1979
DOI: 10.1002/food.19790230312
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Untersuchungen zur Substratspezifität einer Protease aus Thermoactinomyces vulgaris

Abstract: The cleavage specificity of a protease from Thermoactinomyces vulgaris (thermitase) was determined by the insulin B-chain and the cleavability of casein and haemoglobin by this enzyme as compared to other proteases (trypsin, chymotrypsin, proteases from Bac. megaterium and cytophages). The most intense splitting effect on the substrates under investigation (insulin B-chain, casein and haemoglobin) is exerted by thermitase, i. e., the unspecificity of this enzyme is especially marked.

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Cited by 7 publications
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“…Folgende Materialien wurden verwendet : API vorn Institut fur Futterproduktion Paulinenaue, Proteingehalt (N x 6,25) 82.5 :h, Fettgehalt nach WEIBULL-STOLDT 6,3 %, Mineralstoffgclialt 2.8 %; Pepsinkonzentrat des VEB Berlin-Chemie, 13 600 EE; Therrnitase, 2800 TE/g [8] ; DL-Methioninethylester (DL-Met-OEt . HCI), hergestellt nach BOISONAS u. a.…”
Section: Materials Und Methodenunclassified
“…Folgende Materialien wurden verwendet : API vorn Institut fur Futterproduktion Paulinenaue, Proteingehalt (N x 6,25) 82.5 :h, Fettgehalt nach WEIBULL-STOLDT 6,3 %, Mineralstoffgclialt 2.8 %; Pepsinkonzentrat des VEB Berlin-Chemie, 13 600 EE; Therrnitase, 2800 TE/g [8] ; DL-Methioninethylester (DL-Met-OEt . HCI), hergestellt nach BOISONAS u. a.…”
Section: Materials Und Methodenunclassified