Year: 2021 | Month: December | Volume 11 | Issue 6
Standardization of Optimum Conditions for Hydrolyses of Goat Milk Whey Protein with Trypsin Enzyme
Apoorva Argade
Satyavir Singh Ahlawat
DOI:10.30954/2277-940X.06.2021.24
Abstract:
Goat milk is as close to perfect food as possible in nature and was known as “the king of milk” in the world, but the development of functional foods from goat milk has been slow compared to cow and buffalo milk. The study was conducted with an objective to develop a goat milk whey protein hydrolysate (GMWPH) with enhanced antioxidant property and better Ca+ chelating activity. Goat milk whey protein was digested with commercial food-grade Trypsin enzyme under various conditions of incubation temperature (30 to 70 °C), incubation time (30 to 300 min), enzyme concentration level (0.25 to 2%) and pH (6 to 10) of the enzyme reaction to achieve the best hydrolysis. The hydrolysates were analyzed for degree of hydrolysis (DH), antioxidant activity (ABTS) and calcium chelating capacity. It was found that treatment with trypsin at 40 °C incubation temperature, 180 min incubation time, 1.0% enzyme concentration and 8.0 pH effectively degraded the goat milk whey proteins, as determined by SDS-PAGE and measurement of nonprotein nitrogen content. Hydrolysis with trypsin resulted in a significant increase in antioxidant and Ca+ chelation property. Hence, the GMWPH may be useful for development of novel foods for infants, and the elderly osteoporosis patients to replace cow milk.Goat milk is as close to perfect food as possible in nature and was known as “the king of milk” in the world, but the development of functional foods from goat milk has been slow compared to cow and buffalo milk. The study was conducted with an objective to develop a goat milk whey protein hydrolysate (GMWPH) with enhanced antioxidant property and better Ca+ chelating activity. Goat milk whey protein was digested with commercial food-grade Trypsin enzyme under various conditions of incubation temperature (30 to 70 °C), incubation time (30 to 300 min), enzyme concentration level (0.25 to 2%) and pH (6 to 10) of the enzyme reaction to achieve the best hydrolysis. The hydrolysates were analyzed for degree of hydrolysis (DH), antioxidant activity (ABTS) and calcium chelating capacity. It was found that treatment with trypsin at 40 °C incubation temperature, 180 min incubation time, 1.0% enzyme concentration and 8.0 pH effectively degraded the goat milk whey proteins, as determined by SDS-PAGE and measurement of nonprotein nitrogen content. Hydrolysis with trypsin resulted in a significant increase in antioxidant and Ca+ chelation property. Hence, the GMWPH may be useful for development of novel foods for infants, and the elderly osteoporosis patients to replace cow milk.
Highlights
- Bioactive peptides can be produced from goat milk whey proteins with trypsin enzymatic hydrolyzation under controlled conditions.
- These hydrolyzed peptides increased antioxidant properties and worked as nanotubes for calcium binding.
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