Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium

Liang, Tzu Wen; Lin, Jane Jean; Yen, Yue Horng; Wang, Chuan Lu; Wang, San-Lang

doi:10.1016/j.enzmictec.2005.04.023

Cited by 39 publications

(16 citation statements)

References 21 publications

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“…The reaction was terminated by adding 5 ml of 0.19 M trichloroacetic acid (TCA). The reaction mixture was centrifuged and the soluble peptide in the supernatant fraction was measured with tyrosine as the reference compound (Liang et al 2006). One unit of protease activity is defined as the activity that releases 1 lmol tyrosine ml À1 in 1 min at 37°C.…”

Section: Enzyme Assaymentioning

confidence: 99%

Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus

Gupta

Joseph

Mani

et al. 2007

World J Microbiol Biotechnol

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In this communication, we report the presence of a newly identified serine alkaline protease producing bacteria, Virgibacillus pantothenticus (MTCC 6729) in the fresh chicken meat samples and the factors affecting biosynthesis as well as characterization of protease. The strain produced only 14.3 U ml À1 protease in the standard medium after 72 h of incubation, while in optimized culture conditions the production of protease was increased up to 18.2 U ml À1 . The strain was able to produce protease at 40°C at pH 9.0. The addition of dextrose and casein improved protease production. The protease was partially purified and characterized in terms of pH and temperature stability, effect of metal ions and inhibitors. The protease was found to be thermostable alkaline by retaining its 100% and 85% stability at pH 10.0 and at 50°C respectively. The protease was compatible with some of the commercial detergents tested, and was effective in removing protein stains from cotton fabrics. The V. pantothenticus, MTCC 6729 protease appears to be potentially useful as an additive in detergents as a stain remover and other bio-formulations.

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Section: Enzyme Assaymentioning

confidence: 99%

Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus

Gupta

Joseph

Mani

et al. 2007

World J Microbiol Biotechnol

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“…When this peptone is added in the medium to cultivate Vibrio species, it yielded high quantities of protease than media containing commercial peptones. B. subtilis, P. aerigunosa, B. cereus, B. licheniformis and V. parahaemolyticus showed enhanced protease activity in the medium supplemented with cuttle fish powder dissolved in fish wastewater [57]. Similarly, an increased level of protease activity by B. cereus was observed when cultured in media containing defatted tuna waste over raw tuna waste [54].…”

Section: Fish Wastes As Substrate For Protease Productionmentioning

confidence: 58%

Fish Waste-Potential Low Cost Substrate for Bacterial Protease Production: A Brief Review

Ramkumar

Sivakumar²,

Victor³

2016

TOBIOTJ

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Industrial biotechnology processes have recently been exploited for an economic utilization of wastes to produce value added products. Of which, fish waste is one of the rich sources of proteins that can be utilized as low cost substrates for microbial enzyme production. Fish heads, tails, fins, viscera and the chitinous materials make up the wastes from fish industries. Processing these wastes for the production of commercial value added products could result in a decrease in the cost of production. In addition, we can eliminate the pollution of the environment and health issues due to the improper disposal of these fish wastes. This review highlights the potential use of fish waste as a cheaper substrate for the production of economically important protease enzyme.

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“…Many previous studies have purified proteinases from the fermentation products of Monascus. 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: 98%

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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Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium

Cited by 39 publications

References 21 publications

Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus

Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus

Fish Waste-Potential Low Cost Substrate for Bacterial Protease Production: A Brief Review

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

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