Collagen peptides are extensively applied in cosmetics and health products, primarily prepared through physical and chemical degradation methods.In comparison, enzymatic degradation for collagen peptide production offers significant advantages such as mild degradation conditions and controllable molecular weight.This study aimed to explore and achieve efficient expression and preparation of a collagenase with commercial potential, derived from Bacillus cereus, for enzymatic collagen peptide synthesis.Initially, the gene encoding collagenase ColVD021 from Bacillus cereus was synthesized with codon optimization.Through N-terminal sequence truncation optimization, the active expression of ColVD021-Δ30 was achieved in Escherichia coli (8.96±0.21) U/mL.Further enhancement of ColVD021-Δ30 expression levels to (16.24±0.21) U/mL was achieved by optimizing the addition of metal ions Zn2+ and Ca2+.The optimal pH and temperature for ColVD021-Δ30 were determined to be 7.5 and 37 ℃, respectively.Enzymatic hydrolysis results demonstrated that recombinant ColVD021-Δ30 exhibited high degradation activity on collagen from different sources, yielding collagen peptide molecules with molecular weights below 1 000 Da.Additionally, enzymatic digestion of agricultural by-product chicken breast cartilage indicated that ColVD021-Δ30 could directly hydrolyze crushed fresh chicken breast cartilage to produce collagen peptides.This study realized efficient expression of Bacillus cereus collagenase and established an enzymatic process for collagen peptide production, offering a solution for industrial-scale enzymatic synthesis of collagen peptides.
LIU Ping
,
XU Ruirui
,
HUANG Hao
,
TANG Yao
,
WANG Yang
,
KANG Zhen
. Heterologous expression of collagenase from Bacillus cereus and enzymatic production of collagen peptides[J]. Food and Fermentation Industries, 2025
, 51(7)
: 9
-15
.
DOI: 10.13995/j.cnki.11-1802/ts.038998
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