{"title":"<i>Desulfovibrio</i> ‐Hydrogen Sulfide Mediates Capsaicin‐Induced Oxidative Stress and Gut Inflammation via TXNIP/NLRP3 Pathway","authors":"Liangliang Zhu, Xiangru Feng, Xiaoxuan Lu, Geng Han, Jiaqi Zou, Zhaoyang Dong, Ting Luo, Jiayang Jin, Mengyao Zhao, Xiaoguo Ji, Liming Zhao","doi":"10.1002/fbe2.70047","DOIUrl":"https://doi.org/10.1002/fbe2.70047","url":null,"abstract":"ABSTRACT The intake of capsaicin can disrupt the gut microecology and impact health, yet its underlying mechanism is not fully elucidated. This study, by establishing capsaicin‐induced human microbiota‐associated (HMA) mouse models revealed the molecular mechanism by which capsaicin perturbs the gut microbiota and metabolites, leading to intestinal barrier dysfunction, inflammation, and oxidative stress. This study demonstrated that capsaicin intake significantly increased the abundance of Desulfovibrio and raised the level of hydrogen sulfide (H 2 S). Concurrently, the abundance of Faecalibacterium prausnitzii , which shared a symbiotic relationship with Desulfovibrio , also increased. These changes resulted in impaired intestinal barrier function, oxidative stress, and inflammation. Through microbe‐colonization and chromate (an H 2 S inhibitor) intervention experiments, it was confirmed that H 2 S, the metabolite of Desulfovibrio , mediated oxidative stress and triggered capsaicin‐induced gut inflammation by activating the Thioredoxin‐interacting protein (TXNIP)/NOD‐like receptor thermal protein domain‐associated protein 3 (NLRP3) pathway. This study elucidated the mechanism by which capsaicin impaired gut health via the Desulfovibrio ‐H 2 S‐TXNIP/NLRP3 pathway. It also provided a new target for improving and preventing intestinal health problems caused by dietary capsaicin.","PeriodicalId":515945,"journal":{"name":"Food Bioengineering","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/fbe2.70047","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147381542","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Computer‐Aided Functional Oligosaccharide Screening and the Regulatory Role in Lipid Metabolism","authors":"Rui Jing, Shanshan Deng, Mengyao Zhao, Liming Zhao","doi":"10.1002/fbe2.70042","DOIUrl":"https://doi.org/10.1002/fbe2.70042","url":null,"abstract":"ABSTRACT This study investigated the lipid‐lowering effects and intervention mechanisms of structurally diverse functional oligosaccharides on non‐alcoholic fatty liver disease (NAFLD). By integrating computational tools such as molecular docking and molecular dynamics simulations (MDS), a comprehensive “in silico‐in vitro‐in vivo” tri‐dimensional screening and validation model was established that targeted the key lipid metabolism regulators peroxisome proliferator‐activated receptor alpha (PPARα) and peroxisome proliferator‐activated receptor gamma (PPARγ). This model successfully identified xylobiose and raffinose as candidate oligosaccharides with potential lipid‐lowering activity. Molecular docking was employed to elucidate the binding mechanisms between these oligosaccharides and their target proteins, highlighting the high structural stability of the PPARα‐ and PPARγ‐oligosaccharide complexes. Moreover, both the in vitro and in vivo models demonstrated that xylobiose and raffinose ameliorated hepatic lipid accumulation by inhibiting liver lipogenesis and modulating fatty acid oxidation to restore lipid homeostasis. The results demonstrated the reliability and robustness of the integrated computational‐experimental screening strategy, providing a transferable research paradigm for the targeted discovery of functional oligosaccharides and elucidating their underlying mechanisms.","PeriodicalId":515945,"journal":{"name":"Food Bioengineering","volume":"5 1","pages":"14-29"},"PeriodicalIF":0.0,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/fbe2.70042","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147878821","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yi Liu, Yu Xie, Xingyu Shen, Shihui Wang, Yi Xiong, Guimin Zhang
{"title":"Multiple Strategies for Recombinant Expression of Human Chymotrypsinogen C in <i>Pichia Pastoris</i>","authors":"Yi Liu, Yu Xie, Xingyu Shen, Shihui Wang, Yi Xiong, Guimin Zhang","doi":"10.1002/fbe2.70034","DOIUrl":"https://doi.org/10.1002/fbe2.70034","url":null,"abstract":"ABSTRACT Chymotrypsin C (CTRC) is a multifunctional serine protease that have shown great application potential in the field of food processing. This study aims to efficiently express CTRC in Pichia pastoris and provide a safe and highly effective new enzyme formulation for the food industry. Here, we successfully expressed and secreted human chymotrypsinogen C (proCTRC) in P. pastoris through multiple strategies. First, we replaced the native AOX1 promoter with the stronger HpFMD promoter and used ribosomal DNA (rDNA) loci for gene integration to achieve significant expression and secretion of proCTRC. In addition, we designed a mutant pro2M that prevented host protease cleavage by replacing the dipeptide motif “KR” with “EK”. The enzyme activity of wild type and mutant pro2M in the fermentation supernatant reached 0.59 ± 0.003 U/mL and 3.94 ± 0.27 U/mL, respectively. Meanwhile, the mutant showed a specific activity of 54.84 U/mg, 3.3‐fold higher than the wild type's 16.6 U/mg. Further, the recombinant pro2M and proCTRC can exhibite good stability under neutral pH conditions. In summary, we have established P. pastoris as a powerful platform for high‐yield CTRC production and highlighted the importance of engineering protease‐resistant variants to optimize enzyme secretion and activity.","PeriodicalId":515945,"journal":{"name":"Food Bioengineering","volume":"4 4","pages":"407-415"},"PeriodicalIF":0.0,"publicationDate":"2025-11-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/fbe2.70034","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147877819","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Development of <i>Komagataella phaffii</i> Cell‐Free Protein Synthesis Using Cell From Basic Salt Medium","authors":"Yuxin Zhang, Yue Wang, Wenjie Cong, Hualan Zhou, Jianguo Zhang","doi":"10.1002/fbe2.70030","DOIUrl":"https://doi.org/10.1002/fbe2.70030","url":null,"abstract":"ABSTRACT Cell‐free protein synthesis (CFPS) offers a promising option of enzyme production for food bioengineering, with the advantages of eliminating the steps of recombinant microbial cell construction, rapid protein synthesis process, and high throughput of various proteins simultaneously. Komagataella phaffii CFPS is highlighted for its high level of protein synthesis, successfully harnessing the native strong alcohol oxidase 1 promoter in the absence of T7 RNA polymerase. Currently, K. phaffii CFPS uses cell extract from complex medium cultivated K. phaffii cells, which is still high‐cost and limits large‐scale cell extract preparation industrially. This study developed a K. phaffii CFPS using chemically defined medium through optimization of protein concentration in cell extracts, a new cell extract preparation method S603, which simplified the process and enhanced the protein concentration in cell extract, and optimization of methanol induction time. Finally, K. phaffii CFPS using cell extract from chemically defined medium cultivation exhibited 90.8 mg/mL total protein in cell extract and synthesized 600.0 mg/L GFP, which was the highest value until now. This successful K. phaffii CFPS provided a cost‐effective and high‐level expression platform for enzyme production for food bioengineering.","PeriodicalId":515945,"journal":{"name":"Food Bioengineering","volume":"4 4","pages":"502-510"},"PeriodicalIF":0.0,"publicationDate":"2025-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/fbe2.70030","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147906958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}