ArticleApplied and environmental microbiology2004
Cloning of the authentic bovine gene encoding pepsinogen a and its expression in microbial cells.
Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Safety evaluation of the food enzyme rennet containing chymosin and pepsin A from the abomasum of suckling calves, goats, lambs and buffaloes.EFSA journal. European Food Safety Authority · 2024Article
- Safety evaluation of the food enzyme rennet containing chymosin and pepsin A from the abomasum of suckling calves, goats and lambs.EFSA journal. European Food Safety Authority · 2023Article
- Safety evaluation of the food enzyme rennet containing chymosin and pepsin A from the abomasum of calves and cows.EFSA journal. European Food Safety Authority · 2023Article
- Safety evaluation of the food enzyme rennet containing chymosin and pepsin A from the abomasum of suckling goats, lambs and calves.EFSA journal. European Food Safety Authority · 2022Article
- Safety evaluation of the food enzyme rennet containing chymosin and pepsin A from calf abomasum.EFSA journal. European Food Safety Authority · 2022Article
- Safety evaluation of the food enzyme containing chymosin and pepsin from the abomasum of suckling lambs.EFSA journal. European Food Safety Authority · 2022Article
- Safety evaluation of the food enzyme rennet paste from the abomasum of suckling goats, lambs and calves.EFSA journal. European Food Safety Authority · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bovine pepsin is the second major proteolytic activity of rennet obtained from young calves and is the main protease when it is extracted from adult animals, and it is well recognized that the proteolytic specificity of this enzyme improves the sensory properties of cheese during maturation. Pepsin is synthesized as an inactive precursor, pepsinogen, which is autocatalytically activated at the pH of calf abomasum. A cDNA coding for bovine pepsin was assembled by fusing the cDNA fragments from two different bovine expressed sequence tag libraries to synthetic DNA sequences based on the previously described N-terminal sequence of pepsinogen. The sequence of this cDNA clearly differs from the previously described partial bovine pepsinogen sequences, which actually are rabbit pepsinogen sequences. By cloning this cDNA in different vectors we produced functional bovine pepsinogen in Escherichia coli and Saccharomyces cerevisiae. The recombinant pepsinogen is activated by low pH, and the resulting mature pepsin has milk-clotting activity. Moreover, the mature enzyme generates digestion profiles with alpha-, beta-, or kappa-casein indistinguishable from those obtained with a natural pepsin preparation. The potential applications of this recombinant enzyme include cheese making and bioactive peptide production. One remarkable advantage of the recombinant enzyme for food applications is that there is no risk of transmission of bovine spongiform encephalopathy.
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