Fractionation and characterisation of sialylated-mucin glycoprotein from edible birds' nest hydrolysates through anion exchange chromatography.

Edible bird's nest (EBN) is made up of sialylated-mucin glycoprotein with various health benefits due to its high antioxidative activity. However, as a macromolecule with distinct charged sialic acid and amino acids, fractions with different charges would have varied physicochemical properties and antioxidant activity, which have not been studied. Therefore, this study aimed to fractionate and purify the enzymatic hydrolysed of cleaned EBN (EBNh) and EBN by-product (EBNh) through anion exchange chromatography (AEC), and determine their molecular weights, physicochemical properties, and antioxidative activities.

Cultivation Conditions for Phytase Production from Recombinant Escherichia coli DH5α.

Response surface methodology (RSM) was used to optimize the cultivation conditions for the production of phytase by recombinant Escherichia coli DH5α. The optimum predicted cultivation conditions for phytase production were at 3 hours seed age, a 2.5% inoculum level, an L-arabinose concentration of 0.