TY - JOUR
T1 - Influence of harvest season on the proteolytic activity of hepatopancreas and mantle tissues from jumbo squid (Dosidicus gigas)
AU - Ezquerra-Brauer, Josafat Marina
AU - Haard, Norman F.
AU - Ramírez-Olivas, Rosalina
AU - Olivas-Burrola, Hermenegildo
AU - Velázquez-Sánchez, Carlos J.
PY - 2002/11
Y1 - 2002/11
N2 - Jumbo squid (Dosidicus gigas) size and protease activities were evaluated after harvest in April (A) and November (N). A were smaller (560±120 g vs 6040±1130 g) and hepatopancreas was a larger percent of body weight (8.3±2.5 vs 4.6±2.1). Mantle from A had lower water (73.9±1.1 vs 79.1± 1.2) and higher protein (29.0±1.1 vs 23.1±0.8). Lipid and protein contents of N and A hepatopancreas tissues did not differ (P<0.05). Azocaseinolytic, trypsin-like, chymotrypsin-like, aminopeptidase, and carboxypeptidase activities were detected in mantle (ME) and hepatopancreas extracts (HPE). HPE and ME from N had higher activity than A for all substrates (P<0.05). With azocasein substrate, HPE activity from A had a pH optimum of 5 - 6 and a temperature optimum of 70C, whereas HPE from N had highest activity at pH 9 and 40-70C. ME from A had maximum proteolytic activity at pH 6 and 60C, whereas that from N had maximum activity at pH 10 and 40C. SDS-PAGE zymograms of HPE from A and N revealed different patterns of activity and 1 and 2 major protease zones, respectively.
AB - Jumbo squid (Dosidicus gigas) size and protease activities were evaluated after harvest in April (A) and November (N). A were smaller (560±120 g vs 6040±1130 g) and hepatopancreas was a larger percent of body weight (8.3±2.5 vs 4.6±2.1). Mantle from A had lower water (73.9±1.1 vs 79.1± 1.2) and higher protein (29.0±1.1 vs 23.1±0.8). Lipid and protein contents of N and A hepatopancreas tissues did not differ (P<0.05). Azocaseinolytic, trypsin-like, chymotrypsin-like, aminopeptidase, and carboxypeptidase activities were detected in mantle (ME) and hepatopancreas extracts (HPE). HPE and ME from N had higher activity than A for all substrates (P<0.05). With azocasein substrate, HPE activity from A had a pH optimum of 5 - 6 and a temperature optimum of 70C, whereas HPE from N had highest activity at pH 9 and 40-70C. ME from A had maximum proteolytic activity at pH 6 and 60C, whereas that from N had maximum activity at pH 10 and 40C. SDS-PAGE zymograms of HPE from A and N revealed different patterns of activity and 1 and 2 major protease zones, respectively.
UR - http://www.scopus.com/inward/record.url?scp=0036866293&partnerID=8YFLogxK
U2 - 10.1111/j.1745-4514.2002.tb00766.x
DO - 10.1111/j.1745-4514.2002.tb00766.x
M3 - Artículo
SN - 0145-8884
VL - 26
SP - 459
EP - 475
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
IS - 5
ER -