Download full-text PDF

Source

Publication Analysis

Top Keywords

stabilization protease
4
protease properties
4
properties chitosan
4
chitosan immobilized
4
immobilized enzymes
4
stabilization
1
properties
1
chitosan
1
immobilized
1
enzymes
1

Similar Publications

Ubiquitination of OsCSN5 by OsPUB45 activates immunity by modulating the OsCUL3a-OsNPR1 module.

Sci Adv

January 2025

State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.

The COP9 signalosome (CSN) is a highly conserved protein complex in eukaryotes, with CSN5 serving as its critical catalytic subunit. However, the role of CSN5 in plant immunity is largely unexplored. Here, we found that suppression of in rice enhances resistance against the fungal pathogen and the bacterial pathogen pv.

View Article and Find Full Text PDF

Carboxylated nanocellulose from quinoa husk for enhanced protease immobilization and stability of protease in biotechnological applications.

Sci Rep

January 2025

Department of Nanotechnology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran.

Herein, an efficient and feasible approach was developed to oxidize low-cost agricultural waste (quinoa husk, QS) for the synthesis of carboxylated nanocellulose (CNC). The as-prepared rod-like CNCs (average diameter of 10 nm and length of 103 nm) with a high specific surface area (173 m/g) were utilized for the immobilization of a model protease enzyme (PersiProtease1) either physically or via covalent attachment. For chemical immobilization, CNCs were firstly functionalized with N, N'-dicyclohexylcarbodiimide (DCC) to provide DCNCs nanocarrier which could covalently bond to enzyme trough nucleophilic substitution reaction and formation of the amide bond between DCNCs and enzyme.

View Article and Find Full Text PDF

Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy.

Nat Commun

January 2025

Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Croix du sud 4-5, L7.07.07, Louvain-la-Neuve, Belgium.

The SARS-CoV-2 spike protein's membrane-binding domain bridges the viral and host cell membrane, a critical step in triggering membrane fusion. Here, we investigate how the SARS-CoV-2 spike protein interacts with host cell membranes, focusing on a membrane-binding peptide (MBP) located near the TMPRSS2 cleavage site. Through in vitro and computational studies, we examine both primed (TMPRSS2-cleaved) and unprimed versions of the MBP, as well as the influence of its conserved disulfide bridge on membrane binding.

View Article and Find Full Text PDF

Background: The unavoidable propagation of the coronavirus disease 2019 (COVID-19), caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has underscored the urgent requirement for efficacious therapeutic agents. The dried fruit of Retz., namely Chebulae Fructus, is widely used for treating bacterial and viral infectious diseases, which was witnessed to perform anti-SARS-CoV-2 activity in recommended Chinese patent medicine.

View Article and Find Full Text PDF

Antimicrobial peptides (AMPs) show potential as antibiotic alternatives for bacterial infections; nevertheless, the susceptibility to proteases limits their broader utilization. This study developed engineered lipopeptides using antienzymolysis modifications and cysteine (Cys)-dimerization strategy. As the key parameters for the functioning of AMPs, hydrophobicity and positive charges were concentrated within the peptide sequence by adjusting the intermolecular disulfide bond placement to study their distribution effects.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!