conventional batch and novel spinning cloth disc reactors

Hydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supports

Flavour development via lipolysis of milkfats: changes in free fatty acid pool

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