Thermostable phytase in feed and fuel industries.

Phytase with wide ranging biochemical properties has long been utilized in a multitude of industries, even so, thermostability plays a crucial factor in choosing the right phytase in a few of the sectors. Mesophilic phytases are not considered to be a viable option in the feed industry owing to its limited stability in the required feed processing temperature. In the recent past, inclusion of thermostable phytase in fuel ethanol production from starch based raw material has been demonstrated with economic benefits.

Genetic and metabolic engineering approaches for the production and delivery of L-asparaginases: An overview.

L-asparaginase is one of the protein drugs for countering leukemia and lymphoma. A major challenge in the therapeutic potential of the enzyme is its immunogenicity, low-plasma half-life and glutaminase activity that are found to be the reasons for toxicities attributed to asparaginase therapy. For addressing these challenges, several research and developmental activities are going on throughout the world for an effective drug delivery for treatment of cancer.

Microbial phytase: Impact of advances in genetic engineering in revolutionizing its properties and applications.

Phytases are enzymes that increase the availability of phosphorous in monogastric diet and reduces the anti-nutrition effect of phytate. This review highlights contributions of recombinant technology to phytase research during the last decade with specific emphasis on new generation phytases. Application of modern molecular tools and genetic engineering have aided the discovery of novel phytase genes, facilitated its commercial production and expanded its applications.

Replacement P212H altered the pH-temperature profile of phytase from Aspergillus niger NII 08121.

Microbial phytase, a widely used animal feed enzyme, needs to be active and stable in the acidic milieu for better performance in the monogastric gut. Aspergillus niger phytases exhibit an activity dip in the pH range from 3.0 to 3.

Effect of surface charge alteration on stability of L-asparaginase II from Escherichia sp.

Escherichia coli L-asparaginases have great significance in the treatment of leukemia. Consequently, there is considerable interest in engineering this enzyme for improving its stability. In this work, the effect of surface charge on the stability of the enzyme l-asparaginase II was studied by site-directed mutagenesis of the cloned ansB gene from Escherichia sp.

Gene cloning and soluble expression of Aspergillus niger phytase in E. coli cytosol via chaperone co-expression.

A phytase gene from Aspergillus niger was isolated and two Escherichia coli expression systems, based on T7 RNA polymerase promoter and tac promoter, were used for its recombinant expression. Co-expression of molecular chaperone, GroES/EL, aided functional cytosolic expression of the phytase in E. coli BL21 (DE3).

Single-step purification and immobilization of MBP-phytase fusion on starch agar beads: application in dephytination of soy milk.

Periplasmic phytase, appA from E. coli has been noticed as a superior feed and food additive owing to its high specific activity, acidic pH optimum and resistance to gastric proteases. E.