Premium
Valorization of S al Deoiled Cake as Media for Acidic Amylase and Invertase Co‐Production by A spergillus niger NJ ‐1: Optimization by Response Surface Methodology and Application in Oligosaccharide Synthesis
Author(s) -
Singh Samsher,
Gupta Neetu,
Kaur Jasdeep,
Gupta Anshu
Publication year - 2015
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/jfpp.12505
Subject(s) - invertase , amylase , hydrolysis , chemistry , aspergillus niger , starch , food science , maltose , response surface methodology , enzyme , central composite design , biochemistry , chromatography
Valorization of S al deoiled cake ( DOC ) was studied by using it as cheap nutrient source for the co‐production and statistical optimization of two carbohydrases, acidic amylase and invertase, using a newly isolated strain A spergillus niger NJ ‐1 and assessment of produced enzymes in oligosaccharides synthesis. Initially, 4% (w/v) of S al DOC and incubation time of 120 h were found to be the best for optimum enzymes production. Statistical optimization using P lackett– B urman design involved 11 important variables among which five were further optimized by central composite design. Peptone played important role in enzymes co‐production. Both enzymes were stable at acidic pH of 3.0 and 50 C temperature. After optimization, amylase and invertase titers increased to ninefold (9.63 IU/mL ) and 19‐fold (9.96 IU/mL ) compared with unoptimized conditions. Amylase produced maltotrioses and maltopentoses while invertase was able to form kestose during enzymatic hydrolysis. Practical Applications Acidic amylase and invertase co‐produced may find suitable applications in starch hydrolysis and confectionary industries. Peptone interaction may unlock molecular switch between production levels of two industrially important enzymes. This is the first report on the use of forest by‐product S al deoiled cake as media for simultaneous production of acidic amylase and invertase.