Starch Phosphorylase: An Overview of Biochemical Characterization, Immobilization and Peptide Mapping

Abstract

Starch phosphorylase (EC 2.4.1.1) is the key enzyme which catalyzes the reversible conversion of starch and inorganic phosphate into glucose-1-phosphate (G-1-P) and has been reported in many higher plants. It can be exploited for industrial purposes for tailoring starch and for the synthesis of biopolymers which may be useful in food industry and are also of clinical importance. Starch in the form of insoluble granules accumulates in chloroplasts as the primary product of photosynthesis. Multiple forms of the enzyme have been reported in different plant tissues which have been predicted to have different roles in starch metabolism. Here, various biochemical properties have Review Article Jain et al.; BBJ, 5(3): 103-122, 2015; Article no.BBJ.2015.011 104 been reviewed. Various techniques for enzyme immobilization have been discussed. Besides, reports on immobilization of starch phosphorylase from different sources and on different solid matrices have also been reviewed. Peptide mapping reports of various proteins have also been assessed in this review.