{"title":"不同加工方法对牛初乳抗胰蛋白酶活性的影响","authors":"Lukas Trzebiatowski , Plamen Georgiev , Kathrin Büttner , Axel Wehrend","doi":"10.3168/jdsc.2024-0678","DOIUrl":null,"url":null,"abstract":"<div><div>Colostrum is important for supplying the bovine neonate with nutrients, bioactive substances, and immunoglobulins to acquire passive immunity. Trypsin inhibitory activity represents a general characteristic of the first bovine colostrum. It is assumed that the anti-trypsin activity serves to protect bioactive molecules in the colostrum from being digested by the calf. The objectives of the study were to establish a test to determine anti-trypsin activity and test the hypothesis that freezing, acidification, and heat treatment alter anti-trypsin activity compared with untreated bovine colostrum. A photometric assay was established to determine anti-trypsin activity. The activity was expressed in milligrams of inhibited trypsin per milliliter of colostrum. Anti-trypsin activity was measured in untreated colostrum, frozen colostrum (−20°C for 24 h), colostrum acidified using 10% formic acid in a way that it was present as 1% in the sample, and colostrum heat treated according to 2 different protocols (60°C for 60 min and 63.5°C for 30 min). In our study, trypsin inhibition in 40 untreated colostrum samples (0.80 mg/mL, SEM 0.03) corresponded to that observed in frozen colostrum samples (0.79 mg/mL, SEM 0.03). In these first analyzed 40 and 59 extra samples (in total 99 samples), the anti-trypsin activity of frozen colostrum (0.85 mg/mL, SEM 0.01) was compared with colostrum subjected to acidification (0.84 mg/mL, SEM 0.01), heat treatment at 60°C for 60 min (0.65 mg/mL, SEM 0.02), and heat treatment at 63.5°C for 30 min (0.61 mg/mL, SEM 0.02). Acidification did not significantly affect trypsin inhibition. Both heat treatment protocols significantly reduced anti-trypsin activity. In the future, when investigating the effects of postharvest storage and processing on bovine colostrum, the influence on anti-trypsin activity should be evaluated in addition to the effects on immunoglobulins and other components.</div></div>","PeriodicalId":94061,"journal":{"name":"JDS communications","volume":"6 3","pages":"Pages 411-415"},"PeriodicalIF":0.0000,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Influence of different processing methods on anti-trypsin activity in bovine colostrum\",\"authors\":\"Lukas Trzebiatowski , Plamen Georgiev , Kathrin Büttner , Axel Wehrend\",\"doi\":\"10.3168/jdsc.2024-0678\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Colostrum is important for supplying the bovine neonate with nutrients, bioactive substances, and immunoglobulins to acquire passive immunity. Trypsin inhibitory activity represents a general characteristic of the first bovine colostrum. It is assumed that the anti-trypsin activity serves to protect bioactive molecules in the colostrum from being digested by the calf. The objectives of the study were to establish a test to determine anti-trypsin activity and test the hypothesis that freezing, acidification, and heat treatment alter anti-trypsin activity compared with untreated bovine colostrum. A photometric assay was established to determine anti-trypsin activity. The activity was expressed in milligrams of inhibited trypsin per milliliter of colostrum. Anti-trypsin activity was measured in untreated colostrum, frozen colostrum (−20°C for 24 h), colostrum acidified using 10% formic acid in a way that it was present as 1% in the sample, and colostrum heat treated according to 2 different protocols (60°C for 60 min and 63.5°C for 30 min). In our study, trypsin inhibition in 40 untreated colostrum samples (0.80 mg/mL, SEM 0.03) corresponded to that observed in frozen colostrum samples (0.79 mg/mL, SEM 0.03). In these first analyzed 40 and 59 extra samples (in total 99 samples), the anti-trypsin activity of frozen colostrum (0.85 mg/mL, SEM 0.01) was compared with colostrum subjected to acidification (0.84 mg/mL, SEM 0.01), heat treatment at 60°C for 60 min (0.65 mg/mL, SEM 0.02), and heat treatment at 63.5°C for 30 min (0.61 mg/mL, SEM 0.02). Acidification did not significantly affect trypsin inhibition. Both heat treatment protocols significantly reduced anti-trypsin activity. In the future, when investigating the effects of postharvest storage and processing on bovine colostrum, the influence on anti-trypsin activity should be evaluated in addition to the effects on immunoglobulins and other components.</div></div>\",\"PeriodicalId\":94061,\"journal\":{\"name\":\"JDS communications\",\"volume\":\"6 3\",\"pages\":\"Pages 411-415\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"JDS communications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2666910224001984\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"JDS communications","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2666910224001984","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
初乳是重要的为牛新生儿提供营养物质,生物活性物质和免疫球蛋白,以获得被动免疫。胰蛋白酶抑制活性是牛初乳的一个普遍特征。据推测,抗胰蛋白酶活性是为了保护初乳中的生物活性分子不被小牛消化。本研究的目的是建立一种测定抗胰蛋白酶活性的试验,并验证与未经处理的牛初乳相比,冷冻、酸化和热处理会改变抗胰蛋白酶活性的假设。建立了光度法测定抗胰蛋白酶活性。活性以每毫升初乳中抑制胰蛋白酶的毫克数表示。在未经处理的初乳、冷冻初乳(- 20°C 24小时)、用10%甲酸酸化的初乳(在样品中以1%的比例存在)和根据2种不同方案(60°C 60分钟和63.5°C 30分钟)热处理的初乳中测量抗胰蛋白酶活性。在我们的研究中,40个未经处理的初乳样品(0.80 mg/mL, SEM 0.03)对胰蛋白酶的抑制作用与冷冻初乳样品(0.79 mg/mL, SEM 0.03)的抑制作用一致。在首次分析的40和59个额外样品(共99个样品)中,将冷冻初乳(0.85 mg/mL, SEM 0.01)的抗胰蛋白酶活性与酸化(0.84 mg/mL, SEM 0.01)、60°C热处理60分钟(0.65 mg/mL, SEM 0.02)和63.5°C热处理30分钟(0.61 mg/mL, SEM 0.02)的初乳进行了比较。酸化对胰蛋白酶抑制作用无显著影响。两种热处理方案都显著降低了抗胰蛋白酶活性。未来,在研究采后储存和加工对牛初乳的影响时,除了对免疫球蛋白和其他成分的影响外,还应评估对抗胰蛋白酶活性的影响。
Influence of different processing methods on anti-trypsin activity in bovine colostrum
Colostrum is important for supplying the bovine neonate with nutrients, bioactive substances, and immunoglobulins to acquire passive immunity. Trypsin inhibitory activity represents a general characteristic of the first bovine colostrum. It is assumed that the anti-trypsin activity serves to protect bioactive molecules in the colostrum from being digested by the calf. The objectives of the study were to establish a test to determine anti-trypsin activity and test the hypothesis that freezing, acidification, and heat treatment alter anti-trypsin activity compared with untreated bovine colostrum. A photometric assay was established to determine anti-trypsin activity. The activity was expressed in milligrams of inhibited trypsin per milliliter of colostrum. Anti-trypsin activity was measured in untreated colostrum, frozen colostrum (−20°C for 24 h), colostrum acidified using 10% formic acid in a way that it was present as 1% in the sample, and colostrum heat treated according to 2 different protocols (60°C for 60 min and 63.5°C for 30 min). In our study, trypsin inhibition in 40 untreated colostrum samples (0.80 mg/mL, SEM 0.03) corresponded to that observed in frozen colostrum samples (0.79 mg/mL, SEM 0.03). In these first analyzed 40 and 59 extra samples (in total 99 samples), the anti-trypsin activity of frozen colostrum (0.85 mg/mL, SEM 0.01) was compared with colostrum subjected to acidification (0.84 mg/mL, SEM 0.01), heat treatment at 60°C for 60 min (0.65 mg/mL, SEM 0.02), and heat treatment at 63.5°C for 30 min (0.61 mg/mL, SEM 0.02). Acidification did not significantly affect trypsin inhibition. Both heat treatment protocols significantly reduced anti-trypsin activity. In the future, when investigating the effects of postharvest storage and processing on bovine colostrum, the influence on anti-trypsin activity should be evaluated in addition to the effects on immunoglobulins and other components.