2003
DOI: 10.1016/s0014-3057(02)00192-1
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Immobilization of bromelain onto porous copoly(γ-methyl-l-glutamate/l-leucine) beads

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Cited by 35 publications
(18 citation statements)
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“…This shift could be explained as multi-point ionic interaction between enzymes and polymeric matrix due to the activation energy of the enzyme to reorganize an optimum conformation for binding to its substrate. One of the main reasons for enzyme immobilization is the anticipated increase in its stability to various deactivating force due to restricted conformational mobility of the molecules following immobilization [22][23][24].…”
Section: Resultsmentioning
confidence: 99%
“…This shift could be explained as multi-point ionic interaction between enzymes and polymeric matrix due to the activation energy of the enzyme to reorganize an optimum conformation for binding to its substrate. One of the main reasons for enzyme immobilization is the anticipated increase in its stability to various deactivating force due to restricted conformational mobility of the molecules following immobilization [22][23][24].…”
Section: Resultsmentioning
confidence: 99%
“…Moreover, the immobilized β-glucosidase was found to possess 75% of its original activity, whereas the free enzyme remained at 35% at 60 °C. It was obvious that the immobilized β-glucosidase was more stable than the free β-glucosidase due to the increased rigidity of the enzyme after immobilization (Chiou and Wu 2004;Jung et al 2011;Yodoya et al 2003).…”
Section: Thermal Stabilitymentioning
confidence: 99%
“…Compared with the free laccase, the immobilized laccase provided a broader profile and its relative activity maintained more than 78% in the temperature range between 40°C and 70°C. The increased stability of the immobilized laccase was due to the restricted conformational mobility of the molecules after immobilization (Yodoya et al, 2003).…”
Section: Property Of Immobilized Laccasementioning
confidence: 99%