The conditions of adsorption immobilization of papain on super-crosslinked ion-exchangers
Abstract
The regularities of adsorption immobilization of the proteolytic enzyme papain on super-crosslinked
polymers A-100 and MN-500 are considered. Super-crosslinked polystyrol has a high specific surface area,
characterized by a developed porous structure and significant mobility of the polymer grid, being a matrix for
the formation of various nanoclusters of inorganic and organic nature. At the same time, the sorption capacity
of these polymers is much higher than the capacity of other types of organic sorbents. One of the advantages
of sorbents is also non-toxicity and hemocompatibility
The sorption of papain depending on the time of achieving equilibrium and the concentration of hydrogen
ions in the solution were studied. Optimal conditions of adsorption immobilization were established:
immobilization time – 2 hours, pH – 6.5 units, sorbat concentration – 4÷5·10-2 mmol/dm3.
The obtained experimental kinetic curves indicate that the sorption process is limited by the stage of
internal diffusion. The values of effective diffusion coefficients for papain immobilized on MN-500 (7.35 ·
10-9 cm2/s) and A-100 (1.18·10-9 cm2/s) were calculated. It is shown that the best protein sorption is observed
at pH 6.2-6.5 in the region where the catalytic activity of enzyme preparations also had the greatest
value. A multi-molecular nature of the received isotherms of papain adsorption on the sorbents was identified.
It is noted that during the immobilization of papain on super-crosslinked sorbents the main contribution
is made by hydrophobic interactions leading to the manifestation of π-π– electron interaction between the
sorbat and the sorbent. The adsorption isotherms of papain were analyzed using the adsorption theory of BET
and the equilibrium parameters of sorption were calculated: the limit amount of sorbed papain, constants characterizing
the interaction of the sorbat-sorbent and sorbat-sorbat.
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