Present investigation describes immobilization efficiency of endoinulinase onto hetero-functionalized halloysite nanoclay using 3-aminopropyltriethoxysilane and glutaraldehyde as crosslinkers. Under optimal conditions (APTES 0.75%, sonication time 2.25 h, glutaraldehyde 0.75%, activation-time 65 min, immobilized endoinulinase load 60 IU and coupling-time 1 h), maximum yield in enzyme activity (70.65%) and immobilization (89.61%) was obtained. Developed immobilized biocatalyst shown maximum activity at 65 °C and pH 5.0 with wide range thermal (50-80 °C) and pH (4.0-9.0) stability. Increase in half-life (28.70-fold) of immobilized endoinulinase was observed as compared to free enzyme. An enhanced K and reduced V of endoinulinase for inulin was recorded after immobilization. Maximum FOSs production 98.42% was obtained, under optimized conditions (inulin 10%; immobilized endoinulinase load 85 IU; hydrolysis-time 10 h and agitation rate 130 rpm) containing kestose (36.26%), nystose (27.02%), fructofuranosylnystose (9.98%) and FOSs DP 5-9 (25.15%). Developed immobilized biocatalyst exhibited a splendid operational stability for 18 batch cycles.
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Hetero-modification of halloysite nanoclay to immobilize endoinulinase for the preparation of fructooligosaccharides.
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Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147 002, Punjab, India.
Present investigation describes immobilization efficiency of endoinulinase onto hetero-functionalized halloysite nanoclay using 3-aminopropyltriethoxysilane and glutaraldehyde as crosslinkers. Under optimal conditions (APTES 0.75%, sonication time 2.
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Int J Biol Macromol
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College of Food Science and Light Industry, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing, Jiangsu 211816, China.. Electronic address:
Inulin can be hydrolyzed by inulinases to yield inulo-oligosaccharides (IOSs), which have great application potential in the food and nutraceutical industries. However, conventional enzymatic production of IOSs is limited by long hydrolysis times and poor thermo-stability of inulinases. Here, the self-assembling protein scaffold EutM was engineered to co-immobilize exo-inulinase (EXINU) and endo-inulinase (ENINU) for synergistic hydrolysis of inulin to produce IOSs with 3 to 5 monosaccharide units (DP3-5 IOSs).
View Article and Find Full Text PDFGlutaraldehyde functionalization of halloysite nanoclay enhances immobilization efficacy of endoinulinase for fructooligosaccharides production from inulin.
Food Chem
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Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147 002, Punjab, India.
Current work describes the enhancement of immobilization efficacy of Aspergillus tritici endoinulinase onto halloysite nanoclay using crosslinker glutaraldehyde. Under statistical optimized immobilization conditions, viz. glutaraldehyde 1.
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a Department of Applied Microbiology and Biotechnology , Dr. Harisingh Gour University, Sagar (M.P.) , India.
Among microbial enzymes, inulinases or fructo-furanosylhydrolases have received considerable attention in the past decade, and as a result, a variety of applications based on enzymatic hydrolysis of inulin have been documented. Inulinases are employed for generation of fructose and inulo-oligosaccharides (IOS) in a single-step reaction with specificity. The high fructose syrup can be biotransformed into value-added products such as ethanol, single cell protein, while IOS are indicated in nutraceutical industry as prebiotic.
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Appl Biochem Biotechnol
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State Key Laboratory of Bioreactor Engineering, Department of Food Science and Technology, School of Biotechnology, East China University of Science and Technology, 130 # Meilong Rd, P. O. Box 283, Shanghai, 200237, People's Republic of China.
In this study, an endoinulinase gene from Aspergillus fumigatus was cloned and overexpressed in Pichia pastoris. A maximum activity, 3860 U/ml, of the recombinant endoinulinase was obtained by using a high cell-density fermentation approach. The recombinant endoinulinase with a molecular weight of 58 kDa was purified for further enzymatic investigation.
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