This study reports the preparation of silica-coated and nano-fructosome encapsulated lipase B particles (CalB@NF@SiO) and a demonstration of their enzymatic hydrolysis and acylation. CalB@NF@SiO particles were prepared as a function of TEOS concentration (3-100 mM). Their mean particle size was 185 nm by TEM. Enzymatic hydrolysis was performed to compare catalytic efficiencies of CalB@NF and CalB@NF@SiO. The catalytic constants (K, V, and K) of CalB@NF and CalB@NF@SiO were calculated using the Michaelis-Menten equation and Lineweaver-Burk plot. Optimal stability of CalB@NF@SiO was found at pH 8 and a temperature of 35 °C. Moreover, CalB@NF@SiO particles were reused for seven cycles to evaluate their reusability. In addition, enzymatic synthesis of benzyl benzoate was demonstrated via an acylation reaction with benzoic anhydride. The efficiency of CalB@NF@SiO for converting benzoic anhydride to benzyl benzoate by the acylation reaction was 97%, indicating that benzoic anhydride was almost completely converted to benzyl benzoate. Consequently, CalB@NF@SiO particles are better than CalB@NF particles for enzymatic synthesis. In addition, they are reusable with high stability at optimal pH and temperature.
β-Glucosidase plays a pivotal role in transforming ginsenosides into specific minor ginsenosides. In this study, total ginsenosides from Panax notoginseng leaves were used as substrates to stimulate the growth of Aspergillus niger NG1306. Transcriptome analysis identified a β-glucosidase gene, Anglu04478 (1455 bp, 484 amino acids, 54.
β-glucosidases (BGLs) are key enzymes in the depolymerization of cellulosic biomass, catalyzing the conversion of cello-oligosaccharides into glucose. This conversion is pivotal for enhancing the production of second-generation ethanol or other value-added products in biorefineries. However, the process is often cost-prohibitive due to the high enzyme loadings required.
Laboratory of Biochemistry and Molecular Genetics, Faculty of Sciences and Technology of Tangier, Abdelmalek Essaadi University, 90000, Tetouan, Morocco.
Marine sulfated polysaccharides constitute a class of bioactive polymers commonly found in cell walls of macroalgae. Among these macromolecular substances, fucoidans, ulvans, and carrageenans have attracted considerable attention providing interesting therapeutic properties affected by a combination of various structural factors, such as sulfation pattern, molecular weight, monosaccharide composition, and glycosidic linkages. Remarkably, chemical modification, enzymatic hydrolysis and crosslinking are promising approaches for developing the application of these polysaccharides through enhancement and/or addition of new biological properties.
To prepare dual-functional seasoning ingredients with a salty-umami taste, five proteases were applied to hydrolyze proteins, preparing enzymatic hydrolysates. Their taste compounds along with the salty-umami taste, were investigated. The results revealed that enzymatic hydrolysis facilitated the release of taste compounds from .
The quality issues of ultra-high-temperature (UHT) milk, such as protein hydrolysis and aging gels throughout shelf life, are caused by proteases from psychrophilic bacteria. However, existing enzyme activity detection techniques have low sensitivity and cannot accomplish the detection of product deterioration caused by low enzyme activity. In this study, an attempt was made to analyze the relationship between enzymatically cleaved peptides and product quality using peptidomics techniques.
