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Enzymatic modification of vegetable protein: Mechanism, kinetics, and production of soluble and partially soluble protein in a batch reactor
Author(s) -
Constantinides A.,
AduAmankwa B.
Publication year - 1980
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260220804
Subject(s) - chemistry , hydrolysis , chromatography , enzyme , batch reactor , kinetics , protein precipitation , protease , hydrolyzed protein , precipitation , soy protein , biochemistry , catalysis , high performance liquid chromatography , physics , quantum mechanics , meteorology
Enzymatic hydrolysis of insoluble soybean protein by a protease enzyme produced by Penicillium duponti K 1104, was investigated in a batch reactor. The reaction conditions were 30–55°C and pH 3.4–3.7. The mechanism of solubilization of the insoluble protein by the Penicillium duponti enzyme was deduced from a series of experiments. Kinetic models were developed that involved adsorption followed by peptic digestion of protein, inhibition of low‐molecular‐weight peptides, and enzyme deactivation. The uncoupled kinetic parameters were estimated using the Marquardt nonlinear parameter estimation algorithm. A bang–bang production of soluble and partially soluble protein is suggested for higher productivity. The essential amino acids pattern of the enzyme‐Hydrolyzed soy protein was comparable with the unhydrolyzed protein isolate. Aggregation of the soluble protein for an extended time was observable. The low‐molecular‐weight soluble protein was incorporated into noncarbonated beverages. The amount of protein that could be incorporated into a can of 355 ml noncarbonated beverage, without observable changes in the optical density and also aggregation of the protein, was 2.5 g soluble protein. Beverages with caramel color showed excessive decrease in optical density and precipitation. The kinetics and diffusion in a multipore immobilized‐enzyme recycle reactor will be considered in part II of this series.