Results 11 to 20 of about 12,284 (148)

Bioinformatics Aided Elucidation of Functional and Structural Attributes of Bubalus Arnee Bubalis (BAB) Prochymosin

Food Bioengineering
The aspartic protease prochymosin, found in the abomasum of Bubalus arnee bubalis (BAB), is pivotal in κ‐casein cleavage at the Phe105‐Met106 site, facilitating milk coagulation and cheese production.
Raushan Kumar Jha, Prasun Choudhary, Adarsh Kumar Shukla, Surbhi Panwar, Ashwani Kumar   +4 more
doaj   +2 more sources

Safety evaluation of the food enzyme chymosin from the genetically modified <i>Trichoderma reesei</i> strain DP-Nyj88. [PDF]

EFSA J
Abstract The food enzyme chymosin (EC 3.4.23.4) is produced with the genetically modified Trichoderma reesei strain DP‐Nyj88 by Genencor International BV. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA.
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Van Loveren H, Vernis L, Criado A, Fernàndez-Fraguas C, Peluso S, Liu Y.   +16 more
europepmc   +2 more sources

A Novel Legumain-Like Protease in Macrobrachium nipponense: Identification, Characterization, and Function Analysis in Ovary Maturation

Frontiers in Endocrinology, 2022
Legumain, also called aspartic endopeptidase (AEP), is a member of the cysteine protease family and is involved in various physiological processes. In this study, we analyzed the characteristics of a novel legumain-like (named Mn-Lel) in the female ...
Sufei Jiang, Yiwei Xiong, Wenyi Zhang, Junpeng Zhu, Dan Cheng, Yongsheng Gong, Yan Wu, Hui Qiao, Hui Qiao, Hongtuo Fu, Hongtuo Fu   +10 more
doaj   +1 more source

Comparative proteomic analysis of differentially expressed proteins in the urine of reservoir hosts of leptospirosis. [PDF]

PLoS ONE, 2011
Rattus norvegicus is a natural reservoir host for pathogenic species of Leptospira. Experimentally infected rats remain clinically normal, yet persistently excrete large numbers of leptospires from colonized renal tubules via urine, despite a specific ...
Jarlath E Nally, Avril M Monahan, Ian S Miller, Ruben Bonilla-Santiago, Puneet Souda, Julian P Whitelegge   +5 more
doaj   +1 more source

Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases

Parasites & Vectors, 2008
Background Ticks are vectors for a variety of viral, bacterial and parasitic diseases in human and domestic animals. To survive and reproduce ticks feed on host blood, yet our understanding of the intestinal proteolytic machinery used to derive ...
Mareš Michael, Caffrey Conor R, Hajdušek Ondřej, Horn Martin, Franta Zdeněk, Sojka Daniel, Kopáček Petr   +6 more
doaj   +1 more source

In ovo Feeding of L-Leucine Improves Antioxidative Capacity and Spleen Weight and Changes Amino Acid Concentrations in Broilers After Chronic Thermal Stress

Frontiers in Veterinary Science, 2022
L-Leucine (L-Leu) was demonstrated to confer thermotolerance by in ovo feeding in broiler chicks and chickens in our previous studies. However, the L-Leu-mediated roles in recovering from the detrimental effects of heat stress in broilers are still ...
Guofeng Han, Yangyang Cui, Dan Shen, Mingyang Li, Yu Ren, Takashi Bungo, Vishwajit S. Chowdhury, Yansen Li, Chunmei Li   +8 more
doaj   +1 more source

Phosphorylated acidic serine–aspartate-rich MEPE-associated motif peptide from matrix extracellular phosphoglycoprotein inhibits phosphate regulating gene with homologies to endopeptidases on the X-chromosome enzyme activity [PDF]

Journal of Endocrinology, 2007
Inactivating PHEX (phosphate regulating gene with homologies to endopeptidases on the X chromosome) mutations cause X-linked hypophosphatemia in humans and mice (Hyp) through overproduction of fibroblast growth factor 23 (FGF23) a phosphaturic factor, by osteocytes.
Shiguang, Liu, Peter S N, Rowe, Luke, Vierthaler, Jianping, Zhou, L Darryl, Quarles   +4 more
openaire   +2 more sources

Cathepsin E (EC 3.4.23.34) &#8212; a review

Folia Histochemica et Cytobiologica, 2012
Cathepsin E belongs to the third class of enzymes &#8212; hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that
Anna Worowska, Marek Gacko, Michał Chlabicz, Radosław Łapiński   +3 more
doaj   +1 more source

Presence and expression of hydrogenase specific C-terminal endopeptidases in cyanobacteria [PDF]

, 2003
BACKGROUND: Hydrogenases catalyze the simplest of all chemical reactions: the reduction of protons to molecular hydrogen or vice versa. Cyanobacteria can express an uptake, a bidirectional or both NiFe-hydrogenases.
Batur, Mehtap, Lindblad, Peter, Wünschiers, Röbbe   +2 more
core   +3 more sources

Proteases of haematophagous arthropod vectors are involved in blood-feeding, yolk formation and immunity : a review [PDF]

, 2017
Ticks, triatomines, mosquitoes and sand flies comprise a large number of haematophagous arthropods considered vectors of human infectious diseases. While consuming blood to obtain the nutrients necessary to carry on life functions, these insects can ...
A Ali, A Borges-Veloso, A Estrela, A Fontaine, A Mulenga, A Mulenga, A Mulenga, A Santos, A Schwarz, A Seixas, A Seixas, AA Rascón, AB Estrela, AC Bahia, AC Barnard, AF Rowley, AH Kollien, AL Williamson, AR Khan, AS Raikhel, AV Graça-Souza, BM Christensen, C Balczun, C Barillas-Mury, C Gaboriaud, C Logullo, Carla Nunes de Araújo, CC Hsu, CC Hsu, CE Cruz, CH Kim, CN Araújo de, CV Barillas-Mury, D Boldbaatar, D Borovsky, D Feder, D Feder, D Sojka, D Sojka, D Sojka, D Sojka, D Sojka, D Sojka, D Sojka, D Trevisan-Silva, DE Sonenshine, DP Oldiges, DS Buarque, DS Silva da, E Calvo, E Calvo, E Calvo, E Faudry, E Goulielmaki, EC Borges, EL Telleria, EL Telleria, ES Garcia, FA Lara, FG Noriega, FG Noriega, FG Noriega, FL Watson, Flávia Nader Motta, G Bian, G Dias-Lopes, G Renard, G Renard, G Ribeiro, GM Attardo, GR Garcia, H Mehlhorn, HM Müller, HM Müller, IM Francischetti, IM Francischetti, Izabela M. Dourado Bastos, J Chmelar, J Chmelař, J Isoe, J Kotál, J Leyria, J Mendiola, J Rivera, J Vizioli, Jaime M. Santana, JAT Dow, JG Houseman, JM Anderson, JM Ramalho-Ortigão, JM Ribeiro, JM Ribeiro, JM Ribeiro, JM Ribeiro, JM Ribeiro, JM Ribeiro, JMC Ribeiro, JMC Ribeiro, K Uchida, K Yamaji, KA Edgar, L Cerenius, L Cerenius, L Feitosa, L Gupta, L Liu, L Saboia-Vahia, LA Abreu, Lehane, LM Liu, M Abdul Alim, M Delcroix, M Horn, M Kazimírová, M Lehane, M Motobu, MA Alim, MA Alim, MC Brandon, MH Castro de, MH Sorgine, MJ Gorman, MJ Gorman, N Ruttayaporn, ND Rawlings, ND Rawlings, O Hajdušek, P Bork, P Sriwichai, Paula Beatriz Santiago, PB Santiago, PF Pimenta, PJ Waniek, PM Moolhuijzen, Q Jiang, R Amino, R Graf, R Graf, RB Silveira da, RB Silveira da, RW Almeida de, S Imamura, S Karim, S Tsakas, SA Armitage, Sébastien Charneau, T Hatta, T Lopez-Ordoñez, T Masaki, T Miyoshi, T Miyoshi, T Miyoshi, T Okamoto, T Okamoto, TC Assumpção, TC Assumpção, TC Assumpção, TF Huang, V Urbanová, WL Cho, WL Cho, World Health Organization, X Guo, X Nirmala, X Yu, XL Xu, Y Decrem, Y Dong, Y Schlein, Yanna Reis Praça, Z Franta, Z Franta, Z Shen, Ž Radulović   +173 more
core   +2 more sources