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      Optimization of the Hydrolysis of Safflower Oil for the Production of Linoleic Acid, Used as Flavor Precursor

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          Abstract

          Commercial lipases, from porcine pancreas (PPL), Candida rugosa (CRL), and Thermomyces lanuginosus (Lipozyme TL IM), were investigated in terms of their efficiency for the hydrolysis of safflower oil (SO) for the liberation of free linoleic acid (LA), used as a flavor precursor. Although PPL, under the optimized conditions, showed a high degree of hydrolysis (91.6%), its low tolerance towards higher substrate concentrations could limit its use for SO hydrolysis. In comparison to the other investigated lipases, Lipozyme TL IM required higher amount of enzyme and an additional 3 h of reaction time to achieve its maximum degree of SO hydrolysis (90.2%). On the basis of the experimental findings, CRL was selected as the most appropriate biocatalyst, with 84.1% degree of hydrolysis. The chromatographic analyses showed that the CRL-hydrolyzed SO is composed mainly of free LA.

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          Lipases at interfaces: a review.

          Patricia P. Reis, K Holmberg, H. Watzke … (2015)
          Lipases are acyl hydrolases that play a key role in fat digestion by cleaving long-chain triglycerides into polar lipids. Due to an opposite polarity between the enzyme (hydrophilic) and their substrates (lipophilic), lipase reaction occurs at the interface between the aqueous and the oil phases. Hence, interfaces are the key spots for lipase biocatalysis and an appropriate site for modulating lipolysis. Surprisingly enough, knowledge about the effects of the interfacial composition on lipase catalysis is still limited and only described by the term "interfacial quality". Recent systematic studies based on a biophysical approach allowed for the first time to show the effects of the interfacial microenvironment on lipase catalysis. These studies demonstrate that lipase activity as a function of interfacial composition is more attributed to substrate inaccessibility rather than to enzyme denaturation or inactivation, as it is often hypothesized. A detailed analysis of the interfacial properties of all compounds involved in triglyceride digestion revealed that lipolysis is a self-regulated reaction. This feedback mechanism can be explored as a new avenue to control lipase catalysis. To substantiate this hypothesis, oil hydrolysis in a model gastro-intestinal system was performed, which can be seen as an interfacial engineering approach to enzyme reactivity control. The presented characterization of the interfacial composition and its consequences provide a new approach for the understanding of lipase reactions at interfaces with direct impact on biotechnological and health care applications.
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            The effect of reaction conditions upon lipase catalysed hydrolysis of high oleate sunflower oil in a stirred liquid–liquid reactor

            D. Rooney, L.R. Weatherley (2001)
            Article 0 comments Cited 17 times – based on 0 reviews     Review now
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              Enzymatic hydrolysis of soybean oil using lipase from different sources to yield concentrated of polyunsaturated fatty acids.

              Tania Bueno, Julio Santos, Heizir Castro … (2007)
              The ability of three commercially available lipases to mediate the hydrolysis of the soybean oil to yield concentrated of essential fatty acids was evaluated. The tested lipases were from microbial (Candida rugosa and Thermomyces lanuginosa) and animal cells (Porcine pancreatic lipase). In terms of free fatty acids, microbial lipases were more effective to promote the enzymatic hydrolysis of the soybean oil (over 70%) than the porcine pancreatic lipase (24%). In spite of this, porcine pancreatic lipase (PPL) showed the most satisfactory specificity towards both essential fatty acids and was, therefore, chosen to carry out additional studies. An experimental design was performed taking into consideration the enzyme and NaCl amounts as independent variables. The main effects were fitted by multiple regression analysis to a linear model and maximum fatty acids concentration could be obtained using 3.0 wt% of lipase and 0.08 wt% of NaCl. The mathematical model representing the hydrolysis degree was found to describe adequately the experimental results. Under these conditions, concentrations of 29.5 g/L and 4.6 g/L for linoleic and linolenic acids, respectively, were obtained.
              Article 0 comments Cited 15 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Food Sci
                Journal ID (iso-abbrev): Int J Food Sci
                Journal ID (publisher-id): IJFS
                Title: International Journal of Food Science
                Publisher: Hindawi Publishing Corporation
                ISSN (Electronic): 2314-5765
                Publication date (Print): 2015
                Publication date (Electronic): 4 June 2015
                Volume: 2015
                Electronic Location Identifier: 594238
                Affiliations
                1Department of Food Science and Agricultural Chemistry, McGill University, 21111 Lakeshore, Sainte-Anne-de-Bellevue, QC, Canada H9X 3V9
                2AgroSup Dijon, Université de Bourgogne, 1 Esplanade Erasme, 21000 Dijon, France
                Author notes

                Academic Editor: Salam A. Ibrahim

                Article
                DOI: 10.1155/2015/594238
                PMC ID: 4745565
                PubMed ID: 26904663
                SO-VID: 67d27c6e-234a-4034-af26-81f14afa6754
                Copyright © Copyright © 2015 Marya Aziz et al.
                License:

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 24 March 2015
                Date accepted : 4 May 2015
                Categories
                Subject: Research Article

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