猪脂肪酶和微生物脂肪酶在接近幼鸟小肠条件下的稳定性。

Stability of porcine and microbial lipases to conditions that approximate the small intestine of young birds.

作者信息

Kermanshahi H, Maenz D D, Classen H L

机构信息

Department of Animal and Poultry Science, University of Saskatchewan, Saskatoon, Canada.

出版信息

Poult Sci. 1998 Nov;77(11):1671-7. doi: 10.1093/ps/77.11.1671.

DOI:10.1093/ps/77.11.1671

PMID:9835342

Abstract

In vitro experiments were conducted to study the stability of lipase activities from bacterial, fungal, and animal sources under conditions that approximate the small intestine. In the first experiment, the effects of preincubation with trypsin (500, 1,000, and 2,000 U/mL), chymotrypsin (200, 400, and 800 U/mL), and trypsin plus chymotrypsin (TC; 2,000 U/mL trypsin + 800 U/inL chymotrypsin) for 30 min at 40 C, on lipase activities from sources of Pseudomonas spp. (PL1, PL2), Chromobacterium viscosum (CVL), and Aspergillus niger (ANL) were determined. None of the enzymes were inhibited by trypsin. The chymotrypsin decreased the activity of all of the lipases. The TC had no additional negative effect on the activities of PL1 and PL2; however, ANL and CVL activities were further decreased relative to the chymotrypsin only treatment. In the second study, the effects of Na taurodeoxycholate (0.1 to 16 mM) on the activities of PL1, PL2, CVL, ANL, and crude porcine lipase (CPL) at 23 and 40 C were evaluated. At 23 C, in order of potency, Na taurodeoxycholate inhibited the activities of ANL, CPL, and CVL. At this temperature, Na taurodeoxycholate did not inhibit PL1 and PL2. An increase in the temperature to 40 C increased the activity of all of the enzymes tested. At 40 C, Na taurodeoxycholate had similar effects on lipase activities; however, higher Na taurodeoxycholate levels were required to inhibit ANL activity, and only a partial inhibition of CPL occurred. At 23 C, porcine colipase restored the activity of CPL but had no effect on ANL and CVL in the presence of inhibitory levels of Na taurodeoxycholate. At 40 C, porcine colipase had no effect on Na taurodeoxycholate inhibition of lipase activity. The results of this study indicate that PL is more stable than CVL and ANL, and that colipase addition has no beneficial effects on microbial lipase activities under conditions that approximate the avian small intestine.

摘要

进行了体外实验，以研究细菌、真菌和动物来源的脂肪酶在接近小肠的条件下的活性稳定性。在第一个实验中，测定了在40℃下用胰蛋白酶（500、1000和2000 U/mL）、糜蛋白酶（200、400和800 U/mL）以及胰蛋白酶加糜蛋白酶（TC；2000 U/mL胰蛋白酶 + 800 U/mL糜蛋白酶）预孵育30分钟对假单胞菌属（PL1、PL2）、粘质色杆菌（CVL）和黑曲霉（ANL）来源的脂肪酶活性的影响。没有一种酶被胰蛋白酶抑制。糜蛋白酶降低了所有脂肪酶的活性。TC对PL1和PL2的活性没有额外的负面影响；然而，相对于仅用糜蛋白酶处理，ANL和CVL的活性进一步降低。在第二项研究中，评估了牛磺脱氧胆酸钠（0.1至16 mM）在23℃和40℃下对PL1、PL2、CVL、ANL和粗制猪脂肪酶（CPL）活性的影响。在23℃时，按效力顺序，牛磺脱氧胆酸钠抑制ANL、CPL和CVL的活性。在此温度下，牛磺脱氧胆酸钠不抑制PL1和PL2。温度升高到40℃增加了所有测试酶的活性。在40℃时，牛磺脱氧胆酸钠对脂肪酶活性有类似影响；然而，抑制ANL活性需要更高水平的牛磺脱氧胆酸钠，并且对CPL仅发生部分抑制。在23℃时，猪辅脂酶恢复了CPL的活性，但在存在抑制水平的牛磺脱氧胆酸钠时对ANL和CVL没有影响。在40℃时，猪辅脂酶对牛磺脱氧胆酸钠抑制脂肪酶活性没有影响。这项研究的结果表明，PL比CVL和ANL更稳定，并且在接近禽类小肠的条件下添加辅脂酶对微生物脂肪酶活性没有有益影响。