Аннотация
This article reports the characterization and evaluation of the
biotechnological potential of a cysteine protease purified from
Calotropis procera (CpCP3). This enzyme was highly stable to different
metal ions and was able to hydrolyze kappa-casein similarly to bovine
chymosin. Atomic force microscopy showed that the process of casein
micelle aggregation induced by CpCP3 was similar to that caused by
chymosin. The cheeses made using CpCP3 showed higher moisture content
than those made with chymosin, but protein, fat, and ash were similar.
The sensory analysis showed that cheeses made with CpCP3 had high
acceptance index (> 80%). In silico analysis predicted the presence of
only two short allergenic peptides on the surface of CpCP3, which was
highly susceptible to digestive enzymes and did not alter zebrafish
embryos' morphology and development. Moreover, recombinant CpCP3 was
expressed in Escherichia coli. All results support the biotechnological
potential of CpCP3 as an alternative enzyme to chymosin.
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