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1.
Foods ; 12(16)2023 Aug 15.
Article in English | MEDLINE | ID: mdl-37628057

ABSTRACT

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.

2.
Food Technol Biotechnol ; 59(3): 306-313, 2021 Sep.
Article in English | MEDLINE | ID: mdl-34759762

ABSTRACT

RESEARCH BACKGROUND: Microbial ß-fructofuranosidases are widely employed in food industry to produce inverted sugar or fructooligosaccharides. In this study, a newly isolated Aspergillus carbonarius PC-4 strain was used to optimize the ß-fructofuranosidase production in a cost-effective process and the sucrose hydrolysis was evaluated to produce inverted sugars. EXPERIMENTAL APPROACH: Optimization of nutritional components of culture medium was carried out using simplex lattice mixture design for 72 and 120 h at 28 °C. One-factor-at-a-time methodology was used to optimize the physicochemical parameters. Crude enzyme was used for sucrose hydrolysis at different concentrations. RESULTS AND CONCLUSIONS: The optimized conditions of enzyme production were achieved from cultivations containing pineapple crown waste (1.3%, m/V) and yeast extract (0.3%, m/V) after 72 h with an enzyme activity of 9.4 U/mL, obtaining R2=91.85%, R2 adjusted=85.06%, highest F-value (13.52) and low p-value (0.003). One-factor-at-a-time used for optimizing the physicochemical conditions showed optimum temperature (20 °C), pH (5.5), agitation (180 rpm) and time course (72 h) with a 3-fold increase of enzyme production. The invertase-induced sucrose hydrolysis showed the maximum yield (3.45 mmol of reducing sugars) using 10% of initial sucrose concentration. Higher sucrose concentrations caused the inhibition of invertase activity, possibly due to the saturation of substrate or formation of sucrose aggregates, making it difficult for the enzyme to access sucrose molecules within the created clusters. Therefore, a cost-effective method was developed for the invertase production using agroindustrial waste and the produced enzyme can be used efficiently for inverted sugar production at high sucrose concentration. NOVELTY AND SCIENTIFIC CONTRIBUTION: This study presents an efficient utilization of pineapple crown waste to produce invertase by a newly isolated Aspergillus carbonarius PC-4 strain. This enzyme exhibited a good potential for inverted sugar production at high initial sucrose concentration, which is interesting for industrial applications.

3.
Biotechnol Lett ; 43(1): 43-59, 2021 Jan.
Article in English | MEDLINE | ID: mdl-33025334

ABSTRACT

OBJECTIVE: Extracellular fructosyltransferase (FTase, E.C.2.4.1.9) from Aspergillus oryzae IPT-301 was immobilized on silica gel by adsorption and biochemically characterized aiming at its application in the transfructosylation reaction of sucrose for the production of fructooligossaccarides (FOS). RESULTS: The transfructosylation activity (AT) was maximized by the experimental design in function of the reaction pHs and temperatures. The AT of the immobilized enzyme showed the kinetics behavior described by the Hill model. The immobilized FTase showed reuse capacity for six consecutive reaction cycles and higher pH and thermal stability than the soluble enzyme. CONCLUSION: These results suggest a high potential of application of silica gel as support for FTase immobilization aiming at FOS production.


Subject(s)
Aspergillus oryzae/enzymology , Bacterial Proteins , Enzymes, Immobilized , Hexosyltransferases , Oligosaccharides/metabolism , Bacterial Proteins/chemistry , Bacterial Proteins/metabolism , Enzyme Stability , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Hexosyltransferases/chemistry , Hexosyltransferases/metabolism , Hydrogen-Ion Concentration , Oligosaccharides/analysis , Silica Gel/chemistry , Sucrose/metabolism , Temperature
4.
Biotechnol Lett ; 42(12): 2619-2629, 2020 Dec.
Article in English | MEDLINE | ID: mdl-32979133

ABSTRACT

OBJECTIVE: Fructooligosaccharides (FOS) are prebiotic substances that have been extensively incorporated in different products of food industry mostly for their bifidogenic properties and economic value. The main commercial FOS production comes from the biotransformation of sucrose and intracellular and extracellular microbial enzymes-fructosyltransferases (FTase). Aspergillus oryzae IPT-301 produces FTase. In order to increase its production, this study focuses on evaluating the effects of different agitation speed and aeration rates which affect yields in a stirred tank bioreactor. RESULTS: Agitation had more influence on cell growth than aeration. The maximum intracellular FTase activity and the volumetric productivity of total intracellular FTase were obtained at 800 rpm and 0.75 vvm, and reached values of 2100 U g-1 and 667 U dm-3 h-1, respectively. The agitation speed had a strong influence on the activity of extracellular FTase produced which reached the maximum amount of 53 U cm-3. The higher value of total activity obtained was 22,831 U dm-3 at 0.75 vvm and 800 rpm. CONCLUSION: Aeration rates and agitation speed showed strong influence upon the growth and production of fructosyltransferase from Aspergillus oryzae IPT-301 in media containing sucrose as carbon source. The control of aeration rate and agitation speed can be a valuable fermentation strategy to improve enzyme production.


Subject(s)
Bioreactors , Culture Media/chemistry , Hexosyltransferases/biosynthesis , Oligosaccharides/chemistry , Aspergillus oryzae/chemistry , Aspergillus oryzae/enzymology , Carbon/chemistry , Fermentation , Hexosyltransferases/chemistry , Sucrose/chemistry
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