A chymotrypsin-like proteinase from the midgut of larvae

Recovery and techno-functionality of flours and proteins from two edible insect species: Meal worm ( Tenebrio molitor ) and black soldier fly ( Hermetia illucens ) larvae

“…The percentage distribution of the protein bands in the aqueous extracts varied upon flour fraction used and extraction conditions applied. As already described by Bußler et al (2016), the bands observed in the range between 14 and 32 kDa could possibly originate from cuticle proteins with molecular weights predominantly between 14 and 30 kDa (Andersen et al, 1995) or chymotrypsin-like proteinase (24 kDa) (Elpidina et al, 2005), whereas the bands observed ranging from 32 to 95 kDa could possibly originate from enzymes and other proteins, e.g. melanization-inhibiting protein (43 kDa), β-glycosidase (59 kDa), trypsin-like proteinases (59 kDa), and melanization-engaging types of protein (85 kDa) (Cho et al, 1999; Ferreira et al, 2001; Prabhakar et al, 2007; Zhao et al, 2005).…”

Identification and characterization of midgut proteases in Achaea janata and their implications

“…The inability of TPCK to detect chymotrypsin-like activity might be due to the inability of the chymotrypsin-like protease to recognize phenylalanine in a short chymotrypsin substrate, S(Ala) 2 ProPhe-pNA (Valaitis 1995;Elpidina et al 2005). Based on our observation of the absence of TPCK and chymostatin inhibitory effect on the 17 kDa protease and its inhibition by elastinal, this band was considered as an elastase-like protease rather than a chymotrypsin.…”

Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis

“…EDTA, a metalloprotease inhibitor, had no effect on its activity. TPCK, a short substrate-like chymotrypsin inhibitor, did not inhibit the enzyme, which indicated a chymotrypsin-like protease from the midgut of T. molitor larvae [20]. STI, a protease inhibitor from soybean seeds, showed high inhibitive activity.…”

“…Purified Fc-chy showed high activity toward substrate AAPF; further, its activity was inhibited by PMSF and STI, similar to a chymotrypsin-like SP from the midgut of T. molitor larvae [20]. The inhibition characteristics imply that the purified Fc-chy was an SP.…”