Background Because the process is cost-efective, microbial pectinase is used in juice clearing. The isolation,
immobilization, and characterization of pectinase from Aspergillus nidulans (Eidam) G. Winter (AUMC No. 7147) were
therefore the focus of the current investigation.
Results Ammonium sulphate (85%), DEAE-cellulose, and Sephadex G-200 were used to purify the enzyme. Wit
a yield of 30.4%, the fnal specifc activity was 400 units mg−1 protein and 125-fold purifcation. Using SDS-PAG
to validate the purifcation of the pectinase, a single band showing the homogeneity of the purifed pectinase
with a molecular weight of 50 kD was found. Chitosan and calcium alginate both efectively immobilized pecti‑
nase, with immobilization efciencies of 85.7 and 69.4%, respectively. At 50, 55, 60, and 65 °C, the thermostability
of both free and chitosan-immobilized pectinase was examined. The free and chitosan-immobilized enzymes ha
half-lives (t1/2) of 23.83 and 28.64 min at 65 °C, and their Kd values were 0.0291 and 0.0242 min−1, respectively. In addi
tion, the Z values were 44.6 and 31.54 °C, while the D values were 79.2 and 95.1 min. Compared to the untreated one,
the orange, mango, and pineapple juices treated with immobilized pure pectinase showed greater clarity. Following
treatment with pure pectinase, the fruit juice’s 1, 1-diphenyl-2-picrylhydrazyl and 2, 2′-azino-bis 3-ethylbenz
zoline-6-sulfonate scavenging activities increased. Following treatment with pure pectinase, the amounts of tota
phenolics and total favonoids increased.
Conclusion The procedure is deemed cost-efective in the food industry because the strong afnity of fungal pec
tinase for pectin. The investigated pectinase supported its usage in the food industry by being able to clear orange,
mango, and pineapple juices. |
