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Hydrolysis of galactooligosaccharides by commercial preparations of α‐galactosidase and β‐fruetofuranosidase: Potential for use as dietary additives
Author(s) -
Slominski Bogdan A
Publication year - 1994
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740650310
Subject(s) - hydrolysis , chemistry , food science , biochemistry
In vitro and in vivo studies were conducted with six commercial enzyme preparations (SP249, Energex, Rohament CW, Novozyme 230 and crude α ‐galactosidase) to determine their effectiveness in hydrolysing galactooligosaccharides from soya bean and canola meal in the gastrointestinal tract of poultry. The use of the enzyme invertase to enhance galactoside hydrolysis was also studied. A wide range of α ‐galactosidase activity was observed in vitro , with crude α‐galactosidase from Mortirella vinacea and Novozyme 230 preparation showing the highest activity values of 4.3 and 1.5 nkat mg −1 , respectively. All preparations with the exception of crude α‐galactosidase showed invertase activity which is known to convert raffinose and stachyose to the corresponding di‐and trisaccharide, melibiose and manninotriose. Although the activity of invertase was highest on sucrose, the Novozyme 230 preparation showed activity values of 4.2 and 2.3 nkat mg −1 toward raffinose and stachyose substrates, respectively. De novo synthesis of raffinose was observed when soya bean meal, canola meal or pure sucrose and galactose were incubated with certain enzyme preparations (ie Energex). In general, preparations possessing hydrolytic activity towards galactooligosaccharides showed very little synthesis of raffinose while preparations capable of generating raffinose were very weak in the hydrolysis of galactooligosaccharides. The best result in terms of galactooligosaccharide in vitro hydrolysis of canola and soya bean meal was obtained with a combination of α‐galactosidase and invertase. In the in vivo study with caecectomised hens, hydrolysis of galactooligosaccharides averaged 88% when crude α‐galactosidase (2 g kg −1 ) and invertase (1 g kg −1 ) were added to laying, hen diet containing 200 g soya bean meal per kilogram. A problem identified in the current study was that minerals such as calcium phosphate and calcium carbonate common in poultry diets inhibit the hydrolysis activity of α‐galactosidase, indicating that high levels of activity would be required to yield a response in practical poultry feeding.