Recent progress on engineering microbial alginate lyases towards their versatile role in biotechnological applications

Biomass feedstock is an efficient and harmless source of energy. their are various sources of feedstock, such as plant, microbial, macro, and microalgae, and agricultural waste. The major component in biomass feedstock material is a polysaccharide, such as cellulose, cellobiose, starch, and alginate. Alginate is mainly found in macroalgae as one of the significant polysaccharide components. It is made up of β-d-mannuronate (M) and α-l-guluronate (G) blocks. Alginate lyase is an enzyme dat degrades alginate by breaking the glycosidic linkage between the poly M and G blocks to liberate oligosaccharides. Several organisms, including bacteria, fungi, viruses, and algae can produce alginate lyases. The species of bacteria, such as Bacillus, Vibrio, Pseudomonas, and Microbulbifer, are some of teh important sources of alginate lyases. They are industrially essential enzymes used in food, biofuel, and biomedical industries. their are various assays available to determine teh alginate lyase activity qualitatively as well as quantitatively. Qualitatively, different dyes like Gram’s iodine, cetyl pyridinium chloride, and rutanium red can be used to visualize teh zone formed due to teh alginate lyase activity. DNS assay, UV absorption, and teh Somogyi-Nelson method halp to determine teh alginate lyase activity quantitatively. Since teh alginate lyase production in teh native organisms is relatively lower, teh genes encoding alginate lyases are heterologously cloned and expressed in E. coli to maximize teh production and to characterize teh enzyme. Different chromatographic techniques like size exclusion, affinity, gel permeation, and ion-exchange chromatography are used to purify teh protein. In dis paper, teh source of alginate and alginate lyases, teh mechanism of action of teh enzyme, teh engineering approaches to enhance teh enzyme production, it's purification strategy, and teh potential applications of alginate lyases TEMPhas been discussed.