Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics

Abstract

Ulocladium atrum inulinase was immobilized on different composite membranes composed of chitosan/nonwoven fabrics. Km values of free and immobilized U. atrum inulinase on different composite membranes were calculated. The enzyme had optimum pH at 5.6 for free and immobilized U. atrum inulinase on polyester nonwoven fabric coated with 3 percent chitosan solution (PPNWF3), but optimum pH was 5 for immobilized U. atrum inulinase on polyester and polypropylene nonwoven fabrics coated with 1 percent chitosan solution. The enzyme had optimum temperature at 40 degree C for immobilized enzyme on each of polyester and polypropylene composite membranes coated with 1 percent chitosan, while it was 50 degree C for free and immobilized enzyme on polypropylene nonwoven fabric coated with 3 percent chitosan solution. Free U. atrum inulinase was stable at 40 degree C but thermal stability of the immobilized enzyme was detected up to 60 degree C. Reusability of immobilized enzyme was from 38 to 42 cycles of reuse; after this, the immobilized enzyme lost its activity completely. In conclusion, immobilized U. atrum inulinase was considerably more stable than the free enzyme, and could be stored for extended periods.

Exo‐inulinase production from Aspergillus fumigatus NFCCI 2426: purification, characterization, and immobilization for continuous fructose production

“…The increase in K m after immobilization was probably due to the mass transfer resistance to the substrate into the polymer matrix, and effect of the increasing degree of polymerization of substrate caused increase in this value (Abdel-Naby et al, 1999;Curcio et al, 2014;Kusano et al, 1989;Mazutti et al, 2007). Higher V max observed for the immobilized enzyme was rather unusual; however, such increase has been observed in case of immobilized inulinase (Calixto-Romo et al, 2008;Mohamed et al, 2014;Risso et al, 2010). According to Ahmed et al (2019), increased reaction velocities are observed probably due to the configurational modifications on enzyme after interacting with the matrix and molecular flocking caused by immobilization.…”

Inulin Hydrolysis by Immobilized Inulinase on Functionalized Magnetic Nanoparticles Using Soy Protein Isolate and Bovine Serum Albumin

“…One of the most important health benefits of fructose as a sweetener is its insulin‐independent metabolism, which makes it a sugar for diabetic patients. It has low carcinogenicity, raises iron absorption and zinc in children, and enhances the flavor, color, and product stability in food and beverages . Fructose in crystalline form is about 1.8 and 2.3 times sweeter than the table sugar sucrose and glucose, respectively .…”

“…It has low carcinogenicity, raises iron absorption and zinc in children, and enhances the flavor, color, and product stability in food and beverages . Fructose in crystalline form is about 1.8 and 2.3 times sweeter than the table sugar sucrose and glucose, respectively . Inulin is a polysaccharide consisting of linear b‐2,1 linked polyfructose units, which are responsible for its nutritional characteristics and are known to be perfect sources of fructose and high fructose syrup (HFS) .…”

The assisting-approach of horseradish peroxidase immobilized onto amine-functionalized superparamagnetic iron oxide nanoparticles as a biocatalyst

“…In each succeeding reaction cycle, the percentage of relative activity was calculated using the ratio of the enzyme activity to the rst reaction cycle. The important advantages of the use of an immobilized biocatalyst are increased stability and easy separation of the bound peroxidase during washes (Mohamed et al 2014 11. This result will return to the Fenton reaction mechanism (Pereira et al 2012).…”