Milk clotting and proteolytic activity of an enzyme preparation from Bromelia hieronymi fruits

Abstract

A new enzyme preparation (hieronymain), obtained from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae), was assayed for its ability to clot milk and hydrolyze bovine casein and milk whey proteins. Caseinolytic activity at 30 C and pH 6.5 (milk clotting conditions) was 3.3 Ucas/mL and milk clotting activity was 40 0.2 IMCU/mL. The k-casein fraction, involved in the clotting formation, began to be degraded after 10 min of reaction, while the degradation of the other casein fractions proceeded slowly enough as to guarantee the production of a firm curd, with no evidence of extensive hydrolysis, a necessary condition for cheese making. In the case of whey proteins, bovine serum albumin andBromelia hieronymi Mez (Bromeliaceae), was assayed for its ability to clot milk and hydrolyze bovine casein and milk whey proteins. Caseinolytic activity at 30 C and pH 6.5 (milk clotting conditions) was 3.3 Ucas/mL and milk clotting activity was 40 0.2 IMCU/mL. The k-casein fraction, involved in the clotting formation, began to be degraded after 10 min of reaction, while the degradation of the other casein fractions proceeded slowly enough as to guarantee the production of a firm curd, with no evidence of extensive hydrolysis, a necessary condition for cheese making. In the case of whey proteins, bovine serum albumin and 0.2 IMCU/mL. The k-casein fraction, involved in the clotting formation, began to be degraded after 10 min of reaction, while the degradation of the other casein fractions proceeded slowly enough as to guarantee the production of a firm curd, with no evidence of extensive hydrolysis, a necessary condition for cheese making. In the case of whey proteins, bovine serum albumin and a-lactalbumin were quickly degraded after 30 min, while b-lactoglobulin was considerably degraded only after 60 min at 50 C. Miniature cheeses were manufactured both with chymosine and hieronymain and analyzed by a taste panel, who found acceptable both cheeses. Hieronymain might be appropriate for cheese making, as well as for the production of milk protein hydrolysates.-lactalbumin were quickly degraded after 30 min, while b-lactoglobulin was considerably degraded only after 60 min at 50 C. Miniature cheeses were manufactured both with chymosine and hieronymain and analyzed by a taste panel, who found acceptable both cheeses. Hieronymain might be appropriate for cheese making, as well as for the production of milk protein hydrolysates.