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

被引:61
作者
Bruno, Mariela A. [1 ]
Lazza, Cristian M. [1 ]
Errasti, Maria E. [1 ]
Lopez, Laura M. I. [1 ]
Caffini, Nestor O. [1 ]
Pardo, Marcelo F. [1 ]
机构
[1] Univ Nacl La Plata, Fac Ciencias Exactas, Dept Ciencias Biol, LIPROVE, La Plata, Argentina
关键词
Casein; Hydrolysis; Milk clotting; Plant endopeptidases; Proteolytic activity; ARTICHOKE CYNARA-SCOLYMUS; ASPARTIC PROTEINASE; CHEESE; PURIFICATION; PROTEASE; HYDROLYSIS; EXTRACTION; PEPTIDES; CHYMOSIN; FLOWERS;
D O I
10.1016/j.lwt.2009.12.003
中图分类号
TS2 [食品工业];
学科分类号
100403 [营养与食品卫生学];
摘要
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 degrees 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 alpha-lactalbumin were quickly degraded after 30 min. while beta-lactoglobulin was considerably degraded only after 60 min at 50 degrees 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. (C) 2009 Elsevier Ltd All rights reserved.
引用
收藏
页码:695 / 701
页数:7
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