A5061551250- Enzyme Production and Characterization
- Enzyme Catalysis and Immobilization
- Microbial Metabolites in Food Biotechnology
- Carbohydrate Chemistry and Synthesis
- Digestive system and related health
- Microbial Metabolic Engineering and Bioproduction
- Glycosylation and Glycoproteins Research
- Plant biochemistry and biosynthesis
- Pharmacogenetics and Drug Metabolism
- Enterobacteriaceae and Cronobacter Research
- Mycorrhizal Fungi and Plant Interactions
- Actinomycetales infections and treatment
- Microbial Natural Products and Biosynthesis
- Pancreatic function and diabetes
- Diverticular Disease and Complications
- Chemical synthesis and alkaloids
- Diet, Metabolism, and Disease
- Steroid Chemistry and Biochemistry
- Phytochemistry and Bioactivity Studies
- Lysosomal Storage Disorders Research
- Gut microbiota and health
Slovak University of Technology in Bratislava
2009-2024
Czech Academy of Sciences, Institute of Biotechnology
2015-2016
Fungal β-galactosidase from Aspergillus oryzae was immobilized into polyvinylalcohol (PVA) hydrogel by LentiKats® technology and used for the production of short-chain alkyl glycosides. Ethyl- propyl-β-d-galactopyranosides were prepared lactose (100 g/L) varying initial amounts alcohol (10–30% v/v) at 40 °C pH 4.5. The entrapped preserved 50% transgalactosylation activity after 25 repeated cycles in ethyl β-d-galactopyranoside. When 5% (v/v) propanol as an acceptor, enzyme (30–32 U/g enzyme)...
Abstract Three different fungal b-galactosidases, from three commercial sources, were studied for their capacity to produce galacto-oligosaccharides by trans-galactosylation lactose. The enzymes investigated in a soluble form the GOS production at two concentrations of lactose (10 % and 30 w/w). maximum concentration (70.9 g · L -1 ) was obtained initial (pH 4.5, temperature ℃) second hour enzyme reaction. yield (24 w/w) not significantly affected process immobilisation comparison with free...
The application of immobilized enzymes often plays a key role in successfully implementing an economically feasible biocatalytic process at industrial scale. Designing biocatalyst involves solving several tasks, from the selection carrier and immobilization method to characterization kinetic properties enzyme. In this study, we focused on free ß-N-acetylhexosaminidase (Hex), promising enzyme for field biotechnology, especially synthesis bioactive carbohydrates. Hex was via covalent binding...
α-Nitrophenyl derivatives of glycosides are convenient substrates used to detect and characterize α-N-acetylgalactosaminidase. A new procedure combining chemical biocatalytic steps was developed prepare 4-nitrophenyl-2-acetamido-2-deoxy-α-D-galactopyranoside (4NP-α-GalNAc). The α-anomer prepared through synthesis an anomeric mixture followed by selective removal the β-anomer using specific enzymatic hydrolysis. Fungal β-N-acetylhexosaminidase (Hex) from Penicillium oxalicum CCF 1959 served...
In this review, we collected and presented evidence from the scientific literature regarding biotechnological production applications of limonene its oxidative derivates in various fields such as food, pharmaceutical, cosmetic or polymer industries. Limonene biotransformations may be regarded processes aligned to sustainable development. Advantages associated with these bioprocesses include use by-products raw materials, mild reaction conditions, high regio- stereoselectivity value-added...
β-N-acetylhexosaminidases have great potential in applied biocatalysis owing to their ability act on a wide range of natural and modified substrates. In this work, from four Penicillium crustosum strains (PcHex) were studied. The production showed the highest enzymatic activity culture medium after 11–14 days cultivation. specific isolated purified PcHex hydrolysis 4-nitrophenyl-N-acetyl-β-D-galactopyranoside was 15–20 U/mg protein. All similar pH–activity profiles, with optimum pH being...