# Unlocking the Functional Potential of Pecan Nut Cake: A Study on Bioactive Peptide Production

**Authors:** Tianjing Long, Yingjie Xu, Ziang Li, Weimei Kong, Yibo Zhu, Mingxuan Tao, Haibo Luo, Li Cui, Mingjun Sun, Zhen Wu, Xiaoqun Zeng, Daodong Pan, Yuxing Guo

PMC · DOI: 10.3390/foods15020323 · 2026-01-15

## TL;DR

This study shows that fermenting pecan nut cake with specific bacteria increases its health benefits, including antioxidant and enzyme-inhibiting properties.

## Contribution

The study identifies two new bioactive peptides from fermented pecan nut cake with antioxidant and α-glucosidase inhibitory activities.

## Key findings

- Fermented pecan nut cake showed higher antioxidant and α-glucosidase inhibitory activities compared to the unfermented control.
- Two bioactive peptides, FAGDDAPR and LAGNPDDEFRPQ, were identified and shown to reduce oxidative stress in Caco-2 cells.
- Molecular docking suggested interactions of the peptides with superoxide dismutase, Keap1, and α-glucosidase.

## Abstract

This study examined whether co-fermentation with Lactobacillus casei CGMCC 15956 and Lactobacillus delbrueckii CGMCC 21287 could enhance the bioactivity of peptides derived from pecan nut cake (PNC) and clarify the underlying mechanisms. The fermented hydrolysate (PNCH) was compared with an unfermented control. PNCH showed higher antioxidant and α-glucosidase inhibitory activities. Total antioxidant capacity increased from 3.17 to 4.81 mM Trolox, and DPPH radical scavenging activity increased from 62.69% to 84.12%. In addition, the IC50 value for α-glucosidase inhibition decreased from 7.549 to 4.509 mg/mL. In a mouse model of acute alcohol-induced liver injury, PNCH significantly alleviated liver damage through the synergistic enhancement of antioxidant and α-glucosidase inhibitory activities. Peptidomic analysis identified two representative bioactive peptides, FAGDDAPR (from actin) and LAGNPDDEFRPQ (from cupin domain–containing protein 1), both of which exhibited antioxidant and α-glucosidase inhibitory activities. Additionally, these peptides alleviated H2O2-induced oxidative stress in Caco-2 cells, significantly improving GSH and MDA levels, as well as SOD activity. Molecular docking suggested potential interactions of these peptides with superoxide dismutase, Keap1, and α-glucosidase. These findings support the high-value utilization of PNC and the development of functional peptide-based ingredients.

## Linked entities

- **Proteins:** ACTIN (hypothetical protein), KEAP1 (kelch like ECH associated protein 1)
- **Chemicals:** H2O2 (PubChem CID 784), GSH (PubChem CID 124886), MDA (PubChem CID 1614), Trolox (PubChem CID 40634)

## Full-text entities

- **Diseases:** liver damage (MESH:D056486), liver injury (MESH:D017093)
- **Chemicals:** DPPH (MESH:C004931), alcohol (MESH:D000438), H2O2 (MESH:D006861), MDA (MESH:D015104), GSH (MESH:D005978), Trolox (MESH:C010643), PNCH (-)
- **Species:** Mus musculus (house mouse, species) [taxon 10090]

## Figures

3 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12841524/full.md

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Source: https://tomesphere.com/paper/PMC12841524