Heat Inactivation of Bile Salt-Stimulated Lipase Activity in Human Milk and Colostrum

Pan, Su; Dill, C. W.; Alford, E. S.; Richter, R. L.; Garza, Cutberto

doi:10.4315/0362-028x-46.6.525

Cited by 1 publication

(1 citation statement)

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“…The enzyme was slightly more heat sensitive in colostrum than in mature milk and was not affected in either menstrum at 45°C for 40 min. The bile-salt-stimulated lipase in human milk was more sensitive than the lipase in bovine milk (38). Others have recorded times for inactivation of I h at 50°C (39) and 10 min at 55°C (40).…”

Section: Discussionmentioning

confidence: 99%

Inactivation of Bile‐Salt‐Stimulated Human Milk Esterase

O'Connor,

Longbottom,

Walde

1986

J. pediatr. gastroenterol. nutr.

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SummaryThe activity of bile‐salt‐stimulated esterase was monitored in human milk during storage at room temperature, in a refrigerator (4°C), in a freezer (‐ 19°C), and in milk that had been freeze dried and rehydrated after storage of the lypophilized milk at 4°C and ‐ 19°C. In all cases, there was some loss of activity, independent of measurement in the presence or absence of sodium taurocholate, and the loss was highest in milk stored at room temperature, approximating a 50% loss in 1–2 days. Activation and inactivation of solutions of the purified enzyme have been identified by measuring its esterase activity against a variety of 4‐nitrophenylalkanoate esters at pH 7.3 within the temperature range 5–46.5°C. The optimum temperature was 42°C. The presence of bile salt partially serves to maintain the conformation of the bile‐salt‐binding site as the esterolytic binding site becomes inactivated at 50°C. Bile salts thus exert a positive template effect on the enzyme.

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Section: Discussionmentioning

confidence: 99%