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Preparation of immobilized soybean β‐amylase on porous cellulose beads and continuous maltose production
Author(s) -
Maeda Hidekatsu,
Tsao George T.,
Chen Li Fu
Publication year - 1978
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.260200305
Subject(s) - maltose , cellulose , conjugate , chemistry , chromatography , amylase , porosity , diffusion , immobilized enzyme , enzyme , organic chemistry , mathematical analysis , physics , mathematics , thermodynamics
Immobilized soybean β‐amylase was prepared by using porous cellulose beads. The expressed activity of the β‐amylase–cellulose beads conjugated below 35 mesh was 59–69% of the initial activity and the protein content was 10–13%. General properties of the conjugate were almost identical with those of the native enzyme except for the K m value. The K m value of the conjugate was 40m M and the K m value of the native enzyme was 0.6m M . This large difference was probably caused by pore structure, i.e., a pore diffusion problem. The film diffusion problem occurred at the flow rate below a linear velocity of 3 cm/min. Maximum maltose contents of the hydrolyzates prepared by the conjugate and the native enzyme were 69 and 71%, respectively. After a continuous column operation at 50°C for 17 days, the activity of the column was 60% of the activity. The half‐life of the column at 40°C was 40 days.