|
Human trypsin has an optimal [[operating temperature]] of about 37 °C.[{{cite journal | vauthors = Chelulei Cheison S, Brand J, Leeb E, Kulozik U | title = Analysis of the effect of temperature changes combined with different alkaline pH on the β-lactoglobulin trypsin hydrolysis pattern using MALDI-TOF-MS/MS | journal = Journal of Agricultural and Food Chemistry | volume = 59 | issue = 5 | pages = 1572–81 | date = March 2011 | pmid = 21319805 | doi = 10.1021/jf1039876 | bibcode = 2011JAFC...59.1572C | url = http://mediatum.ub.tum.de/node?id=1470049 }}] In contrast, the [[Atlantic cod]] has several types of trypsins for the [[poikilotherm]] fish to survive at different body temperatures. Cod trypsins include trypsin I with an activity range of {{convert|4|to|65|C|F}} and maximal activity at {{convert|55|°C|°F|abbr=on}}, as well as trypsin Y with a range of {{convert|2|to|30|C|F}} and a maximal activity at {{convert|21|°C|°F|abbr=on}}.[{{cite journal | vauthors = Gudmundsdóttir A, Pálsdóttir HM | title = Atlantic cod trypsins: from basic research to practical applications | journal = Marine Biotechnology | volume = 7 | issue = 2 | pages = 77–88 | year = 2005 | pmid = 15759084 | doi = 10.1007/s10126-004-0061-9 | bibcode = 2005MarBt...7...77G | s2cid = 42480996 }}]
|
|
Animal trypsin has an optimal [[operating temperature]] of about 37 °C.[{{cite journal | vauthors = Chelulei Cheison S, Brand J, Leeb E, Kulozik U | title = Analysis of the effect of temperature changes combined with different alkaline pH on the β-lactoglobulin trypsin hydrolysis pattern using MALDI-TOF-MS/MS | journal = Journal of Agricultural and Food Chemistry | volume = 59 | issue = 5 | pages = 1572–81 | date = March 2011 | pmid = 21319805 | doi = 10.1021/jf1039876 | bibcode = 2011JAFC...59.1572C | url = http://mediatum.ub.tum.de/node?id=1470049 }}] In contrast, the [[Atlantic cod]] has several types of trypsins for the [[poikilotherm]] fish to survive at different body temperatures. Cod trypsins include trypsin I with an activity range of {{convert|4|to|65|C|F}} and maximal activity at {{convert|55|°C|°F|abbr=on}}, as well as trypsin Y with a range of {{convert|2|to|30|C|F}} and a maximal activity at {{convert|21|°C|°F|abbr=on}}.[{{cite journal | vauthors = Gudmundsdóttir A, Pálsdóttir HM | title = Atlantic cod trypsins: from basic research to practical applications | journal = Marine Biotechnology | volume = 7 | issue = 2 | pages = 77–88 | year = 2005 | pmid = 15759084 | doi = 10.1007/s10126-004-0061-9 | bibcode = 2005MarBt...7...77G | s2cid = 42480996 }}] |
|
As a protein, trypsin has various molecular weights depending on the source. For example, a molecular weight of 23.3 kDa is reported for trypsin from bovine and porcine sources. |
|
As a protein, trypsin has various molecular weights depending on the source. For example, a molecular weight of 23.3 kDa is reported for trypsin from bovine and porcine sources. |