Influence of different immobilization techniques to improve the enantioselectivity of lipase from Geotrichum candidum applied on the resolution of mandelic acid

Júnior, Wilson Galvão de Morais; Maia, Ariel Moura; Martins, Pedro Alves; Fernández‐Lorente, Gloria; Guisán, José M.; Pessela, Benevides C.

doi:10.1016/j.mcat.2018.07.024

Cited by 10 publications

(5 citation statements)

References 46 publications

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“…Immobilized enzymes are more robust, show higher stability, and are easier to handle compared to their soluble forms. They are also easily recovered/recycled after use [ 78 , 84 , 85 , 86 , 87 , 88 ].…”

Section: The Impact Of Enzyme Immobilization On Industrial Processesmentioning

confidence: 99%

“…Lipase immobilization techniques have been the subject of several studies developed over the years [ 6 , 13 , 16 , 81 , 82 , 83 , 84 , 95 , 96 , 97 , 98 ]. These techniques improve recyclability, stability, and enzymatic activity, impacting market productivity and profitability.…”

Section: The Impact Of Enzyme Immobilization On Industrial Processesmentioning

confidence: 99%

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Trends in the Use of Lipases: A Systematic Review and Bibliometric Analysis

Santos

Vieira

Almeida

et al. 2023

Foods

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Scientific mapping using bibliometric data network analysis was applied to analyze research works related to lipases and their industrial applications, evaluating the current state of research, challenges, and opportunities in the use of these biocatalysts, based on the evaluation of a large number of publications on the topic, allowing a comprehensive systematic data analysis, which had not yet been conducted in relation to studies specifically covering lipases and their industrial applications. Thus, studies involving lipase enzymes published from 2018 to 2022 were accessed from the Web of Science database. The extracted records result in the analysis of terms of bibliographic compatibility among the articles, co-occurrence of keywords, and co-citation of journals using the VOSviewer algorithm in the construction of bibliometric maps. This systematic review analysis of 357 documents, including original and review articles, revealed studies inspired by lipase enzymes in the research period, showing that the development of research, together with different areas of knowledge, presents good results related to the applications of lipases, due to information synchronization. Furthermore, this review showed the main challenges in lipase applications regarding increased production and operational stability; establishing well-defined evaluation criteria, such as cultivation conditions, activity, biocatalyst stability, type of support and reactor; thermodynamic studies; reuse cycles; and it can assist in defining goals for the development of successful large-scale applications, showing several points for improvement of future studies on lipase enzymes.

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Section: The Impact Of Enzyme Immobilization On Industrial Processesmentioning

confidence: 99%

Section: The Impact Of Enzyme Immobilization On Industrial Processesmentioning

confidence: 99%

Trends in the Use of Lipases: A Systematic Review and Bibliometric Analysis

Santos

Vieira

Almeida

et al. 2023

Foods

View full text Add to dashboard Cite

show abstract

“…Moreover, administration of endo-β-N-acetylglucosaminidase showed that these lipases are glycosylated, and beyond their high homology, they have different substrate specificity [ 107 ]. Furthermore, chemically modified to contain more amino groups, surface lipase produced by G. candidum (GCL) indicated faster and easiest immobilization on carboxymethyl and sulfopropyl agarose-based supports [ 107 , 108 ]. Administration of the ionic derivatives into fish oil resulted in increased hydrolysis and production of a high yield of Omega-3 polyunsaturated fatty acids (6.65 U and 7.85 U per gram of support of carboxymethyl derivative and sulfopropyl derivative, respectively) [ 107 ].…”

Section: Production Of Enzymes With Industrial Interestmentioning

confidence: 99%

Uncovering the Biotechnological Importance of Geotrichum candidum

Kamilari

Stanton

Reen

et al. 2023

Foods

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Fungi make a fundamental contribution to several biotechnological processes, including brewing, winemaking, and the production of enzymes, organic acids, alcohols, antibiotics, and pharmaceuticals. The present review explores the biotechnological importance of the filamentous yeast-like fungus Geotrichum candidum, a ubiquitous species known for its use as a starter in the dairy industry. To uncover G. candidum’s biotechnological role, we performed a search for related work through the scientific indexing internet services, Web of Science and Google Scholar. The following query was used: Geotrichum candidum, producing about 6500 scientific papers from 2017 to 2022. From these, approximately 150 that were associated with industrial applications of G. candidum were selected. Our analysis revealed that apart from its role as a starter in the dairy and brewing industries, this species has been administered as a probiotic nutritional supplement in fish, indicating improvements in developmental and immunological parameters. Strains of this species produce a plethora of biotechnologically important enzymes, including cellulases, β-glucanases, xylanases, lipases, proteases, and α-amylases. Moreover, strains that produce antimicrobial compounds and that are capable of bioremediation were identified. The findings of the present review demonstrate the importance of G. candidum for agrifood- and bio-industries and provide further insights into its potential future biotechnological roles.

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“…Moreover, enzyme activity, selectivity, specificity, and inhibition may be tuned, and in some instances, convert an apparently inefficient enzyme into a very effective one [82][83][84]. The use of immobilization techniques to improve the enzyme specificity and selectivity has been reported in many instances [91][92][93][94][95][96][97][98][99][100][101][102][103][104].…”

Section: Introductionmentioning

confidence: 99%

Tuning Almond Lipase Features by Using Different Immobilization Supports

Cherni,

Carballares,

Siar

et al. 2024

Catalysts

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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.

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Influence of different immobilization techniques to improve the enantioselectivity of lipase from Geotrichum candidum applied on the resolution of mandelic acid

Cited by 10 publications

References 46 publications

Trends in the Use of Lipases: A Systematic Review and Bibliometric Analysis

Trends in the Use of Lipases: A Systematic Review and Bibliometric Analysis

Uncovering the Biotechnological Importance of Geotrichum candidum

Tuning Almond Lipase Features by Using Different Immobilization Supports

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