Results 61 to 70 of about 36,613 (150)

Enhancing Consumer Acceptance of Cricket (Acheta domesticus) Protein Hydrolysate Through ProteAX‐Mediated Enzymatic Hydrolysis to Improve Techno‐Functional and Organoleptic Properties

Food Science &Nutrition, Volume 14, Issue 6, June 2026.
ProteAX‐assisted hydrolysis of cricket (Acheta domesticus) protein enhanced its techno‐functional and sensory properties. Optimal hydrolysis at a 1.5% enzyme concentration for 5 h produced a hydrolysate with a 67.71% degree of hydrolysis, 69.51% protein content, high solubility, improved water and oil absorption capacities, low bitterness, and a strong
Fetriyuna Fetriyuna, Rozanah Nushrotina, Ade Chandra Iwansyah, Nandi Sukri, Ratna Chrismiari Purwestri   +4 more
wiley   +1 more source

Glutamyl endopeptidase of Bacillus intermedius, strain 3-19

, 2020
A homogeneous glutamyl endopeptidase splitting peptide bonds of glutamic, rarely of aspartic acid residues in peptides and proteins, was isolated from Bacillus intermedius 3-19 culture filtrate using chromatography on CM cellulose and Mono S.
Leshchinskaya I., Balaban N., Viryasov M., Shakirov E., Itskovitch E., Stepanov V., Mardanova A., Sharipova M., Rudenskaya G.   +8 more
core  

Identifying the histone H3 endopeptidase.

, 2014
(a) Schematic of histone H3 endopeptidase enrichment. Whole cell extract from early stationary phase cells was used to purify the histone H3 endopeptidase.
Yong Xue (307664), Ajay A. Vashisht (128117), Trent Su (198030), Yuliang Tan (233304), James A. Wohlschlegel (212752)   +4 more
core   +1 more source

Neutral Endopeptidase Expression and Distribution in Human Skin and Wounds [PDF]

, 1999
Cutaneous sensory nerves mediate inflammation and wound healing by the release of neuropeptides such as substance P. Neutral endopeptidase is a cell surface enzyme that degrades substance P and thereby terminates its biologic actions. The distribution of
Haycox, Claire L., Song, In-Sung, Ansel, John C., Olerud, John E., Usui, Marcia L., Seckin, Deniz, Chiu, Diane S., Bunnett, Nigel W.   +7 more
core   +1 more source

Leucyl endopeptidase

, 2004
Leucyl endopeptidase (EC 3.4.21.57) is a serine proteinase displaying leucine-specific proteolytic activity isolated from spinach leaves. The history, biochemical characterization, biological aspects and relationships of leucyl endopeptidase with ...
ADUCCI, PATRIZIA, Ascenzi, P.
core   +1 more source

Leucyl endopeptidase

, 2013
In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1].
ADUCCI, PATRIZIA, Aducci, P, Paolo Ascenzi, Ascenzi, P, Ascenzi, P., Patrizia Aducci   +5 more
core   +1 more source

Crystal structure of glycyl endopeptidase from Carica papaya: A cysteine endopeptidase of unusual substrate specificity

, 1995
Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors ...
Hemmings, Andrew M., Buttle, David J., O'Hara, Bernard P., Pearl, Laurence H.   +3 more
core   +1 more source

Abstracts

Molecular Oncology, Volume 20, Issue S1, Page 1-692, August 2026.
Abstracts submitted to the ‘EACR 2026 Congress: Innovative Cancer Science’, from 08–11 June 2026 and accepted by the Congress Organising Committee are published in this Supplement of Molecular Oncology, an affiliated journal of the European Association for Cancer Research (EACR).
wiley   +1 more source

Hydrogels Based on Poly(aspartic acid): Synthesis and Applications

, 2019
This review presents an overview on the recent progress in the synthesis, crosslinking, interpenetrating networks, and applications of poly(aspartic acid) (PASP)-based hydrogels.
Adelnia, Hossein, Little, Peter J, Blakey, Idriss, Ta, Hang T   +3 more
core   +1 more source

Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain

, 2006
Asparaginyl endopeptidase (AEP), also known as legumain, is a cysteine protease that has been ascribed roles in antigen presentation yet its exact role in human biology remains poorly understood.
Sexton, Kelly B., Kelly B. Sexton, Witte, Martin D., Blum, Galia, Galia Blum, Bogyo, Matthew, Martin D. Witte, Matthew Bogyo, Witte, Martin D.; id_orcid   +8 more
core   +1 more source