Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction ...

Immobilization is often the key to optimizing the operational performance of an enzyme in industrial processes, particularly for use in non-aqueous media. Different methods for the immobilization of enzymes are critically reviewed. The methods are divided into three main categories, viz. (i) binding to a prefabricated support (carrier), (ii) entrapment in organic or inorganic polymer matrices, ...

Enzymes are attractive, "green" alternatives to chemical catalysts within the industrial sector, but their robustness to environmental conditions needs optimizing. Here, an enzyme is tagged chemically and recombinantly with a self-assembling peptide that allows the conjugate to spontaneously assemble with pure peptide to form β-sheet-rich nanofibers decorated with tethered enzyme. Above a criti...

Endophytic fungi generally reside asymptomatically in the tissues of higher plants and generally are source of original amidase group of enzymes. Asparaginase is an important anticancer enzyme, endophytic fungi Eurotium Sp. was isolated from rhizomes of Curcuma longa and evaluated for asparaginase production by qualitative plate assay on modified Czapex dox’s agar and quantitative analysis by N...

BACKGROUND Extracellular expression of proteins has an absolute advantage in a large-scale industrial production. In our previous study, Thermobifida fusca cutinase, an enzyme mainly utilized in textile industry, was expressed via type II secretory system in Escherichia coli BL21(DE3), and it was found that parts of the expressed protein was accumulated in the periplasmic space. Due to the fact...

BACKGROUND Laccases have huge potential for biotechnological applications due to their broad substrate spectrum and wide range of reactions they are able to catalyze. These include, for example, the formation and degradation of dimers, oligomers, polymers, and ring cleavage as well as oxidation of aromatic compounds. Potential applications of laccases include detoxification of industrial efflue...

The α-amylases are endo-acting enzymes that hydrolyze starch by randomly cleaving the 1,4-α-d-glucosidic linkages between the adjacent glucose units in a linear amylose chain. They have significant advantages in a wide range of applications, particularly in the food industry. The eukaryotic α-amylase isolated from the Antarctic ciliated protozoon Euplotes focardii (EfAmy) is an alkaline enzyme,...

Alkaline proteases are the most important groups of commercial enzymes, which have been broadly used in industrial processes. In this study, Bacillus sp. PTCC 1538 was selected as a biological agent to produce alkaline protease. Enzyme production under submerge fermentation using waste effluent investigated. Since costs raw material plays an role cost enzyme production, corn steep liquor (CSL) ...

Abstract This study evaluated the lactose hydrolysis by immobilized ?-galactosidase, which was produced Kluyveromyces marxianus using porungo cheese whey as substrate. Initially, yeast cultivated in medium at 30 °C and 200 rpm, showing a maximal ?-galactosidase production of 14.19 U mL-1. The crude extract obtained used to evaluate enzymatic solution. optimal pH temperature free enzyme investig...

Introductory courses in biochemistry teach that enzymes are specific for their substrates and the reactions they catalyze. Enzymes diverging from this statement are sometimes called promiscuous. It has been suggested that relaxed substrate and reaction specificities can have an important role in enzyme evolution; however, enzyme promiscuity also has an applied aspect. Enzyme condition promiscui...