Abstract
A demineralized bovine bone was hydrolyzed by a specific bone-degrading collagenolytic protease extracted from Bacillus cereus MBL13 (isolated from chopped animal bone wastes) to utilize its collagen in nutraceuticals with high calcium bioavailability. Bovine bone peptide (BBP), a novel oligophosphopeptide with a high calcium binding ability (8.25 mmol/g-protein), was isolated from bovine bone hydrolysates by Chelex 100, ultrafiltration, hydroxyapatite chromatography, gel filtration chromatography, and reverse-phase high performance liquid chromatography. The results showed that demineralization treatment can significantly increase hydrolysis (p < 0.05). The amino acid content of BBP showed that the Asp, Ala, Tyr, and Thr contents were remarkable increments compared to the bone hydrolysates. The molecular mass of BBP was found to be around 3.305 kDa through SDS-PAGE and MALDI-TOF mass spectrometry. FT-IR spectra showed characteristic absorption peaks. Moreover, BBP exhibited higher calcium binding activity than that of casein oligophosphopeptide (CPP). Therefore, this study demonstrated that B. cereus MBL13 collagenolytic protease (BCC) could degrade bovine bone collagen, and prepared oligophosphopeptide could be utilized as a nutraceutical with high calcium-binding activity.
Highlights
Collagens and their peptide fragments are produced in large quantities as by-products of livestock and poultry industries
We report the hydrolysis of bovine bone by the collagenolytic protease secreted from B. cereus MBL13, the preparation of phosphopeptide with high affinity to calcium
The specific enzymatic hydrolysis of B. cereus MBL13 collagenolytic protease (BCC) was examined in comparison to various proteinases, which are commonly used in protein hydrolysis [30,31,32]
Summary
Collagens and their peptide fragments are produced in large quantities as by-products of livestock and poultry industries. Many studies have identified the structure, function, and biological activities of bone collagen and its peptides [5,6,7,8]. More than 5 million tons of bovine bone wastes are discarded annually in China as inedible byproducts. The development of environment-friendly treatment of waste animal bones for obtaining collagens and their peptide fragments has received significant attention. Protein, of which most is collagen, accounts for approximately 25%–30% of the gross weight of bovine bones. Bovine bone may be a good resource for high quality collagen products. Type I collagen has been successfully extracted from bovine bones, and the hydrolysis of collagen protein has been conducted using proteases. The recycling of collagen from animal bone wastes has received significant research interest that mainly focuses on enzyme hydroxylation. An urgent demand for developing biotechnological alternatives to such waste recycling exists
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