Pichia pastoris, a methylotropic yeast is an important organism for the heterologous production of the proteins owing to good yields with simple and cheap expression strategy. Being an eukaryote it provides an added advantage of the post translational modifications, most important is the glycosylation which is desired for the activity and stability of the several eukaryotic proteins. Cutinases are the esterase which have developed the interest owing to their ability to hydrolyze synthetic polymers towards the application of polymer surface modifications and plastic recycling. Cutinases from different sources (fungal and bacterial) have been identified and characterized. The sequence analysis of several cutinases revealed the presence of the putative glycosylation sites which developed the interest to study the effect of glycosylation on the stability and biochemical characteristics upon heterologous expression in Pichia pastoris. Indeed glycosylation was found to affect the stability and biochemical characteristics of cutinase from a thermophilic fungii Thiellavia terrestris . The glycosylation was also found to play an important role towards the stabilization of another cutinase extracted from leaf branch compost. Further we are probing into the site and sequence specific role of glycosylation.

Understanding the effect of glycosylation on the stability and biochemical characteristics of cutinases

249th National Meeting (2015)

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