Immobilization of ABL on S. wallichiana stem displayed slightly
better activity from 2.76 mmol/min/g-support at 100 rpm to
3.47 mmol/min/g-support at 250 rpm, but above this remained
relatively constant. A corresponding decrease in lipase activity
from 3.42 to 1.97 mmol/min/g-support was found at alkali pH (9.0–
11.0). This might result from either changes in enzyme conformation or denaturation. Lipase activity was the highest at pH 8.0
(3.67 mmol/min/g-support), close to the isoelectric point of ABL,
7.75 (data not shown) is consistent with the enzyme's expected
maximum adsorption