The Role of Calcium Ions to Improve Activity of Chitinase Isolated from Vibrio sp.
[摘要] Chitinase (EC 3.2.1.14) plays a crucial role in chitin degradation, specifically breaking down the 1→4 β-glycosidic bonds of N-acetyl-D-glucosamine (GlcNAc) to produce its mono- or oligomers. This study aims to study the characteristics of chitinase 2+ from Vibrio sp. (isolated from tiger shrimp in Indonesia) and explore the role of calcium ions (Ca ) in increasing chitinase oactivity. The optimum condition for chitinase activities is pH 7.5, 45 C of temperature, and 120 min of incubation time. The 2+enzyme activity parameters such as K and V values were calculated by varying the concentration of Ca , namely: 0 % ; m max0.2 % ; 0.4 %; 0.6% ; 0.8 %. The final product of the chitinase reaction, the GlcNAc, is then used to measure the enzyme activity based on the Somogyi-Nelson method. The results showed that chitinase isolated from Vibrio sp. has increasing 2+ 2+ –1activity with the addition of Ca . Without the addition of Ca , the K and V of chitinase were 7.781 µmol mL and m max–1 2+0.066 µmol min , respectively. The treatment of 0.4 % Ca shows optimum activity with the K and V at 6.723 µmol m max–1 –1 2+mL and 0.079 µmol min , respectively. The results showed the potential use of Ca as a chitinase activator to fulfill demands for energy-efficient and economically profitable chitinase usage.
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[效力级别] [学科分类] 生物科学(综合)
[关键词] Eco-friendly waste management;Enzyme activity;Marine waste;Profitable chitinase;Utilization of Agro-industrial waste. [时效性]