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ENZYMATIC SOLUBILIZATION OF LEAF PROTEIN CONCENTRATE IN MEMBRANE REACTORS
Author(s) -
PAYNE R. EDWARD,
HILL C. G.,
AMUNDSON C. H.
Publication year - 1978
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1978.tb02310.x
Subject(s) - chemistry , chromatography , substrate (aquarium) , membrane reactor , hydrolysis , trypsin , batch reactor , membrane , enzymatic hydrolysis , permeation , enzyme , biochemistry , catalysis , oceanography , geology
The enzymatic solubilization of an insoluble alfalfa protein fraction was studied in a batch reactor and in a continuous flow semi‐batch membrane reactor. The “white” cytoplasmic protein fraction obtained by heat precipitation was solubilized using the proteolytic enzyme trypsin. Batch studies were carried out at pH 7.7 with a trypsin to substrate ratio of 2 x 10m ‐3 (by weight). At 27, 37 and 47°C the hydrolysis reaction was found to be first‐order in substrate concentration. The activation energy was 23.25 kcal. At 47°C the conversion level was 97% after 4 hr. For the membrane reactor system, the effects of the variables pH, temperature, substrate concentration, and trypsin to substrate ratio were evaluated with the aid of factorial design methods. The optimum operating conditions for the membrane reactor studies were 47°C at pH 7.7 with a trypsin to substrate ratio of 4 x 10 ‐3 at a 0.5% solids concentration level. The hydrolysis process was enhanced if the reactor was operated in a washout mode prior to the addition of enzyme suggesting that soluble low molecular weight inhibitors were washed out of the reactor with the permeate. 55% of the total amount of insoluble starting material appeared as products in the permeate after 4 hr of operation under the conditions stated above.