Interesterification of fat blends using a fermented solid with lipolytic activity

Rasera, K.; Osório, Natália M.; Mitchell, David A.; Krieger, Nádia; Ferreira‐Dias, Suzana

doi:10.1016/j.molcatb.2011.12.008

Cited by 13 publications

(10 citation statements)

References 41 publications

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“…In addition, lipase produced by SSF, using Rhizopus sp. as a thermotolerant fungus, In food applications, lipase produced in SSF by Rhizopus oryzae and Rhizopus microsporus, on a mixture of sugarcane bagasse and sunflower seed meal, was used in interesterification processes of oils to produce fat products with desirable properties (Rasera et al, 2012). This enzyme was able to catalyze the interesterification of a mixture of palm stearin, palm kernel oil and a concentrate of triacylglycerols enriched with omega-3 polyunsaturated fatty acids.…”

Section: Lipasementioning

confidence: 99%

From Wastes to High Value Added Products: Novel Aspects of SSF in the Production of Enzymes

El-Bakry

Abraham

Cerda

et al. 2015

Critical Reviews in Environmental Science and Technology

107

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Solid state fermentation (SSF), a process that occurs in the absence or near absence of water, has been used for the production of various high value added products such as enzymes and other organic components. This paper reviews the recent studies reported on the use of SSF for the production of enzymes; lipases, proteases, cellulases, hemicellulases, ligninases, glucoamylases, pectinases and inulinases. The microorganisms used for fermentation are mostly fungi and substrates are waste materials from the agriculture and food industry. This shows the advantages of SSF from an economical and environmental viewpoint. The paper provides an Downloaded by [New York University] at 03:19 04 February 2015 ACCEPTED MANUSCRIPT ACCEPTED MANUSCRIPT 2 update on several issues, viz. wastes, microorganisms and scale-up and control of the process of fermentation in solid-state.

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Section: Lipasementioning

confidence: 99%

From Wastes to High Value Added Products: Novel Aspects of SSF in the Production of Enzymes

El-Bakry

Abraham

Cerda

et al. 2015

Critical Reviews in Environmental Science and Technology

107

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“…Lipases can be used as biocatalysts in the synthesis of value-added esters for use in the cosmetic [ 1 ],[ 2 ] and aroma industries [ 3 ]-[ 5 ], in the enzymatic synthesis of biodiesel [ 6 ]-[ 12 ], in the modification of fats and oils [ 13 ] and to carry out stereospecific reactions in the synthesis of pharmaceuticals and other high-value compounds [ 14 ]-[ 16 ]. In many of these applications water is not the solvent, with the reaction being carried out in hydrophobic solvents, although hydrophilic solvents such as methanol or ethanol may be present as substrates [ 17 ],[ 18 ].…”

Section: Introductionmentioning

confidence: 99%

First co-expression of a lipase and its specific foldase obtained by metagenomics

et al. 2014

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BackgroundMetagenomics is a useful tool in the search for new lipases that might have characteristics that make them suitable for application in biocatalysis. This paper reports the cloning, co-expression, purification and characterization of a new lipase, denominated LipG9, and its specific foldase, LifG9, from a metagenomic library derived from a fat-contaminated soil.ResultsWithin the metagenomic library, the gene lipg9 was cloned jointly with the gene of the foldase, lifg9. LipG9 and LifG9 have 96% and 84% identity, respectively, with the corresponding proteins of Aeromonas veronii B565. LipG9 and LifG9 were co-expressed, both in N-truncated form, in Escherichia coli BL21(DE3), using the vectors pET28a(+) and pT7-7, respectively, and then purified by affinity chromatography using a Ni2+ column (HiTrap Chelating HP). The purified enzyme eluted from the column complexed with its foldase. The molecular masses of the N-truncated proteins were 32 kDa for LipG9, including the N-terminal His-tag with 6 residues, and 23 kDa for LifG9, which did not have a His-tag. The biochemical and kinetic characteristics of the purified lipase-foldase preparation were investigated. This preparation was active and stable over a wide range of pH values (6.5-9.5) and temperatures (10-40°C), with the highest specific activity, of 1500 U mg−1, being obtained at pH 7.5 at 30°C. It also had high specific activities against tributyrin, tricaprylin and triolein, with values of 1852, 1566 and 817 U mg−1, respectively. A phylogenetic analysis placed LipG9 in the lipase subfamily I.1. A comparison of the sequence of LipG9 with those of other bacterial lipases in the Protein Data Bank showed that LipG9 contains not only the classic catalytic triad (Ser103, Asp250, His272), with the catalytic Ser occurring within a conserved pentapeptide, Gly-His-Ser-His-Gly, but also a conserved disulfide bridge and a conserved calcium binding site. The homology-modeled structure presents a canonical α/β hydrolase folding type I.ConclusionsThis paper is the first to report the successful co-expression of a lipase and its associated foldase from a metagenomic library. The high activity and stability of Lip-LifG9 suggest that it has a good potential for use in biocatalysis.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-014-0171-7) contains supplementary material, which is available to authorized users.

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“…The physical, nutritional and sensory properties of margarines are attained by appropriate processing of selected blends of fats and oils 1. Until the 1990s, hardstocks for margarines and shortenings were mainly obtained through hydrogenation of polyunsaturated oils 1–3. Although this process is relatively inexpensive, it destroys essential PUFAs and creates non‐natural isomers of saturated fats 2.…”

Section: Introductionmentioning

confidence: 99%

“…Over the last decade, lipase‐catalyzed interesterification processes have been developed for the production of margarines and shortenings 2, 3, 14–22 and some processes have already been implemented at industrial scale 4, 23, 24.…”

Section: Introductionmentioning

confidence: 99%

Batch and continuous lipase‐catalyzed interesterification of blends containing olive oil for trans‐free margarines

Soares

Osório

Silva

et al. 2013

Euro J Lipid Sci & Tech

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The interesterification of natural fats can improve certain physical and nutraceutical properties by modification of their acylglycerol profile. The aim of this study was the production of structured lipids by lipase-catalyzed interesterification of blends of palm stearin (PS), palm kernel oil (PK), and olive oil (OO), to be incorporated in margarines. Interesterification activity was evaluated by the decrease of the solid fat content at 358C (SFC 358C ) of the blends. The best interesterification conditions, found by response surface methodology (RSM), catalyzed by ''Lipozyme 1 TL IM'' or ''Lipozyme 1 RM IM,'' were 658C and a blend of 45% w/w of PS, 30% w/w of PK, and 25% w/w of OO. Under these conditions, after 2 h of batch interesterification, the product had a SFC 358C of 3.0%. The reaction was implemented in a continuous packed-bed bioreactor, under optimized conditions, for 226 h (''Lipozyme 1 TL IM'') or 188 h (''Lipozyme 1 RM IM''), at a residence time of 7 min. The inactivation profile of both biocatalysts followed the first-order deactivation model: half-lives of 88 h (''Lipozyme 1 TL IM'') and 60 h (''Lipozyme 1 RM IM'') were estimated, respectively. Free fatty acid content of continuous interesterified blends (c.a. 1% w/w) was lower than that of batch-interesterified blends (c.a. 4-5% w/w). Practical applications:The obtained structured lipids, with low SFC 358C , are adequate for the production of trans-free table margarines. Using sn-1,3 specific lipases as catalysts, the original fatty acids at sn-2 position will be maintained with nutritional benefits. PS and PK are fats used as trans-free sources of solid fat, for the margarine industry, which are not very sensitive to oxidation. PK, a lauric fat, imparts a fast crystallization rate and confers plasticity to the final products. The incorporation of OO will enrich the blends with natural antioxidants and oleic acid at sn-2 position in acylglycerols. The development of response surface models, describing both final SFC values of interesterified blends and SFC decrease, will allow predicting results for novel proportions of fats and oils and/or a novel combination composition-temperature. The implementation of the interesterification in continuous reactors promotes a faster reaction and lower acidity of interesterified blends, with benefits in terms of product separation and purification. Abbreviations: a, residual activity; a w , water activity; Abs 232 nm , absorbance at 232 nm; Abs 270 nm, absorbance at 270 nm; AI, acidity index; CCRD, central composite rotatable design;

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Interesterification of fat blends using a fermented solid with lipolytic activity

Cited by 13 publications

References 41 publications

From Wastes to High Value Added Products: Novel Aspects of SSF in the Production of Enzymes

From Wastes to High Value Added Products: Novel Aspects of SSF in the Production of Enzymes

First co-expression of a lipase and its specific foldase obtained by metagenomics

Batch and continuous lipase‐catalyzed interesterification of blends containing olive oil for trans‐free margarines

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