Characterization of a recombinant Aspergillus niger GZUF36 lipase immobilized by ionic liquid modification strategy.

Enzyme immobilized on magnetic nanomaterials is a promising biocatalyst with efficient recovery under applied magnets. In this study, a recombinant extracellular lipase from Aspergillus niger GZUF36 (PEXANL1) expressed in Pichia pastoris GS115 was immobilized on ionic liquid-modified magnetic nano ferric oxide (FeO@SiO@ILs) via electrostatic and hydrophobic interaction. The morphology, structure, and properties of FeO@SiO@ILs and immobilized PEXANL1 were characterized by scanning electron microscopy, Fourier transform infrared spectroscopy, x-ray diffraction, vibration sample magnetometer, and zeta potential analysis.

Adsorption-precipitation-cross-linking immobilization of GDSL-type esterase from Aspergillus niger GZUF36 by polydopamine-modified magnetic clarity tetroxide nanocouplings and its enzymatic characterization.

Recombinant INANE1 (rINANE1), a recombinant intracellular GDSL-type esterase from Aspergillus niger GZUF36, has high acetate substrate specificity. Here, rINANE1 was successfully immobilized on polydopamine (PDA)-modified magnetic ferric oxide nanoparticles (FeONPs) by adsorption-precipitation-cross-linking to obtain cross-linked enzyme aggregate (CLEA)-rINANE1-FeO@PDA. FeO, FeO@PDA, and CLEA-rINANE1-FeO@PDA were characterized by scanning electron microscopy, X-ray diffraction, vibrating-sample magnetometry, Fourier transform infrared (FTIR) spectroscopy, and zeta potential analysis.

Characterization, High-Density Fermentation, and the Production of a Directed Vat Set Starter of Used in the Food Industry: A Review.

have been widely concerned for decades. Bacteria of the genus have been commonly employed in fermented food to improve the appearance, smell, and taste of food or prolong its shelf-life. They comprise 261 species (by March 2020) that are highly diverse at the phenotypic, ecological, and genotypic levels.

Gene Expression, Biochemical Characterization of a sn-1, 3 Extracellular Lipase From GZUF36 and Its Model-Structure Analysis.

In this study, a sn-1, 3 extracellular lipases from GZUF36 (PEXANL1) was expressed in , characterized, and the predicted structural model was analyzed. The optimized culture conditions of showed that the highest lipase activity of 66.5 ± 1.

Purification, characterization, and chemical modification of Bacillus velezensis SN-14 fibrinolytic enzyme.

Fermented bean foods are a crucial source of fibrinolytic enzymes. The presented study aimed to purify, characterize, and chemically modify Bacillus velezensis SN-14 fibrinolytic enzyme. The fibrinolytic enzyme was purified using CTAB/isooctane/hexyl alcohol/n-butyl alcohol reverse micellar system, and the purified enzyme was chemically modified to improve its enzymatic activity and stability.

Effect of cross-linked enzyme aggregate strategy on characterization of sn-1,3 extracellular lipase from Aspergillus niger GZUF36.

The sn-1,3 extracellular lipase from Aspergillus niger GZUF36 (EXANL1) has important potential applications. The cross-linked enzyme aggregate (CLEA) of purified EXANL1 (CLEA-EXANL1) achieved optimum activity recovery (148.5 ± 0.

Gene cloning, expression, purification and characterization of a sn-1,3 extracellular lipase from GZUF36.

Sn-1,3 extracellular GZUF36 lipase (EXANL1) has wide application potential in the food industry. However, the strain has defects such as easy degradation and instability in the expression of sn-1,3 lipase. To obtain a stable expression of this lipase and its subsequent enzymatic properties, the gene encoding EXANL1 was cloned and expressed in BL21 (DE3) cells using pET-28a as the expression vector.

Influence of different parameters on reverse micelle extraction combined with acetone precipitation to purify sn-1,3 extracellular lipase from GZUF36.

There are few reports on the feasibility of combined reverse micelle extraction and acetone precipitation to obtain electrophoretic pure enzymes. We aimed to purify a sn-1,3 extracellular lipase from a novel GZUF36 through this combination in this work. This lipase preliminarily purified by controlling the volume ratio (1:2.