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ABSTRACT The hydrolytic activities and specificities of gel‐entrapped C. cylindracae lipase (CCL) and R. arrhizus lipase (RAL) toward olive oil and tributyrin were investigated. Lipases in hydrophobic gels with the longest chain lengths generally displayed highest activity. The optimal temperature was 30–35° for free and 37–40° for gel‐entrapped lipases. The ratio of the activity on tributyrin to that of olive oil (expressed as T/O ratio), an indicator of substrate specificity, increased from 0.3 for free lipases to 12.3 ± 2.3 for CCL lipase in ENTP‐2000‐formed gel and 16.2 ± 0.3 for RAL lipase in ENTP‐4000‐formed gel.
Journal of Food Science – Wiley
Published: Mar 1, 1994
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