Enhancing the stability of a carboxylesterase by entrapment in chitosan coated alginate beads

Abstract

Introduction Esterases are hydrolytic enzymes that cleave ester bonds, liberating alcohol and carboxylic acid (E.C 3.1.1.1). They have a wide range of applications in food processing, beverages, and perfume industries (Panda and Gowrishankar, 2005). Microorganisms produce different types of esterases, and are unique in catalyzing specific reactions. For example, arylesterase obtained from Saccharomyces cerevisiae is used for enhancing flavor in alcoholic beverages (Lomolino et al., 2003). Similarly sterol esterases isolated from Pseudomonas sp., Chromobacterium, and Ophiostoma picea are used by the paper industry to reduce problems of pitch during paper making (Kontkanen et al., 2004). The genus Aeromonas is ubiquitous in the environment; they are found in fresh water, drinking water, and saline water. Cold-adapted lipases have been isolated from Aeromonas LPB4 from deep sea sediments and A. hydrophila from food products (Soltan et al., 2016). Immobilized enzymes are preferred over free enzyme because they can be used for many reaction cycles and can be separated easily from the final product. Immobilization leads to conformational changes in the enzyme thus altering many of its properties and can lead to enhanced activity and stability (Mateo et al., 2007). Enzyme immobilization by entrapment is a technique by which the free enzyme is secured in a semipermeable support material, and this prevents the enzyme from diffusing while allowing substrates and products to pass through freely (Won et al., 2005). These support materials can be natural polymers such as cellulose, agar, chitin, alginate, dextrans, or synthetic polymers, such as polystyrene, polyacrylate, polymethacrylate, vinyl, and allyl polymers. Recently, a silica based solid binding peptide was used as a support material for the immobilization of hemicellulase enzyme. The immobilized enzyme was used for the catalysis of simple and complex polysaccharides (Care et al., 2017). Amongst all the polymers mentioned, alginate is the most commonly used due to its thermostability and nontoxicity. A type of esterase (lipase B) obtained from Candida antarctica was immobilized on chitosan-alginate complex, which was functionalized by a few covalent modifications. The immobilized enzyme was used for the synthesis of butyl oleate (Silva et al., 2011). Alginates are commercially available as sodium alginate. Alginate is a

Preparation of immobilized arylsulfatase on magnetic Fe3O4 nanoparticles and its application for agar quality improvement

“…This decrease in V max might be attributed to limited accessibility of substrate molecules to the active sites of the enzyme and the interaction of the enzymes with the functional groups on the surface of beads or large areas of contact between enzyme and support (Keerti et al., 2014 ). Similar observations about the changes of apparent K m and V max values of immobilized enzyme have been reported in some other studies (Hassan et al., 2019 ; Raghu & Pennathur, 2018 ).…”

The synergistic effect of chitosan-alginate nanoparticle loaded with doxycycline antibiotic against multidrug resist enterobacteriaceae

“…The N-H deformation band of chitosan was found at 1,564 cm -1 [50]. Stretching vibrations of C-H bond at 2715 cm -1 indicated the presence of aliphatic groups [51]. The bands at1100-1000 cm -1 is due to the saccharide structure of the chitosan [52], as illustrated in Figure-11.…”

Immobilization of Providencia stuartii Cells in Pumice Stone and Its Application for N-Acetylglucosamine Production

“…It is also higher than other research using alginate beads to immobilize chitosan, i.e. about 74% ( 34 ), calcium agar beads and agar beads to immobilize α-amylase, i.e. 80 and 63.83%, respectively ( 35 ).…”