Abstract Candida rugosa lipase (CRL) is an enzyme that widely used in biopharmaceutical and biopesticide industries due to its high catalytic ability reusability. However, conditions from industrial processes are often outside CRL stability range may cause denaturation or destabilization of the enzyme, causing it be not reusable, hence lowering economic value. To increase activity, stability, r...

The main goal of this study was to investigate the effect of extraction conditions on the enzymatic properties of thermoacidic amylase enzyme derived from dragon peel. The studied extraction variables were the buffer-to-sample (B/S) ratio (1:2 to 1:6, w/w), temperature (-18°C to 25°), mixing time (60 to 180 seconds), and the pH of the buffer (2.0 to 8.0). The results indicate that the enzyme ex...

Novel hybrid magnetic cross-linked enzyme aggregates of phenylalanine ammonia lyase (HM-PAL-CLEAs) were developed by co-aggregation of enzyme aggregates with magnetite nanoparticles and subsequent crosslinking with glutaraldehyde. The HM-PAL-CLEAs can be easily separated from the reaction mixture by using an external magnetic field. Analysis by scanning electron microscopy (SEM) and confocal la...

Lipolytic potential of Aspergillus japonicus LAB01 was investigated by describing the catalytic properties and stability of a secreted extracellular lipase. Enzyme production was considered high under room temperature after 4 days using sunflower oil and a combination of casein with sodium nitrate. Lipase was partially purified by 3.9-fold, resulting in a 44.2% yield using ammonium sulphate pre...

Biocatalytic syntheses often require unfavorable conditions, which can adversely affect enzyme stability. Consequently, improving the stability of biocatalysts is needed, and this achieved by immobilization. In study, we aimed to compare soluble immobilized transaminases from different species. A cysteine in a consensus sequence was converted single aldehyde formylglycine-generating for directe...

The stability (longevity of activity) three crude urease extracts was evaluated in a laboratory study as part an effort to reduce the cost for applications that do not require high purity enzyme. A low-cost, stable source will greatly facilitate engineering such biocementation soil. Inexpensive have been shown be effective at hydrolyzing urea carbonate precipitation. However, some studies sugge...

Abstract Metal organic frameworks (MOFs) are multi-dimensional network of crystalline material held together by bonding metal atoms and ligands. Owing to unique structural, chemical, physical properties, MOFs has been used for enzyme immobilization be employed in different catalytic process, including degradation antibiotics. Immobilization process other than providing large surface provides wi...

tyrosinase (ec: 1.14.18.1) is a copper - containing enzyme which is distributed in all domains of life such as prokaryote, eukaryote, mammals, invertebrates and plants. tyrosinase catalyzes the oxidation of monophenols to diphenols and diphenols to o-quinones . the tyrosinase crystallographic data shows two histidine -rich regions named cua and cub. a loop containing residues m374, s375 and v37...

background tyrosinase, as a copper-containing enzyme, is widely distributed in different levels of life span. it is also a key enzyme in melanin biosynthesis, which plays a crucial role in determining the color of mammalian skin and hair. objectives the current study aimed to determine the effect of a palladium complex on cresolase and catecholase reactions of mushroom tyrosinase (mt). material...

The structures of enzymes reflect two tendencies that appear opposed. On one hand, they fold into compact, stable structures; on the other hand, they bind a ligand and catalyze a reaction. To be stable, enzymes fold to maximize favorable interactions, forming a tightly packed hydrophobic core, exposing hydrophilic groups, and optimizing intramolecular hydrogen-bonding. To be functional, enzymes...