Caractérisation des systèmes enzymatiques protéolytiques de deux souches psychrotrophes isolées de laits crus réfrigérés

Millière, Jean-Bernard; Veillet-Poncet, Louise

doi:10.1051/lait:1979585-58614

Cited by 6 publications

(2 citation statements)

References 4 publications

(4 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The whey proteins have been shown by many workers (Bengtsson et al 1973;Yanagiya et al 1973;Law et al 1977;DeBeukelar et al 1977;Richardson & Te Whaiti, 1978;Milliere & Veillet-Poncet, 1979;Stepaniak et al 1982a), to be relatively insensitive to the action of psychrotroph proteinases, possibly owing to the highly globular nature of whey proteins in contrast to the random non-helical structure of the caseins.…”

Section: Effects Of Proteinases From Psychrotrophic Bacteria On Milk mentioning

confidence: 99%

Proteinases of psychrotrophic bacteria: their production, properties, effects and control

Fairbairn

Law

1986

Journal of Dairy Research

193

View full text Add to dashboard Cite

Section: Effects Of Proteinases From Psychrotrophic Bacteria On Milk mentioning

confidence: 99%

Proteinases of psychrotrophic bacteria: their production, properties, effects and control

Fairbairn

Law

1986

Journal of Dairy Research

193

View full text Add to dashboard Cite

“…De la leche bronca se ha aislado Pseudomonas 28 P 12 la cual produce una sola enzima que hidroliza a la #-caseína más rápidamente que a la "-caseína (Milliere y Veillet-Poncet, 1979).…”

Section: Proteasas De Pseudomonasunclassified

Efecto de enzimas proteolíticas endógenas y una bacteriana en la formación de emulsiones modelo a partir de músculo estriado de cazón (Rhizopriondon terraenovae) y cerdo

Barrientos

View full text Add to dashboard Cite

show abstract

Heat inactivation of exogenous proteinases fromPseudomonas fluorescens

Kroll¹,

Klostermeyer²

1984

Z Lebensm Unters Forch

View full text Add to dashboard Cite

The inactivation reaction of the proteinase of a P. fluorescens strain of biotype I in milk was investigated at 130-150 degrees C, also in milk and in buffer with and without added CaCl2 at temperatures below 100 degrees C. The decline in activity corresponded to first order kinetics in the UHT region; Ea = 115 kJ/mol. D values were 290 (130 degrees C), 124 (140 degrees C) and 54 s (150 degrees C); therefore, the usual temperature time combinations of UHT treatment are not sufficient to achieve the required rates of inactivation. At temperatures below 80 degrees C, inactivation corresponded increasingly to second order kinetics with considerably higher reaction rates; at 55 degrees C, an inactivation reaction corresponding to that induced by UHT treatment could be achieved at a thermal stress lower by a factor of 500. This "low temperature inactivation" was observed in a further 20 strains representing the spectrum of P. fluorescens. The average rates of inactivation following heat treatment in milk for 20 min are 47% at 55 degrees C and 44% at 60 degrees C. This can be regarded as the most effective temperature range for the inactivation of the proteinases in milk. Clear connections can be seen between the biotype groups and the optimum temperature for inactivation: biotype group I ca. 55 degrees C, group II (with a few exceptions) less than or equal to 50 degrees C and group III greater than or equal to 60 degrees C. The inactivation reaction is systematically influenced by the proteins and Ca++ ions present in milk.

show abstract

Caractérisation des systèmes enzymatiques protéolytiques de deux souches psychrotrophes isolées de laits crus réfrigérés

Cited by 6 publications

References 4 publications

Proteinases of psychrotrophic bacteria: their production, properties, effects and control

Proteinases of psychrotrophic bacteria: their production, properties, effects and control

Efecto de enzimas proteolíticas endógenas y una bacteriana en la formación de emulsiones modelo a partir de músculo estriado de cazón (Rhizopriondon terraenovae) y cerdo

Heat inactivation of exogenous proteinases fromPseudomonas fluorescens

Contact Info

Product

Resources

About