Process Biochemistry最新文献_第10页

Understanding selenoproteins: Structural insights, biological functions and transformative applications in therapeutics

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-03 DOI: 10.1016/j.procbio.2024.12.028

Bhairav Prasad , Akanksha Akanksha , Palki Sahib Kaur , Saurabh Gupta

{"title":"Understanding selenoproteins: Structural insights, biological functions and transformative applications in therapeutics","authors":"Bhairav Prasad , Akanksha Akanksha , Palki Sahib Kaur , Saurabh Gupta","doi":"10.1016/j.procbio.2024.12.028","DOIUrl":"10.1016/j.procbio.2024.12.028","url":null,"abstract":"<div><div>Present study summarizes the key role of selenoproteins in biological processes, their therapeutic potential, and the implications of their dysfunction in various diseases. Selenoproteins play a vital role in various biological functions, including antioxidative defense, thyroid hormone metabolism, and redox balance maintenance. These proteins are critical for immune responses, muscle development, and cellular integrity. Sophisticated techniques like X-ray crystallography and mass spectrometry have been used to characterize their structures and interactions. Selenoproteins have promising applications in medicine as therapeutic agents and nutritional supplements for cancer, cardiovascular disorders, immune function, mitochondrial health, and neurodegenerative diseases. Deficiencies in dietary selenium or mutations in selenoproteins can lead to disorders such as cancer, Kashin-Beck disease, Keshan disease, atherosclerosis, and DNA damage. This review covers the occurrence, diversity, biological roles, and therapeutic potential of selenoproteins in health and disease. In conclusion, selenoproteins are essential for maintaining cellular homeostasis and overall health, with their diverse biological roles, therapeutic potential, and association with various diseases. Future research should focus on further elucidating the molecular mechanisms underlying selenoprotein function, optimizing their therapeutic applications, and exploring novel strategies for preventing and treating selenoprotein-related diseases.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 148-160"},"PeriodicalIF":3.7,"publicationDate":"2025-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099610","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Oceanobacillus in high-temperature Daqu: Taxonomic diversity, metabolic characteristics and biofortification effect

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2025-01-02 DOI: 10.1016/j.procbio.2025.01.002

Xu Liu , Jun-Jie Fu , Han-Jun Shen , Li-Juan Chai , Xiao-Juan Zhang , Hong-Yu Xu , Song-Tao Wang , Su-Yi Zhang , Cai-Hong Shen , Jin-Song Shi , Zhen-Ming Lu , Zheng-Hong Xu

{"title":"Oceanobacillus in high-temperature Daqu: Taxonomic diversity, metabolic characteristics and biofortification effect","authors":"Xu Liu , Jun-Jie Fu , Han-Jun Shen , Li-Juan Chai , Xiao-Juan Zhang , Hong-Yu Xu , Song-Tao Wang , Su-Yi Zhang , Cai-Hong Shen , Jin-Song Shi , Zhen-Ming Lu , Zheng-Hong Xu","doi":"10.1016/j.procbio.2025.01.002","DOIUrl":"10.1016/j.procbio.2025.01.002","url":null,"abstract":"<div><div>High-temperature Daqu (HTD) is a critical component in Jiang-flavor Baijiu production, supplying flavor precursors, enzymes, and diverse microorganisms. Notably, HTD harbors <em>Oceanobacillus</em>, an ecological generalist whose role in the microecosystem remains to be defined. Here, we first identified 21 amplicon sequence variants (ASVs) belonging to six <em>Oceanobacillus</em> species in 20 HTD samples through 16S rRNA gene sequencing. Subsequently, representative strains of eight <em>Oceanobacillus</em> species were selectively isolated from HTD using predicted culture media. These strains exhibited potent enzymatic activities including cellulase and neutral proteinase, alongside diverse metabolic capabilities. Furthermore, we evaluated the impact of <em>Oceanobacillus caeni</em>, the predominant species, on HTD fermentation. Compared to the control, the relative abundance of <em>Oceanobacillus caeni</em> in the biofortified HTD increased significantly, from 3.82 % to 10.25 %, with the biomass of <em>Oceanobacillus caeni</em> surged from 5.15 × 10<sup>8</sup> to 2.95 × 10<sup>9</sup> copies/g. The activities of cellulase and neutral proteinase in the biofortified HTD escalated to 1.20 U and 57.14 U, respectively. The levels of volatile pyrazines and phenols in the biofortified HTD increased by 1.45 and 1.55 times, respectively. Levels of other volatiles including isovaleraldehyde, furfural, isobutyric acid, phenylacetone, ethyl palmitate, and 1,2-dimethoxybenzene saw respective increases of 3.77, 2.26, 1.94, 2.21, 5.21, and 2.27 times. This study sheds light on the role of <em>Oceanobacillus</em> in HTD, offering a theoretical foundation for improving Daqu quality.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 68-79"},"PeriodicalIF":3.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Direct immobilization of an engineered Bacillus subtilis lipase A variant: Evaluation of substrate specificity, solvent stability and peptide synthesis

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-12-31 DOI: 10.1016/j.procbio.2024.12.027

Karen Rodríguez-Núñez , Manuel Barraza , Pamela Vásquez , Claudia Bernal , Ronny Martínez

{"title":"Direct immobilization of an engineered Bacillus subtilis lipase A variant: Evaluation of substrate specificity, solvent stability and peptide synthesis","authors":"Karen Rodríguez-Núñez , Manuel Barraza , Pamela Vásquez , Claudia Bernal , Ronny Martínez","doi":"10.1016/j.procbio.2024.12.027","DOIUrl":"10.1016/j.procbio.2024.12.027","url":null,"abstract":"<div><div>Enzyme-mediated peptide synthesis is a promising alternative for current industrial requirements, mainly due to its potential for increasing process sustainability and efficiency. In this work, peptide synthesis using lipases was studied, and the peptide synthesis activity of a previously reported <em>Bacillus subtilis</em> lipase A (BSLA) variant, P5F3_BSLA (F41L-∆W42-∆D43-R44P) was evaluated. P5F3_BSLA was immobilized on a hydrophilic mesoporous silica support functionalized with glyoxyl groups. A rapid and direct immobilization approach was used from cell culture supernatant in a single vessel without prior protein purification. The effect of immobilization on the performance of P5F3_BSLA regarding substrate specificity, peptide synthesis, and thermal and solvent resistance was evaluated and compared to the WT_BSLA enzyme. The variant showed a similar immobilization yield compared to Wt_BSLA; however, it showed different immobilization kinetics. The P5F3 variant showed an increased solvent resistance in 100 % isopropyl alcohol and an increased activity against long-chain fatty acid substrates. Besides, the P5F3_BSLA variant showed a 1.2-fold increase in glycine polymerization compared to WT_BSLA. The simple, efficient, and successful immobilization of this lipase, its resistance to solvents, and its potential use in peptide synthesis opens an exciting possibility of applications for the industry, highlighting the combination of protein engineering and enzyme immobilization tools to develop biocatalysts with novel properties from widely studied enzymes.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 49-56"},"PeriodicalIF":3.7,"publicationDate":"2024-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099611","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Prospective comparison between mannan-oligosaccharide (MOS) and other hemicellulose-derived oligosaccharides

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-12-31 DOI: 10.1016/j.procbio.2024.12.026

Nadinne Medeiros Assis , Viridiana Santana Ferreira-Leitão , Ayla Sant’Ana da Silva

{"title":"Prospective comparison between mannan-oligosaccharide (MOS) and other hemicellulose-derived oligosaccharides","authors":"Nadinne Medeiros Assis , Viridiana Santana Ferreira-Leitão , Ayla Sant’Ana da Silva","doi":"10.1016/j.procbio.2024.12.026","DOIUrl":"10.1016/j.procbio.2024.12.026","url":null,"abstract":"<div><div>Mannan-oligosaccharides (MOS) are emerging prebiotics composed of mannose residues linked by α- or β-glycosidic bonds. α-MOS are derived from the cell wall of <em>Saccharomyces cerevisiae</em>, while β-MOS can be derived from mannan-rich plants, offering a sustainable approach to obtaining byproducts. To understand the landscape of β-MOS production, this study compares α-MOS and β-MOS with other plant-based oligosaccharides, including xylo-oligosaccharides (XOS) and arabino-(xylan)-oligosaccharides (AOS/AXOS), through scientific, technological, and market surveys. The analysis revealed growing interest in XOS, followed by MOS, and early stages of R&D in AOS/AXOS. Manual curation of MOS studies indicated that β-MOS production is concentrated on sources like konjac and carob, with increasing attention on agro-residues from coffee, coconut, and oil palm industries. The production process often involves enzymatic hydrolysis, highlighting biotechnology's role. The market shows established α-MOS products and the rise of β-MOS. This study identifies research gaps and market opportunities for hemicellulose-derived oligosaccharides, particularly β-MOS.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 33-48"},"PeriodicalIF":3.7,"publicationDate":"2024-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099608","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A novel dual-function biomimetic approach for high throughput organic dye biodegradation and hydrogen peroxide sensing using a nanosized artificial peroxidase with ultra-improved substrate affinity and superb catalytic efficiency

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-12-28 DOI: 10.1016/j.procbio.2024.12.025

Saeed Reza Hormozi Jangi , Zahra Dehghani

{"title":"A novel dual-function biomimetic approach for high throughput organic dye biodegradation and hydrogen peroxide sensing using a nanosized artificial peroxidase with ultra-improved substrate affinity and superb catalytic efficiency","authors":"Saeed Reza Hormozi Jangi , Zahra Dehghani","doi":"10.1016/j.procbio.2024.12.025","DOIUrl":"10.1016/j.procbio.2024.12.025","url":null,"abstract":"<div><div>A high throughput novel dual-function biomimetic artificial enzyme-based approach was developed for dye biodegradation and hydrogen peroxide quantification using a nanosized artificial peroxidase with superb catalytic efficiency and ultra-improved substrate affinity compared to the native enzyme. The artificial peroxidase was chemically, kinetically, and biochemically characterized. A high specific activity of 0.0503 UI mg<sup>−1</sup>, an optimal-pH of 4.0, an optimal-temperature of 35 ℃, and a high storage stability for at-least 30 days was determined for this nanozyme. It retained 88.2 % and 90 % of its activity at 60 ℃ (200 min) and 5 cycles, respectively, revealing its high thermal and cycling stability. Its catalytic efficiency and substrate affinity were 3.2-fold and 7.1-order higher than the native peroxidase, respectively. The mechanistic insights were provided for the activity of nanozyme. A dye biodegrading protocol with a yield of 99.1 % (75.2 % after 10 reuses) within 30.0 min was developed and applied for dye degradation from real waters and textile wastewater. An analytical highly sensitive, reproducible, and selective H<sub>2</sub>O<sub>2</sub> biosensor was also designed, providing a linear quantification range over 1.0–180.0 µM, a detection limit of 0.23 µM, and accurate results for milk analysis. This method showed very better figures of merits than reported ones.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 1-20"},"PeriodicalIF":3.7,"publicationDate":"2024-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Sustainable production of polyhydroxybutyrate biopolymers and cellulose microfibers from sugarcane waste

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-12-25 DOI: 10.1016/j.procbio.2024.12.022

Treerat Sooksawat , Ketsaraporn Ngaopok , Surasak Siripornadulsil , Sittipong Amnuaypanich , Marisa Attapong , Wilailak Siripornadulsil

{"title":"Sustainable production of polyhydroxybutyrate biopolymers and cellulose microfibers from sugarcane waste","authors":"Treerat Sooksawat , Ketsaraporn Ngaopok , Surasak Siripornadulsil , Sittipong Amnuaypanich , Marisa Attapong , Wilailak Siripornadulsil","doi":"10.1016/j.procbio.2024.12.022","DOIUrl":"10.1016/j.procbio.2024.12.022","url":null,"abstract":"<div><div>Thermochemically pretreating sugarcane bagasse (SCB) and sugarcane leaves (SCL) at 121 °C generated fermentable sugars that were transformed into polyhydroxybutyrate (PHB) by PHB-producing bacteria. The SCB hydrolysate contained reducing sugars (25.0–26.1 g/L), which were mainly xylose (16.4–17.6 g/L) and glucose (7.8–8.0 g/L). The bacteria used glucose more effectively than xylose and glycerol did, as the maximum PHB contents (% cell dry weight) observed with glucose, xylose, and glycerol were 69.3 %, 16.2 %, and 21.4 %, respectively. After 72 h of incubation, <em>Burkholderia cepacia</em> ASL22 and <em>Priestia megaterium</em> ASL11, KKR5, and SRB3 converted 50 % of the SCB hydrolysate in E2 broth into PHB, and the maximum weight (1.97 g/L) and content (32.6 %) of PHB were obtained with <em>B. cepacia</em> ASL22. Strain ASL22 also grew on E2 agar, producing 56.0 g/L PHB when 10 % SCB hydrolysate and 0.3 % (v/v) glycerol were used as cosubstrates. Furthermore, combining alkaline treatment, xylanase hydrolysis, and NaClO<sub>2</sub> bleaching converted SCB and SCL into high-purity cellulose microfibers (CMF) with a low yield (31 %). After peroxide bleaching, alkaline treatment and sonication, the CMF yields ranged from 88.3 % to 95.1 %, but some lignin and hemicellulose remained. Thus, sugarcane waste can be processed biologically and physicochemically to produce value-added products, thereby reducing pollution.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 134-147"},"PeriodicalIF":3.7,"publicationDate":"2024-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Designing a cost-effective and scalable expression platform for highly efficient recombinant endo-β-N-acetylglucosaminidase H using fed-batch strategy in E. coli

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-12-24 DOI: 10.1016/j.procbio.2024.12.019

Shilpa Mohanty, Babbal, Mohini Talwar, Shivani Chauhan, Priya Sinha, Shubham Sharma, Yogender Pal Khasa

{"title":"Designing a cost-effective and scalable expression platform for highly efficient recombinant endo-β-N-acetylglucosaminidase H using fed-batch strategy in E. coli","authors":"Shilpa Mohanty, Babbal, Mohini Talwar, Shivani Chauhan, Priya Sinha, Shubham Sharma, Yogender Pal Khasa","doi":"10.1016/j.procbio.2024.12.019","DOIUrl":"10.1016/j.procbio.2024.12.019","url":null,"abstract":"<div><div><em>N</em>-glycosylation of proteins is a complex post-translational phenomenon critical in key cellular processes. Anomalies in protein glycosylation leads to the onset of disease. Therefore, it necessitates stringent monitoring of glycosylation patterns in recombinant proteins as the <em>N</em>-glycans modulate their pharmacokinetics, stability, activity, and immunogenicity. <em>N-</em>glycans characterization requires their enzymatic removal before subjecting them to mass spectrometry. Endo-β-<em>N</em>-acetylglucosaminidase H (Endo H) is one such deglycosylating enzyme that cleaves between the <em>N</em>-acetylglucosamine residue in the <em>N</em>-glycan’s di-<em>N</em>-acetylchitobiose core. Due to its commercial importance in therapeutics, we targeted a high-level <em>Streptomyces plicatus</em> Endo H expression in <em>Escherichia coli</em>. The Endo H gene was cloned under the T7 promoter containing an N-terminal 6X His tag. Shake flask expression studies in TB glucose medium resulted in 220.54 mg/L of recombinant Endo H with a specific product yield (Y<sub>P/X</sub>) of 78.07 mg/g DCW. It was purified using Ni-NTA chromatography with a recovery and purity yield of 84 % and 95 %, respectively. The specific activity of the enzyme calculated using glycoprotein RNase B as the substrate was 3.43 × 10<sup>5</sup> U/mg. It showed remarkable catalytic performance as it deglycosylated denatured RNase B even at an E:S (enzyme: substrate) ratio of 1:1000 in 1 h. Further, it deglycosylated native RNase B at an E:S ratio of 1: 10,000 with excellent efficacy. Optimization of high cell density fermentation using a fed-batch strategy resulted in a maximum Endo H production of 5.80 g/L with a Y<sub>P/X</sub> of 91.67 mg/g DCW when culture was induced at an OD<sub>600</sub> of 114.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 21-32"},"PeriodicalIF":3.7,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143094488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Research hot spots and development trends of biodegradable plastics

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-12-23 DOI: 10.1016/j.procbio.2024.12.018

Nuohan Wang , Dayi Qian , Xiaona Wang , Yongsheng Li , Tianlong Zheng , Qunhui Wang

{"title":"Research hot spots and development trends of biodegradable plastics","authors":"Nuohan Wang , Dayi Qian , Xiaona Wang , Yongsheng Li , Tianlong Zheng , Qunhui Wang","doi":"10.1016/j.procbio.2024.12.018","DOIUrl":"10.1016/j.procbio.2024.12.018","url":null,"abstract":"<div><div>A workable way to reduce the pollution that conventional waste plastics cause to the environment is to use biodegradable plastics. This study examines the current research trends and future prospects in the field of biodegradable plastics using bibliometric analysis and author keyword cluster visualization. It is highlighted that given the current environment, large-scale production of materials such as polylactic acid (PLA), polybutylene adipate terephthalate (PBAT), and whole-starch-based plastics require improved development of modified and composite materials, additional production lines to accelerate the expansion of current manufacturing capacities, and further process optimization. It is advised to use biomass waste as feedstock for less industrialized polymers like polyhydroxyalkanoates (PHAs), find high-performance bactericides, increase product conversion rates, reduce manufacturing costs, and progressively increase output. Currently, a number of fundamental technical bottlenecks need to be overcome in order to help improve the industrialization level of biodegradable plastics and promote the development of \"waste free\" cities. These bottlenecks include lactide synthesis and purification, PHAs separation and extraction, and the ongoing promotion of the formulation of mandatory standards and policy requirements in downstream application fields.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"150 ","pages":"Pages 80-93"},"PeriodicalIF":3.7,"publicationDate":"2024-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143099607","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Optimization of the conditions for immobilization of crude pectinase on chitin using ultrasound and glutaraldehyde and its application in grape juice clarification 超声-戊二醛固定化粗果胶酶条件的优化及其在葡萄汁澄清中的应用

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-11-28 DOI: 10.1016/j.procbio.2024.11.032

Sohini Bera, Nipona Shill, Bhaskar Jyoti Kalita, Nandan Sit

引用次数: 0

Bioconversion of snakeskin shed into bioactive hydrolysate possessing antioxidant and cell proliferative potential 蛇皮蜕皮转化为具有抗氧化和细胞增殖潜能的生物活性水解产物

IF 3.7 3区生物学

Process Biochemistry Pub Date : 2024-11-27 DOI: 10.1016/j.procbio.2024.11.031

Vijan Lal Vikash , Deena Praveena Kumar , Parthasarathy Baskaran Sujiritha , Ganesan Ponesakki , Suresh Kumar Anandasadagopan , Numbi Ramudu Kamini

{"title":"Bioconversion of snakeskin shed into bioactive hydrolysate possessing antioxidant and cell proliferative potential","authors":"Vijan Lal Vikash , Deena Praveena Kumar , Parthasarathy Baskaran Sujiritha , Ganesan Ponesakki , Suresh Kumar Anandasadagopan , Numbi Ramudu Kamini","doi":"10.1016/j.procbio.2024.11.031","DOIUrl":"10.1016/j.procbio.2024.11.031","url":null,"abstract":"<div><div>The underutilization of keratin-rich snakeskin shed (SS) to produce bioactive hydrolysate has not been explored to prevent oxidative stress, limiting its potential in biomedical and nutritional applications. This study aims to generate SS hydrolysate (SSH) through SS degradation using a keratinase-producing <em>Bacillus altitudinis</em> VK-1120. The contents of protein and amino acid of SSH were 13.93 ± 0.48 and 5.57 ± 0.06 mg/mL, respectively, after 96 h. Morphological and chemical changes before and after bacterial degradation were analysed. The SSH contained 16 amino acids, including eight essential amino acids, and demonstrated significant antioxidant activity, with a maximum efficacy of 4.16 ± 0.03 μg/mL for 2,2-diphenyl-1-picrylhydrazyl and 1319.53 ± 8.32 μg/mL for hydroxyl radical scavenging activity, equivalent to L-ascorbic acid. Furthermore, Fe<sup>2+</sup>- chelation and ferric-reducing antioxidant power were found to be 581.33 ± 3.33 μg/mL of EDTA-Na<sub>2</sub> and 193.4 ± 5.83 μM of ferrous (II) sulphate equivalent<sub>,</sub> respectively. Cell viability and migration analysis showcased the proliferation of fibroblast cells with 50, 200, and 500 ng/mL of SSH at 24 h and a reduction in wound area with increasing SSH concentration. Therefore, SS could be utilized as a bioresource for producing both keratinase and antioxidant-rich hydrolysate for identifying biologically active molecules.</div></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":"149 ","pages":"Pages 10-21"},"PeriodicalIF":3.7,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142745870","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0