کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
70090 | 48809 | 2011 | 5 صفحه PDF | دانلود رایگان |

Mannanase was immobilized on chitin with glutaraldehyde by cross-linking reaction. The immobilization conditions and the characterization of immobilized enzyme were carried out. The immobilization yield and the mannanase activity recovery were 94.81% and 72.17%, respectively. The optimal mannanase activity shifted to lower pH after immobilization. However, the optimum temperature remained unchanged at 70 °C. The immobilized enzyme exhibited better thermal and pH stability than the free one. It also exhibited a high storage stability and retained 70% of its initial activity after 120 days. The main hydrolysis products yielded from locust bean gum were mannotriose and mannotetraose. The resulting manno-oligosaccharides could be used as a special nutrient for lactic bacteria.
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► Immobilized mannanase on chitin crosslinked by glutaraldehyde.
► Immobilized enzyme exhibited better thermal and pH stability than the free one.
► Immobilized mannansase is suitable for practical manno-oligosaccharide production.
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 73, Issues 1–4, December 2011, Pages 111–115