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- Title
Immobilization of Cryptococcus flavus a-amylase on glass tubes and its application in starch hydrolysis.
- Authors
Pereira, Sueli Essado; Fernandes, Kátia Flávia; Ulhoa, Cirano José
- Abstract
α-Amylase from Cryptococcus flavus was previously purified after exchange chromatography on Q-Sepharose and gel filtration on Sephacryl S-100. The enzyme was purified 128-fold with a recovery rate of 81% of activity. The molecular mass of the α-amylase was 67 kDa as determined by SDS-PAGE. The enzyme was characterized after immobilization on glass tubes. The immobilization yield, efficiency, and activity recovery of α-amylase were 79, 57, and 45%, respectively. The optimum pH of the immobilized enzyme was shifted to a more acidic pH (4.5) compared with the free enzyme (5.5). The optimum temperature of the immobilized enzyme was the same for the free enzyme (50°C), but it showed a higher thermal stability. The immobilized enzyme showed activity until the 10th cycle, maintaining 47% of initial activity, and was capable of hydrolyzing starch from potato, wheat, corn, and cassava. The main products released from starch were maltose, maltotriose, and maltotetraose.
- Subjects
CRYPTOCOCCUS; ENCAPSULATION (Catalysis); CHROMATOGRAPHIC analysis; GEL permeation chromatography; MOLECULAR weights; GLASS tubes
- Publication
Starch / Staerke, 2017, Vol 69, Issue 3/4, p1
- ISSN
0038-9056
- Publication type
Article
- DOI
10.1002/star.201600189