PMID:25326060

Citation	Nawaz, MA, Karim, A, Aman, A, Marchetti, R, Qader, SA and Molinaro, A' (2014) Continuous degradation of maltose: improvement in stability and catalytic properties of maltase (α-glucosidase) through immobilization using agar-agar gel as a support. Bioprocess Biosyst Eng '
Abstract	Maltose degrading enzyme was immobilized within agar-agar support via entrapment method due to its industrial utilization. The maximum immobilization efficiency (82.77 %) was achieved using 4.0 % agar-agar keeping the diameter of bead up to 3.0 mm. The matrix entrapment showed maximum catalytic activity at pH 7.0 and temperature 65 °C. Substrate saturation kinetics showed that the K m of immobilized enzyme increased from 1.717 to 2.117 mM ml(-1) where as Vmax decreased from 8,411 to 7,450 U ml(-1 )min(-1) as compared to free enzyme. The immobilization significantly increased the stability of maltase against various temperatures and immobilized maltase retain 100 % of its original activity after 2 h at 50 °C, whereas the free maltase only showed 60 % residual activity under same condition. The reusability of entrapped maltase showed activity up to 12 cycles and retained 50 % of activity even after 5th cycle. Storage stability of agar entrapped maltase retain 73 % of its initial activity even after 2 months when stored at 30 °C while free enzyme showed only 37 % activity at same storage conditions.
Links	PubMed Online version:10.1007/s00449-014-1302-6
Keywords
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Significance

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:MGA		GO:0004558: alpha-1,4-glucosidase activity	ECO:0000314:		F		Degradation of maltose: made more stable and catalytic via immobilization using agar	complete CACAO 10576

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