Biochemical characterization of an isoform of chymotrypsin from the viscera of Monterey sardine (Sardinops sagax caerulea), and comparison with bovine chymotrypsin

Study on enzymes of industrial interest in digestive viscera: Greater amberjack (Seriola dumerili)

“…Another similar result was reported for pirarucu A. gigas [8], with optimal temperature at 65 °C . Results of optimum temperature for chymotrypsin from Monterey sardine Sardinops sagax caerulea [25] are in accordance with that found in the present work. Guerrero-Zárate et al [13] reported optimum temperature of 60 °C for alkaline proteases (trypsin and chymotrypsin) in juveniles of tropical gar A. tropicus.…”

“…The K m is used to assess the affinity of the tested enzyme to the substrate and constitutes one of the characteristics observed by the industry during the prospection process for novel commercial enzymes. The results for trypsin showed similar values to that of alkaline trypsin from silver mojarra D. rhombeus [7], pirarucu A. gigas [8] and crevalle jack C. hippos [1]; while chymotrypsin values diverged from that reported by Castillo-Yañez et al [25]. The effect of temperature on the activity of trypsin in this work was similar to that of Brownstripe red snapper Lutjanus vitta [26] and zebra blenny Salaria basilisca [11].…”

“…Optimum pH of chymotrypsin was similar to the reports for Monterey sardine S. sagax caeruleus [25], showing a relatively high activity in the pH range of 8.0-10.0. Here, the optimum pH range (7.5-9.0) found for chymotrypsin indicated denaturation when subjected to extensive acidic pH range (below 5.0) or for long time to high alkaline pH ranges (> 12.0).…”

Partial Characterization of Digestive Proteases in the Green Cichlid, Cichlasoma beani

“…The number of active fractions found in C. beani was similar to that reported in marine species such as P. maculatofasciatus [33], and freshwater species such as P. splendida [22], C. undecimalis [16], and A. tropicus [24]. In other omnivorous species such as the South American pilchard Sardinops sagax caerulea [43] and round sardinella Sardinella aurita [44], trypsin showed active fractions with different molecular weights ranging between 35 and 38.8 kDa, while purified chymotrypsin from S. sagax caerulea had a molecular weight of 35.5 kDa [45]. The inhibitors SBT1 and PMSF, specific for serine protease, presented the highest percentages of inhibition as they eliminated three active fractions in C. beani, which could be trypsin-like or chymotrypsin-like enzymes [42,[44][45][46].…”

“…In other omnivorous species such as the South American pilchard Sardinops sagax caerulea [43] and round sardinella Sardinella aurita [44], trypsin showed active fractions with different molecular weights ranging between 35 and 38.8 kDa, while purified chymotrypsin from S. sagax caerulea had a molecular weight of 35.5 kDa [45]. The inhibitors SBT1 and PMSF, specific for serine protease, presented the highest percentages of inhibition as they eliminated three active fractions in C. beani, which could be trypsin-like or chymotrypsin-like enzymes [42,[44][45][46]. On the other hand the inhibitors specific for metalloproteases phenanthroline and EDTA, inhibited two active fractions in the first group of enzymes.…”