SemOpenAlex |

SemOpenAlex

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4285174476> ?p ?o ?g. }

Showing items 1 to 74 of 74 with 100 items per page.

W4285174476 endingPage "143" @default.
W4285174476 startingPage "143" @default.
W4285174476 abstract "Background and objective Lipases (triacylglycerol acylhydrolase, EC. 3.1.1.3) belong to a class of hydrolases that are specific for the hydrolysis of fats into fatty acids and glycerol that have much application in different industrial processes. Fungi, yeast, and bacteria have been reported to be sources of lipase. There are many immobilized methods for enzyme, and the commonly used methods are physical adsorption, entrapment, and cross-linkage. This study aimed to evaluate lipase production by Aspergillus niger NRRL-599 in solid cultivation using agro-industrial waste as a substrate. Partial purification of the crude enzyme and its characterization and immobilization using nanoparticles were carried out. The potential application of the immobilized and partially purified enzyme was also studied in the field of textile.Materials and methods Partially purified A. niger NRRL-599 lipase was immobilized by physical adsorption onto modified titanium dioxide nanoparticles using gelatin and palmitic acid binders and characterized by transmission electron microscopy, dynamic light scattering, and Fourier-transform infrared.Results and conclusion In our study, lipase produced by A. niger NRRL-599 was partially purified by ammonium sulfate at 60% saturation and immobilized on gelatin-coated titanium dioxide. Comparison between the properties of the free and the immobilized A. niger NRRL-599 lipase forms was carried out. The optimum pH was 9.0 and 10.0 for the free and immobilized forms, respectively. The half-life of the soluble-free lipase at 50 and 55°C was 17.3 and 23.1 min, respectively, whereas for the immobilized form was 23.1 and 34.6 min, respectively. At 50 and 55°C, the deactivation rate constants (kD) for soluble lipase were 6.6×10−3 and 5×10−3, respectively, and 6.6×10−3 and 3.3×10−3, respectively, for immobilized lipase. The Km was 11.11 and 12.5 mM for the immobilized and free forms, respectively. The Vmax was 416.6 U/mg protein and 296.3 U/mg protein for immobilized and free lipase forms, respectively. This confirms that the apparent affinity toward the substrate increases by immobilization. Partially purified lipase and immobilized enzymes were used in the textiles in the treatment of wool fibers before dying to improve the color strength." @default.
W4285174476 created "2022-07-14" @default.
W4285174476 creator A5003158454 @default.
W4285174476 creator A5017751078 @default.
W4285174476 creator A5044671282 @default.
W4285174476 creator A5048364502 @default.
W4285174476 creator A5056540430 @default.
W4285174476 creator A5071802886 @default.
W4285174476 creator A5075045488 @default.
W4285174476 date "2022-01-01" @default.
W4285174476 modified "2023-10-18" @default.
W4285174476 title "Comparative studies of free and immobilized partially purified lipase from Aspergillus niger NRRL-599 produced from solid-state fermentation using gelatin-coated titanium nanoparticles and its application in textile industry" @default.
W4285174476 cites W2965920689 @default.
W4285174476 doi "https://doi.org/10.4103/epj.epj_90_21" @default.
W4285174476 hasPublicationYear "2022" @default.
W4285174476 type Work @default.
W4285174476 citedByCount "1" @default.
W4285174476 countsByYear W42851744762023 @default.
W4285174476 crossrefType "journal-article" @default.
W4285174476 hasAuthorship W4285174476A5003158454 @default.
W4285174476 hasAuthorship W4285174476A5017751078 @default.
W4285174476 hasAuthorship W4285174476A5044671282 @default.
W4285174476 hasAuthorship W4285174476A5048364502 @default.
W4285174476 hasAuthorship W4285174476A5056540430 @default.
W4285174476 hasAuthorship W4285174476A5071802886 @default.
W4285174476 hasAuthorship W4285174476A5075045488 @default.
W4285174476 hasConcept C100544194 @default.
W4285174476 hasConcept C13965031 @default.
W4285174476 hasConcept C150394285 @default.
W4285174476 hasConcept C178790620 @default.
W4285174476 hasConcept C181199279 @default.
W4285174476 hasConcept C185592680 @default.
W4285174476 hasConcept C2775960407 @default.
W4285174476 hasConcept C2778823387 @default.
W4285174476 hasConcept C2779697368 @default.
W4285174476 hasConcept C2779942233 @default.
W4285174476 hasConcept C33633552 @default.
W4285174476 hasConcept C43617362 @default.
W4285174476 hasConcept C55493867 @default.
W4285174476 hasConcept C94412978 @default.
W4285174476 hasConceptScore W4285174476C100544194 @default.
W4285174476 hasConceptScore W4285174476C13965031 @default.
W4285174476 hasConceptScore W4285174476C150394285 @default.
W4285174476 hasConceptScore W4285174476C178790620 @default.
W4285174476 hasConceptScore W4285174476C181199279 @default.
W4285174476 hasConceptScore W4285174476C185592680 @default.
W4285174476 hasConceptScore W4285174476C2775960407 @default.
W4285174476 hasConceptScore W4285174476C2778823387 @default.
W4285174476 hasConceptScore W4285174476C2779697368 @default.
W4285174476 hasConceptScore W4285174476C2779942233 @default.
W4285174476 hasConceptScore W4285174476C33633552 @default.
W4285174476 hasConceptScore W4285174476C43617362 @default.
W4285174476 hasConceptScore W4285174476C55493867 @default.
W4285174476 hasConceptScore W4285174476C94412978 @default.
W4285174476 hasIssue "2" @default.
W4285174476 hasLocation W42851744761 @default.
W4285174476 hasOpenAccess W4285174476 @default.
W4285174476 hasPrimaryLocation W42851744761 @default.
W4285174476 hasRelatedWork W2007269833 @default.
W4285174476 hasRelatedWork W2018754081 @default.
W4285174476 hasRelatedWork W2019155956 @default.
W4285174476 hasRelatedWork W2054183208 @default.
W4285174476 hasRelatedWork W2122314920 @default.
W4285174476 hasRelatedWork W2135864793 @default.
W4285174476 hasRelatedWork W2340131720 @default.
W4285174476 hasRelatedWork W2377902424 @default.
W4285174476 hasRelatedWork W2386698984 @default.
W4285174476 hasRelatedWork W2388731426 @default.
W4285174476 hasVolume "21" @default.
W4285174476 isParatext "false" @default.
W4285174476 isRetracted "false" @default.
W4285174476 workType "article" @default.