Purification and characterisation of two extracellular acid proteinases from Monascus pilosus

Lakshman, P.L.N.; Toyokawa, Yoichi; Toyama, Hirohide; Taira, Toki; Yasuda, Masaaki

doi:10.1016/j.foodchem.2010.02.007

Cited by 16 publications

(24 citation statements)

References 29 publications

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“…The observed half-life for the protease was approximately 120 minutes at 50°C. The thermostability of acidic proteases highly varied within the Rhizopus oryzae (30-45°C) [11], Aspergillus oryzae MTCC 5341 (40-57°C) [30], A. niger I1 (30-40°C) [3], and Mucor pilosus (25-55°C) [31] species. Rhizopuspepsin from R. oryzae MTCC 3690 had a half-life of ~20 minutes at 60°C, and retained full activity after Fig.…”

Section: Results and Disscusionmentioning

confidence: 99%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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Abstract:The present study characterises an acidic protease purified from the Rhizopus stolonifer strain, RN-11. The acidic protease with a 70 kDa molecular weight, was stable within pH 2-4 at temperatures 40-50℃. The temperature and pH value conducive to optimal catalytic activity were pH 2.5 and 50℃, respectively. Treatment with 5 mmol metal ions showed that the acidic protease was activated by Na . It was proposed that the studied acidic protease might represent a previously uncharacterised type of acidic protease produced by the Rhizopus stolonifer RN-11 strain.

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Section: Results and Disscusionmentioning

confidence: 99%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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“…2A). This could be due to the presence of proteinases produced during fermentation by MJ-1, which hydrolyzed muscle proteins to yield alkaline components, such as peptides and amines (26). Additionally, pH values of the fermented products can increase along with the Monascus pigments secreted (21,27).…”

Section: Resultsmentioning

confidence: 99%

“…For example, Liang et al (34) found that the Monascus purpureus CCRC31499 (a safe and widely used microorganism in traditional food) could produce a protease when it was grown in a medium containing shrimp and crab shell powder from marine wastes. Subsequently, Lakshman et al (35) purified and characterized two extracellular acid proteinases (MpiAP1 and MpiAP2) from Monascus pilosus.…”

Section: )mentioning

confidence: 99%

Effect of Monascus as a nitrite substitute on color, lipid oxidation, and proteolysis of fermented meat mince

Xiang

Zhang

2015

Food Sci Biotechnol

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Monascus spp. are fungi, traditionally eaten in Asian countries, that have the the potential to be used as a nitrite substitute in meat-product processing. Effects of using Monascus ruber MJ-1 as a nitrite substitute on color, lipid oxidation and proteolysis of fermented meat mince were investigated in this study. After 4 days of fermentation, a* and L* values for the samples were significantly higher and lower than the values for the control, respectively; however, b* values were significantly lower than that of the control throughout the fermentation process (p<0.05). Furthermore, Monascus ruber MJ-1 fermentation decreased the thiobarbituric acid reactive substances (TBARs) value and increased the myofibril fragmentation index (MFI) value of meat mince significantly (p<0.05). SDS-PAGE results further indicated that myofibrillar proteins were degraded during fermentation, while sarcoplasmic proteins were not. These results suggest prospects for the broad application of Monascus as a nitrite substitute in meat processing.

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“…No. 3403 (M. purpureus) (Yasuda et al, 1984b) and M. pilosus (Lakshman et al, 2010) as homogenous preparations using SDS-polyacrylamide gel electrophoresis. The molecular mass of the enzyme from M. purpureus was estimated to be 40 kDa by gel-filtration and 43 kDa by sedimentation method; therefore, it was determined to be a monomeric structure.…”

Section: Characterization and Application Of Aspartic Proteinases Fromentioning

confidence: 99%