Abstract
Backgroundβ-Galactosidase is a vital enzyme with diverse application in molecular biology and industries. It was covalently attached onto functionalized graphene nano-sheets for various analytical applications based on lactose reduction.Methodology/Principal FindingsResponse surface methodology based on Box-Behnken design of experiment was used for determination of optimal immobilization conditions, which resulted in 84.2% immobilization efficiency. Native and immobilized functionalized graphene was characterized with the help of transmission and scanning electron microscopy, followed by Fourier transform infrared (FTIR) spectroscopy. Functionalized graphene sheets decorated with islands of immobilized enzyme were evidently visualized under both transmission and scanning electron microscopy after immobilization. FTIR spectra provided insight on various chemical interactions and bonding, involved during and after immobilization. Optimum temperature and energy of activation (Ea) remains unchanged whereas optimum pH and Km were changed after immobilization. Increased thermal stability of enzyme was observed after conjugating the enzyme with functionalized graphene.SignificanceImmobilized β-galactosidase showed excellent reusability with a retention of more than 92% enzymatic activity after 10 reuses and an ideal performance at broad ranges of industrial environment.
Highlights
Introduction bGalactosidase is an enzyme of industrial importance and has two main commercial applications in food technology; the reduction of lactose in dairy commodities for safe consumption by lactose intolerant peoples and production of galacto-oligosaccharides (GOS) via transgalactosylation reaction for a balanced gastrointestinal flora preservation.Lactose, an integral component of breast milk, causes a discomfort in most of the children and adolescent peoples worldwide, in terms of abdominal pain, nausea, flatulence and bloating
This damage could be reduced significantly by pre-treatment of enzyme with lactose, which shields the active site from deformation during immobilization process through steric effects [34]
Pretreatment of Chick pea b-galactosidase (CpGAL) with lactose was done before starting any immobilization experiments
Summary
Introduction bGalactosidase is an enzyme of industrial importance and has two main commercial applications in food technology; the reduction of lactose in dairy commodities for safe consumption by lactose intolerant peoples and production of galacto-oligosaccharides (GOS) via transgalactosylation reaction for a balanced gastrointestinal flora preservation.Lactose, an integral component of breast milk, causes a discomfort in most of the children and adolescent peoples worldwide, in terms of abdominal pain, nausea, flatulence and bloating. Galactosidase is an enzyme of industrial importance and has two main commercial applications in food technology; the reduction of lactose in dairy commodities for safe consumption by lactose intolerant peoples and production of galacto-oligosaccharides (GOS) via transgalactosylation reaction for a balanced gastrointestinal flora preservation. Galacto-oligosaccharides (GOS) are non-digestible sugars containing two to five molecules of galactose and one molecule of glucose or lactose connected through glycosidic bonds. Transgalactosylation dominates early in the reaction, producing GOS with a high yield. Health benefit offers by GOS includes reduction of detrimental bacteria [1,2], promoting of vitamin producing flora [3], prevention of constipation and increase in mineral absorption [4], GOS have shown to be very stable at high temperatures and low pH. GOS can be used in a variety of products, including fermented milk products, breads, jams, confectionery, beverages, etc [5]
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