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Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology

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A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (15 January 2024) | Viewed by 16550

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Dr. Priscilla Amaral

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Department of Biochemical Engineering, Escola de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21949-900, RJ, Brazil
Interests: bioproducts; yeast; biosurfactants; byproducts conversion; enzymes
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Prof. Dr. Ivaldo Itabaiana Junior

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School of Chemistry, Department of Biochemical Engineering, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
Interests: biocatalysis; hybrid catalysis; nanomaterials; enzymes; lipases; biomass valorization; levoglucosan; glycerol; biotransformation; microorganism; biochemistry
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Dear Colleagues,

Biotechnology has turned its attention to the development of more environmentally friendly processes. Among the enzymes of great importance in the scenario, lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) have gained high prominence through the years. This class of hydrolases is widespread in the animal and plant kingdoms, and most microorganisms have the natural ability to express them. Lipases can catalyze the hydrolysis of triacylglycerols, releasing fatty acids and glycerol, and the amount of water and presence of a hydrophobic lid are crucial in these processes. However, the ability to perform the synthesis, the non-necessity of co-factors, and the activity in organic solvents, besides their high enantio-, chemo- and regioselectivities, make them very attractive for applications in reactions of esterification, transesterification, kinetic resolution couplings, and others, being very important in organic syntheses, the hydrolysis of fats and oils, flavor enhancement, the synthesis of biopolymers and biodiesel, and the production of enantiopure pharmaceuticals and agrochemicals, which show its potential use in a wide range of industrial sectors. In order to improve the activity of lipases in different reaction media as well as increase the versatility of the reactors applied, lipases can be immobilized by different protocols, generating biocatalysts with high stability, retention of activity, and reuse capacity, being the target of several studies involving the construction of new supports, new methodologies, and even new industrial applications in order to generate more economically competitive processes. Together with this trend, the fermentative processes have been important tools to increase the productivity of lipases, besides being a direct strategy to valorize oily residues as microbial substrates.

Therefore, due to the promising perspectives of lipases, this Special Issue intends to publish research papers or review articles with, but not limited to, the following topics:

Lipase immobilization (surface immobilization, encapsulation, whole-cell immobilization, and others);
New material for lipase immobilization;
Characterization of lipases, enzyme kinetics, thermostability, bioactivity, etc.);
Biocatalysis and biotransformation with lipases;
Cascade reactions with lipases;
Hybrid catalysis with lipases;
Production of microbial lipases;
Overexpression of lipases;
Prospecting of new lipases;
Purification of lipases;
New renewable processes with lipases.

Prof. Dr. Priscilla Amaral
Prof. Dr. Ivaldo Itabaiana Junior
Guest Editors

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Keywords

lipase catalysis
microbial production
immobilization
characterization
purification
overexpression

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Published Papers (7 papers)

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Research

14 pages, 851 KiB

Open AccessArticle

Tuning Almond Lipase Features by Using Different Immobilization Supports

by Oumaima Cherni, Diego Carballares, El Hocine Siar, Pedro Abellanas-Perez, Diandra de Andrades, Javier Rocha-Martin, Sellema Bahri and Roberto Fernandez-Lafuente

Catalysts 2024, 14(2), 115; https://doi.org/10.3390/catal14020115 - 31 Jan 2024

Cited by 3 | Viewed by 1493

Abstract

The lipase from Prunus dulcis almonds has been immobilized for the first time. For this purpose, two different supports, an octadecyl methacrylate particulate support, and aminated agarose (monoaminoethyl-N-aminoethyl) have been utilized. Both immobilized biocatalysts show improved enzyme stability, but great changes in enzyme specificity were detected. The enzyme immobilized via ion exchange maintained its activity intact versus p-nitrophenyl butyrate, while the enzyme immobilized on the hydrophobic support fully lost its activity versus this substrate, which was confirmed to be due to substrate adsorption on the support. However, this biocatalyst was much more active versus triacetin (more than 10-fold), R- or S- methyl mandelate at pH 7. At pH 9, a strong effect of using phosphate or bicarbonate as reaction buffers was detected. Using bicarbonate, the interfacially immobilized enzyme presented no activity versus R-isomer, but it was very active versus the S-isomer and triacetin. Using a phosphate buffer during the reaction, all compounds were recognized as substrates. The enzyme immobilized via ion exchange was significantly more active using phosphate; in fact, using bicarbonate, the enzyme was inactive versus both methyl mandelate isomers. This paper shows for the first time a great interaction between the effects of the immobilization protocol and buffer used during reaction on the enantiospecificity of lipases. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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16 pages, 1764 KiB

Open AccessFeature PaperArticle

The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading

by Pedro Abellanas-Perez, Diego Carballares, Javier Rocha-Martin and Roberto Fernandez-Lafuente

Catalysts 2024, 14(2), 105; https://doi.org/10.3390/catal14020105 - 26 Jan 2024

Cited by 3 | Viewed by 1649

Abstract

The lipases from Thermomyces lanuginosus (TLL) and Candida antarctica (B) (CALB) were immobilized on octyl-agarose beads at 1 mg/g (a loading under the capacity of the support) and by overloading the support with the enzymes. These biocatalysts were compared in their stabilities in 10 mM of sodium phosphate, HEPES, and Tris-HCl at pH 7. Lowly loaded CALB was more stable than highly loaded CALB preparation, while with TLL this effect was smaller. Phosphate was very negative for the stability of the CALB biocatalyst and moderately negative using TLL at both loadings. The stability of the enzymes in HEPES and Tris-HCl presented a different response as a function of the enzyme loading (e.g., using lowly loaded CALB, the stabilities were similar in both buffers, but it was clearly smaller in HEPES using the highly loaded biocatalysts). Moreover, the specific activity of the immobilized enzymes versus p-nitrophenol butyrate, triacetin and R- or S-methyl mandelate depended on the buffer, enzyme loading, and interaction between them. In some cases, almost twice the expected activity could be obtained using highly loaded octyl-CALB, depending on the buffer. A co-interaction between the effects on enzyme activity and the specificity of support enzyme loading and buffer nature was detected. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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29 pages, 9404 KiB

Open AccessArticle

Bioprocessing and Screening of Indigenous Wastes for Hyper Production of Fungal Lipase

by Usman Ali, Zahid Anwar, Shoaib Hasan, Muddassar Zafar, Noor ul Ain, Fareed Afzal, Waseem Khalid, Muhammad Abdul Rahim, Hanae Naceiri Mrabti, Ammar AL-Farga and Hamdi Abdel Rasool Abdelsamad Eljeam

Catalysts 2023, 13(5), 853; https://doi.org/10.3390/catal13050853 - 8 May 2023

Cited by 5 | Viewed by 2143

Abstract

Background: Lipase is one of the most important enzymes produced from microbial fermentation. Agricultural wastes are a good source of enzyme production because they are cost-effective and production rates are also higher. Method: In this study, eight lignolitic substrates were screened for lipase production. Results: Out of these substrates, guava leaves showed maximum activity of 9.1 U/mL from Aspergillus niger by using the solid-state fermentation method. Various factors such as temperature, pH, incubation period, moisture content, inoculum size, and substrate size that influence the growth of fungi were optimized by response surface methodology (RSM), and then characterization was performed. When all physical and nutritional parameters were optimized by RSM, the maximum lipase activity obtained was 12.52 U/mL after 4 days of incubation, at pH 8, 40 °C temperature, 3 mL inoculum size, 20% moisture content, and 6 g substrate concentration. The enzyme was partially purified through 70% ammonium sulfate precipitation. After purification, it showed 34.291 U/mg enzyme activity, increasing the purification fold to 1.3. The enzyme was then further purified by dialysis, and the purification fold increased to 1.83 having enzyme activity of 48.03 U/mg. Furthermore, activity was increased to 132.72 U/mg after column chromatography. A purification fold of 5.07 was obtained after all purification steps. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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16 pages, 2236 KiB

Open AccessEditor’s ChoiceArticle

β-Sitosterol Oleate Synthesis by Candida rugosa Lipase in a Solvent-Free Mini Reactor System: Free and Immobilized on Chitosan-Alginate Beads

by Adejanildo da S. Pereira, Jully L. Fraga, Camila P. L. Souza, Alexandre G. Torres and Priscilla F. F. Amaral

Catalysts 2023, 13(4), 780; https://doi.org/10.3390/catal13040780 - 21 Apr 2023

Cited by 2 | Viewed by 1796

Abstract

Candida rugosa lipase (CRL) was immobilized by the ionic gelling technique using alginate and chitosan as encapsulating agents. An immobilization yield of 99% and an immobilization efficiency of 51% were obtained. Maximum hydrolytic activity for free and immobilized CRL was detected at 40 °C and for synthesis activity at 35 °C. The optimum pH for immobilized and free CRL hydrolysis activity was 8.0. The V_max obtained for the hydrolysis reaction was higher for free CRL (4121.4 μmol/min/g) compared to immobilized CRL (2359.13 μmol/min/g). A Vmax of 2.24 μmol/min/g was detected for the synthetic activity of free CRL. The K_m obtained for the hydrolysis reaction was higher (660.02 μmol/L) for immobilized CRL than for free CRL (403.06 μmol/L). For the synthetic activity, a K_m of 234.44 μmol/L was calculated. The conversion of β-sitosterol oleate ranged from 80.85 to 96.84% for free CRL, higher than the maximum found for immobilized CRL (32%). The scale-up (scale factor: 50) with the free CRL was successfully performed, achieving a high conversion value (92%) in a 500 mL bioreactor. This conversion value was within the range predicted by the mathematical model obtained using mini reactors. These mini reactors are good models to test several conditions of enzyme reactions that are intended for large scales. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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15 pages, 3131 KiB

Open AccessArticle

Scale-Up Lipase Production and Development of Methanol Tolerant Whole-Cell Biocatalyst from Magnusiomyces spicifer SPB2 in Stirred-Tank Bioreactor and Its Application for Biodiesel Production

by Purimprat Srimhan and Tipparat Hongpattarakere

Catalysts 2023, 13(3), 617; https://doi.org/10.3390/catal13030617 - 20 Mar 2023

Cited by 3 | Viewed by 1899

Abstract

This study aimed to economically develop the yeast whole-cell biocatalyst from the lipase-secreting Magnusiomyces spicifer SPB2 to serve green biodiesel production. The scaled-up productions of lipases were optimized using a 5-L stirred-tank bioreactor. The maximum extracellular lipase and cell-bound lipase (CBL) yields of 1189.65 U/L and 5603.74 U/L were achieved at 24 h and 60 h, respectively, in the modified IMY medium (pH 5.0) containing 2% of soybean oil as a carbon source and 0.2% Gum Arabic as an emulsifying agent. The optimized cultivation was initiated with an inoculum size of 1 × 10⁷ cells/mL and conducted under an aeration rate of 0.75 vvm with an agitation speed of 400 rpm. The obtained whole-cell biocatalyst of M. spicifer SPB2 was applied to catalyze the transesterification reaction using palm oil and methanol as substrates. The greatest yield of 97.93% fatty acid methyl ester (FAME) was reached at 72 h using a palm oil/methanol ratio of 1:7, indicating high methanol stability of the biocatalyst. Moreover, substrate homogenization accelerated the reaction to achieve FAME production of 97.01% at 48 h and remained stable afterwards. Without homogenization, the highest FAME of 98.20% was obtained at 60 h. The whole-cell biocatalyst prepared from lipase-secreting M. spicifer SPB2 at an up-scaled level greatly enhanced efficiency and feasibility for commercial biodiesel production through a green conversion process. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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14 pages, 3003 KiB

Open AccessArticle

Bio-Based Materials versus Synthetic Polymers as a Support in Lipase Immobilization: Impact on Versatile Enzyme Activity

by Karina Jasińska, Bartłomiej Zieniuk, Urszula Jankiewicz and Agata Fabiszewska

Catalysts 2023, 13(2), 395; https://doi.org/10.3390/catal13020395 - 11 Feb 2023

Cited by 8 | Viewed by 2191

Abstract

To improve enzyme stability, the immobilization process is often applied. The choice of a support on which the enzymes are adsorbed plays a major role in enhancing biocatalysts’ properties. In this study, bio-based (i.e., chitosan, coffee grounds) and synthetic (i.e., Lewatit VP OC 1600) supports were used in the immobilization of lipases of various microbial origins (yeast (Yarrowia lipolytica) and mold (Aspergillus oryzae)). The results confirmed that the enzyme proteins had been adsorbed on the surface of the selected carriers, but not all of them revealed comparably high catalytic activity. Immobilized CALB (Novozym 435) was used as a commercial reference biocatalyst. The best hydrolytic activity (higher than that of CALB) was observed for Novozym 51032 (lipase solution of A. oryzae) immobilized on Lewatit VP OC 1600. In terms of synthetic activity, there were only slight differences between the applied carriers for A. oryzae lipase, and the highest measures were obtained for coffee grounds. All of the biocatalysts had significantly lower activity in the synthesis reactions than the reference catalyst. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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15 pages, 1862 KiB

Open AccessArticle

Lipase Production by Yarrowia lipolytica in Solid-State Fermentation Using Amazon Fruit By-Products and Soybean Meal as Substrate

by Aparecida Selsiane Sousa Carvalho, Júlio Cesar Soares Sales, Felipe Valle do Nascimento, Bernardo Dias Ribeiro, Carlos Eduardo Conceição de Souza, Ailton Cesar Lemes and Maria Alice Zarur Coelho

Catalysts 2023, 13(2), 289; https://doi.org/10.3390/catal13020289 - 27 Jan 2023

Cited by 9 | Viewed by 4506

Abstract

The production of polyunsaturated fatty acids from fish oil, which is related to various health benefits including effects against cardiovascular diseases, antihypertensive, anticancer, antioxidant, antidepression, anti-aging, and anti-arthritis effects, among others, can be advantageously performed through the application of lipase. However, the high cost associated with enzyme production can make the process unfeasible and thus alternative substrates should be investigated to solve these problems. This research aimed to produce lipase by Yarrowia lipolytica IMUFRJ50682 in solid-state fermentation using by-products of the food processing industry (andiroba oil cake and soybean meal) and verify the potential application in the initial hydrolysis of fish oil to further produce polyunsaturated fatty acids in a suitable process. A screening was carried out for the analysis of andiroba oil cake and soybean meal combinations in different proportions (0:100 to 100:0, respectively) at 48 h of the fermentation process. Afterward, the solid matrix composed by soybean meal and andiroba oil cake was supplemented with soy oil and Tween 80 to improve the lipase activity. The enzymatic extract was characterized in relation to the protein profile by electrophoresis. Finally, the enzymatic extract and the solid biocatalyst produced were applied to evaluate the potential hydrolysis of the fish oil in an initial study. Maximum lipolytic activity (63.7 U·g⁻¹) was achieved using andiroba oil cake and soybean meal (50:50) after 24 h of fermentation. Soybean oil 1.5% and Tween 80 (0.001%) in an emulsion provided an increase of 1.5-fold (82.52 U·g⁻¹) in the enzyme activity. The electrophoretic analysis demonstrated a band between 37 and 40 kDa that may be related to lipase and a band of 75 kDa referring to the α subunit of the β-conglycinin present in soybean meal. After 48 h, the solid biocatalyst showed a higher degree of hydrolysis (DH) (71.0%) than the enzymatic extract (61.5%). The solid biocatalyst was stable during storage at room temperature for 7 months. The production of lipases using Amazon fruit by-product and soybean meal in solid-state fermentation is viable as well as the application of the extract and solid biocatalyst in the initial application for the hydrolysis of fish oil to further produce polyunsaturated fatty acids in an industrially suited process. Full article

(This article belongs to the Special Issue Lipase: A Multi-Purpose Biocatalyst at the Forefront of Biotechnology)

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