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Elastase
The inactive proelastase is activated by trypsin to the active form elastase. Elastase attacks peptide bonds next to the small amino acid residues such 3s glycine, alanine and serine and has a broader specificity than the other two enzymes.
All the three enzymes viz. trypsin, chymotrypsin and elastase are endopeptidases (a subclass of peptide hydrolases that hydrolyse the more centrally situated peptide bonds). You have already seen that pepsin is also an endopeptidase.
It is the process of separating colloidal and suspended impurities from water by passing it through a porous bed made of fine sand and other proper sized granular materials. Filtra
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