Fermentation by Bacillus siamensis BSJ-2 degrades Cruciferin to improve bioactive peptides and essential amino acids in rapeseed meal

Abstract Background Rapeseed meal is an economical agricultural by-product with a high protein content. The main storage protein Cruciferin accounts for about 60% crude protein, but is difficult to be digested. The nutritional value of rapeseed meal is constrained by the low digestibility of Cruciferin. Results We identified Bacillus siamensis BSJ-2 as a potent Cruciferin-degrading strain and demonstrated that fermentation with B. siamensis BSJ-2 substantially improved the protein quality and value of rapeseed meal. Peptidomic analysis revealed a marked increase in the abundance and diversity of total peptides following B. siamensis BSJ-2 fermentation. Notably, a series of newly identified Cruciferin-derived peptides containing the sequence motif SYDLPILRFLRL were specifically enriched in B. siamensis BSJ-2-fermented rapeseed meal and exhibited antioxidant activity. Furthermore, targeted metabolomic analysis demonstrated a pronounced increase in several essential amino acids after B. siamensis BSJ-2 fermentation. Conclusions Our findings demonstrate that fermentation with B. siamensis BSJ-2 can effectively remodel the protein-derived peptide and amino acid profiles of rapeseed meal, enhancing the generation of potential bioactive peptides and essential amino acids. This study provides new insights into the value-added bioconversion of rapeseed meal and establishes a promising microbial fermentation strategy for developing high-protein, nutritionally enhanced feed ingredients.

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Journal
BMC Microbiology
Published
2026-10-16
DOI
https://doi.org/10.1186/s12866-026-05784-0
Primary Topic
Protein Hydrolysis and Bioactive Peptides
Type
article
Field-Weighted Citation Impact
0.00

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article

Fermentation by Bacillus siamensis BSJ-2 degrades Cruciferin to improve bioactive peptides and essential amino acids in rapeseed meal

Siyue Wang, Fangfei Yun, Tianwei Wang, Kunling Teng et al.
BMC Microbiology
Protein Hydrolysis and Bioactive Peptides
article

Fermentation by Bacillus siamensis BSJ-2 degrades Cruciferin to improve bioactive peptides and essential amino acids in rapeseed meal

Siyue Wang, Fangfei Yun, Tianwei Wang, Kunling Teng, Jin Zhong, Sijie Jin, Jie Zhang, Tianqi Xia
article en

Abstract

Abstract Background Rapeseed meal is an economical agricultural by-product with a high protein content. The main storage protein Cruciferin accounts for about 60% crude protein, but is difficult to be digested. The nutritional value of rapeseed meal is constrained by the low digestibility of Cruciferin. Results We identified Bacillus siamensis BSJ-2 as a potent Cruciferin-degrading strain and demonstrated that fermentation with B. siamensis BSJ-2 substantially improved the protein quality and value of rapeseed meal. Peptidomic analysis revealed a marked increase in the abundance and diversity of total peptides following B. siamensis BSJ-2 fermentation. Notably, a series of newly identified Cruciferin-derived peptides containing the sequence motif SYDLPILRFLRL were specifically enriched in B. siamensis BSJ-2-fermented rapeseed meal and exhibited antioxidant activity. Furthermore, targeted metabolomic analysis demonstrated a pronounced increase in several essential amino acids after B. siamensis BSJ-2 fermentation. Conclusions Our findings demonstrate that fermentation with B. siamensis BSJ-2 can effectively remodel the protein-derived peptide and amino acid profiles of rapeseed meal, enhancing the generation of potential bioactive peptides and essential amino acids. This study provides new insights into the value-added bioconversion of rapeseed meal and establishes a promising microbial fermentation strategy for developing high-protein, nutritionally enhanced feed ingredients.

BMC Microbiology
Chinese Academy of Sciences (CN), Institute of Microbiology (CN), University of Chinese Academy of Sciences (CN), Dezhou University (CN)
National Key Research and Development Program of China
Zero hunger
Openalex Percentile: Top 24%
Protein Hydrolysis and Bioactive Peptides
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