1967
DOI: 10.3168/jds.s0022-0302(67)87485-x
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Factors Affecting Stability of Rennin

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Cited by 21 publications
(7 citation statements)
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“…Thermal denaturation of chymosin is dependent on pH (Farkye & Imafidon, 1995), ionic strength (Larson & Whitaker, 1970) and the total solids content of the system (Verhey, 1973). Substances such as sugars, proteins and calcium increase the thermostability of chymosin (Van de Beek & Gerlsma, 1969), while NaCl and urea decrease its thermostability (Mickelsen & Ernstrom, 1967).…”
mentioning
confidence: 99%
“…Thermal denaturation of chymosin is dependent on pH (Farkye & Imafidon, 1995), ionic strength (Larson & Whitaker, 1970) and the total solids content of the system (Verhey, 1973). Substances such as sugars, proteins and calcium increase the thermostability of chymosin (Van de Beek & Gerlsma, 1969), while NaCl and urea decrease its thermostability (Mickelsen & Ernstrom, 1967).…”
mentioning
confidence: 99%
“…Long extraction time had a negative effect on the activity and yield of prochymosin. According to Mickelsen and Ernstrom (1967), during extraction, chymosin was partially inactivated because of its low stability in an aqueous medium.…”
Section: Results and Discussion Control Methods Of Prochymosin Extractionmentioning
confidence: 99%
“…Chymosin is a very heat stable enzyme at pH values between 5.3 and 6.3 (Foltmann, 1959;Mickelsen and Ernstrom, 1967). Generally, during extraction of biologically active substances, yield increases with increasing temperature because of the increasing diffusion rate.…”
Section: Fig 4-prochymosinmentioning
confidence: 99%
“…A proportional pH decrease was experienced with increasing S gf in batch mode, but when switched to continuous operation the pH eventually reached 4.8±5.2. This range has been reported in the literature as the most stable pH range for minimum activity loss at various temperatures 8,18 and the pH data for S gf in the range 2.5±7.5 g dm…”
Section: Variation Of Medium Phmentioning
confidence: 99%