Calliandra selloi Macbride trypsin inhibitor: Isolation, characterization, stability, spectroscopic analyses

Glycosylation, amino acid analysis and kinetic properties of a major Kunitz-type trypsin inhibitor from Acacia victoriae Bentham seeds

“…The inhibition was of the competitive type, as there was an increase in K m with no change in V max compared to the reaction in the absence of inhibitor. The K i value for AvTI was also estimated to be 1.06 Â 10 À8 M. Compared with trypsin inhibitor from other sources, AvTI was found to have a stronger affinity for trypsin than Calliandra selloi Macbride Kunitz trypsin inhibitor (K i 2.21 Â 10 À7 M) (Yoshizaki et al, 2007), but weaker than other Kunitz trypsin inhibitors, such as those obtained from other leguminous plants, including Archidendron ellipticum (K i 2.46 Â 10 À10 M) (Bhattacharyya et al, 2006), Dimorphandra mollis (K i 1.70 Â 10 À9 M) (Mello et al, 2001), Glycine soja (K i 3.20-6.20 Â 10 À9 M) (Deshimaru, Hanamoto, Kusano, Yoshimi, & Terada, 2002), Caesalpinia bonduc (K i 2.75 Â 10 À10 M) (Bhattacharyya, Rai, & Babu, 2007) and Inga laurina (K i 6.00 Â 10 À9 M) (Macedo et al, 2007). …”

Extraction, purification and properties of trypsin inhibitor from Thai mung bean (Vigna radiata (L.) R. Wilczek)

“…Two trypsin inhibitory activity bands were observed for cowpea (10 and 18 kDa) and pigeon pea (15 and 25 kDa) (Benjakul et al, 2000). Yoshizaki et al (2007) reported that the molecular weight of a trypsin inhibitor purified from Calliandra selloi Macbride seeds was 20 kDa. Wang et al (2006) reported that a novel protease inhibitor, designated mungoin, from mung bean (Phaseolus mungo) seeds had a molecular mass of 10 kDa in SDS-PAGE.…”

Castor bean cake contains a trypsin inhibitor that displays antifungal activity against Colletotrichum gloeosporioides and inhibits the midgut proteases of the dengue mosquito larvae

“…This affinity chromatography is especially advantageous because it is highly selective. Therefore, various protocols for purification of trypsin inhibitors include the use of affinity columns where trypsin is covalently attached (Macedo et al, 2003;Oliveira et al, 2007Oliveira et al, , 2012Yoshizaki et al, 2007). However, according to Macedo et al, (2003), the possibility of breakage during chromatography of these inhibitors should not be neglected as trypsin immobilized on the matrix is catalytically active.…”