Serine protease from Artocarpus altilis (breadfruit) latex

Abstract

Breadfruit is recognized as a plant with the potential to be cultivated as an alternative staple food due to its high starch content and envisioned as a solution to mitigate hunger. The plant bears abundant fruits throughout the year with its productivity is comparable to other staple crops and it thrives well in countries where the poor population is high. Breadfruit however, exudes copious amount of latex upon harvesting and the stained epicarp often perceived as low in quality. Standardized methods of harvesting in plantations include a stage of latex draining by inverting the fruit for several hours. The latex will be drained to the ground and considered as an agricultural waste with no current commercial application. Despite being considered as a nuisance, plant latexes is a rich source of proteases functioned as a defensive mechanism against pathogenic attacks. In the effort to identify its potential, the breadfruit latex protease was purified and its characteristics were determined. The stability of the protease was investigated and its kinetics of inactivation was estimated in this research. Based on the analyses, breadfruit latex was discovered to consist of a serine protease with highly stable properties, potentially developed as an alternative commercial protease.