Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins

Abstract

BACKGROUND The Arctic muskox has economic potential as an alternative meat species and is becoming increasingly popular. The present study aimed to determine the primary structure and pseudoperoxidase activity of muskox myoglobin (Mb) compared to cattle and water buffalo myoglobins. RESULTS The primary structure of muskox Mb was determined via a matrix‐assisted laser desorption ionization‐time of flight mass spectrometry‐based mapping approach using the sheep Mb as a reference sequence. The muskox Mb consists of 153 amino acid residues and shows 100% identity with sheep Mb, whereas 98.69% and 97.38% identity is found with cattle and water buffalo Mbs, respectively. Muskox Mb has an autoxidation rate (MetMb formation) higher than both cattle and water buffalo Mbs at pH 7.2 (37 °C). Moreover, its pseudoperoxidase activity is higher than both cattle and water buffalo Mbs at pH 7.4 (physiological pH), whereas it is slightly lower than cattle Mb and higher than water buffalo at a lower pH (5.8), corresponding to the conditions in meat. CONCLUSION For the first time, the present study reports the purification of myoglobin from muskoxen and, furthermore, a comparative study is conducted on autoxidation and pseudoperoxidase activity with respect to cattle and water buffalo Mbs at both physiological and acid pH. Overall, the results of the current research provide novel information for future studies useful to the meat industry when considering the importance of myoglobin as a principal pigment in meat colour stability. © 2019 Society of Chemical Industry

Structural and functional characterization of the cytotoxic protein ledodin, an atypical ribosome‐inactivating protein from shiitake mushroom (Lentinula edodes)

“…Intact protein spectra were acquired in positive ion linear mode, by using a pulse voltage of 1200 V. A four-point external calibration was applied by using an appropriate mixture (10 pmol/μL) of insulin, cytochrome c, horse b and trypsinogen as standard proteins (Merk Life Science S.r.l. ; Ragucci et al, 2019).…”

Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles

“… 22 , 23 Myoglobin contains 153 amino acids, a heme group where an iron ion is bonded to four nitrogen atoms of the porphyrin ring, a proximal histidine group (His-93), and a distal histidine group (His-64) with a net isoelectric point (IEP) of pH 7. 24 Here, we use hydrophilic silica nanospheres of diameter 30 nm as model NPs. The silica NPs have been widely used as a model to study adsorption and delivery of proteins due to their low toxicity, hydrophilicity induced by surface by the silanol groups (Si–O–H), and well-established synthetic procedures to precisely control their physical and chemical properties.…”

“…Myoglobin is a globular protein found in skeletal and cardiac muscle cells. It acts as a local oxygen reservoir to provide temporary oxygen when blood oxygen delivery is insufficient during periods of intense muscular activity. , Myoglobin contains 153 amino acids, a heme group where an iron ion is bonded to four nitrogen atoms of the porphyrin ring, a proximal histidine group (His-93), and a distal histidine group (His-64) with a net isoelectric point (IEP) of pH 7 . Here, we use hydrophilic silica nanospheres of diameter 30 nm as model NPs.…”

Gene Organization, Expression, and Localization of Ribotoxin-Like Protein Ageritin in Fruiting Body and Mycelium of Agrocybe aegerita

“…Protein elution were obtained using linear gradients of 0.1% TFA (solvent A) and acetonitrile containing 0.1% TFA (solvent B) from 5 to 65% of solvent B over 60 min, monitoring the absorbance at 214 nm [ 34 ]. The relative molecular masses (M r ) of protein were determined by using a MALDI-TOF micro MX spectrometer (Waters, Manchester, UK) in linear mode, as previously reported [ 35 ].…”