Empirical kinetic models for tryptic whey-protein hydrolysis

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Empirical kinetic models for tryptic whey- protein hydrolysis

Enzymic hydrolyses of naturally occurring protein sources represent complex reactions at a molecular level because of the specificity pattern of proteases and the composition of the substrates involved. In addition, rather global criteria are in practical use for describing the extent of protein hydrolysis. Therefore, mechanistically based kinetic modelling may not be applicable under these cir...

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Kinetic Model for Whey Protein Hydrolysis by Alcalase Multipoint- Immobilized on Agarose Gel Particles

Partial hydrolysis of whey proteins by enzymes immobilized on an inert support can either change or evidence functional properties of the produced peptides, thereby increasing their applications. The hydrolysis of sweet cheese whey proteins by alcalase, which is multipoint-immobilized on agarose gel, is studied here. A MichaelisMenten model that takes into account competitive inhibition by the ...

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A kinetic model for hydrolysis of whey proteins by cardosin A extracted from Cynara cardunculus

The enzymatic hydrolysis of the major whey proteins, namely b-lactoglobulin (b-Lg) and a-lactalbumin (a-La), was experimentally studied using whey as substrate; an aspartic protease (cardosin A), previously extracted from the flowers of Cynara cardunculus and purified by gel filtration and ion exchange chromatographies, was used for this purpose. Sweet whey was incubated for 24 h at various enz...

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Controlled whey protein hydrolysis using two alternative proteases

Whole whey was hydrolyzed for 12 h with Protease 2A and Trypsin using two concentrations of enzyme (20 and 40 g/kgprotein). Samples were assayed for total viable counts of adventitious micro ̄ora that survived thermization, total acidity, total concentration of free amino acids, peptide pro®le and overall degree of hydrolysis. The highest total concentration of free amino acids was observed when...

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Enzymatic hydrolysis of heat-induced aggregates of whey protein isolate.

The effects of heat-induced denaturation and subsequent aggregation of whey protein isolate (WPI) solutions on the rate of enzymatic hydrolysis was investigated. Both heated (60 °C, 15 min; 65 °C, 5 and 15 min; 70 °C, 5 and 15 min, 75 °C, 5 and 15 min; 80 °C, 10 min) and unheated WPI solutions (100 g L(-1) protein) were incubated with a commercial proteolytic enzyme preparation, Corolase PP, un...

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ژورنال

عنوان ژورنال: Process Biochemistry

سال: 1997

ISSN: 1359-5113

DOI: 10.1016/s0032-9592(96)00060-x