Statistical Optimization of Milk Clotting Enzyme Biosynthesis by Mucor mucedo Kp736529 and its Further Application in Cheese Production

Ayana, Ibrahim A.A. Abou; Ibrahim, Amal Elsady; Saber, WesamEldin I. A.

doi:10.3923/ijds.2015.61.76

Cited by 14 publications

(16 citation statements)

References 17 publications

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“…In the same way, the MCA of MCE from B. subtilis B1 was improved by 5.57-fold after optimization by response surface methodology [40]. In another study, optimizing the production of MCE enzyme from Mucor mucedo KP736529 by the CCD led to a 6.12-fold increase in MCA compared with initial activity [41]. According to [42], the activity of acid protease from a mixed culture of A. oryzae AS3042 and A. niger SL-09 was increased by five fold using response surface methodology (RSM) optimization.…”

Section: Resultsmentioning

confidence: 97%

Optimization of media composition and growth conditions for production of milk-clotting protease (MCP) from Aspergillus oryzae DRDFS13 under solid-state fermentation

et al. 2020

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This study reports the optimization of milk-clotting protease production from Aspergillus oryzae DRDFS13 under solid-state fermentation (SSF) in both one-variable-at-a-time and response surface methodology (RSM). The production and optimization of milk-clotting protease obtained from Aspergillus oryzae DRDFS13 under solid-state fermentation (SSF) using different agroindustrial wastes as solid substrates were studied. The agro-industrial wastes used included wheat bran, rice bran, pea bran, and grass pea bran. The chemical composition of the best solid substrate was tested using standard methods. Others cultivation parameters were studied, and the results showed that the optimum fermentation medium composed of wheat bran, casein (1% w/w), and glucose (0.5% w/w) and the conditions for maximum milk-clotting protease production were at the moisture content of 55.0%, inoculum of 0.5*10 6 spores/mL, incubation temperature of 30°C, pH of 6.0, and fermentation time of 5 days. The highest milk-clotting activity was obtained from the crude enzyme extracted using 0.1 M NaCl and partial purification of the crude enzyme using chilled acetone, and 80% (NH 4) 2 SO 4 increased the ratio of MCA/PA from 0.56 to 1.30 and 0.65, respectively. Moreover, the highest MCA (137.58 U/mL) was obtained at a casein concentration of 0.5%, pH 4.0, and 25°C, using RSM. Thus, results from the present study showed that the optimization of milk-clotting protease production from A. oryzae DRDFS 13 under SSF by both one-variable-at-a-time and RSM significantly increased the milk-clotting activity. This is the first report from a fungus in the Ethiopian setting and a modest contribution to highlight the potential of harnessing microbial protease enzymes for industrial applications.

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Section: Resultsmentioning

confidence: 97%

Optimization of media composition and growth conditions for production of milk-clotting protease (MCP) from Aspergillus oryzae DRDFS13 under solid-state fermentation

et al. 2020

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“…e fungal enzyme (MCE) showed higher proteolytic activity than calf rennet with the absence of bitter taste defects. e organoleptic scores of E-cheese were also higher than C-cheese [26].…”

Section: Application In Dairy Industrymentioning

confidence: 88%

The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries

Mamo

Assefa

2018

Journal of Food Quality

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Proteases represent one of the three largest groups of industrial enzymes and account for about 60% of the total global enzymes sale. According to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, proteases are classified in enzymes of class 3, the hydrolases, and the subclass 3.4, the peptide hydrolases or peptidase. Proteases are generally grouped into two main classes based on their site of action, that is, exopeptidases and endopeptidases. Protease has also been grouped into four classes based on their catalytic action: aspartic, cysteine, metallo, and serine proteases. However, lately, three new systems have been defined: the threonine-based proteasome system, the glutamate-glutamine system of eqolisin, and the serine-glutamate-aspartate system of sedolisin. Aspartic proteases (EC 3.4.23) are peptidases that display various activities and specificities. It has two aspartic acid residues (Asp32 and Asp215) within their active site which are useful for their catalytic activity. Most of the aspartic proteases display best enzyme activity at low pH (pH 3 to 4) and have isoelectric points in the pH range of 3 to 4.5. They are inhibited by pepstatin. The failure of the plant and animal proteases to meet the present global enzyme demand has directed to an increasing interest in microbial proteases. Microbial proteases are preferred over plant protease because they have most of the characteristics required for their biotechnological applications. Aspartic proteases are found in molds and yeasts but rarely in bacteria. Aspartic protease enzymes from microbial sources are mainly categorized into two groups: (i) the pepsin-like enzymes produced by Aspergillus, Penicillium, Rhizopus, and Neurospora and (ii) the rennin-like enzymes produced by Endothia and Mucor spp., such as Mucor miehei, M. pusillus, and Endothia parasitica. Aspartic proteases of microbial origin have a wide range of application in food and beverage industries. These include as milk-clotting enzyme for cheese manufacturing, degradation of protein turbidity complex in fruit juices and alcoholic liquors, and modifying wheat gluten in bread by proteolysis.

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“…Stability. To investigate the effect of temperature, proteolytic activity was tested at different temperatures (20,25,30,35,40,45,50,55, 60, and 65°C) using hemoglobin as a substrate for 5 min at pH 5.0. ermal stability was examined by incubating the enzyme at 30, 40, 50, 60, and 70°C for 60 min. After 60 min, the remaining enzyme activity was determined at optimum pH and temperature.…”

Section: Determination Of Optimum Temperature and Itsmentioning

confidence: 99%

Production, Optimization, and Characterization of an Acid Protease from a Filamentous Fungus by Solid-State Fermentation

Usman

Mohammed

Mamo

2021

International Journal of Microbiology

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Acid proteases represent an important group of enzymes, extensively used in food and beverage industries. There is an increased demand for acid proteases adapting to the industrial extreme environment, especially lower pH. Thus, this necessitates the search for a better acid protease from fungi that best performs in industrial conditions. The fungal isolates were isolated from grape and dairy farm soil using potato dextrose agar and further screened for protease production based on the hydrolysis of clear zone on skim milk agar. The potential fungi were then subjected to secondary screening under solid-state fermentation (SSF). After the secondary screening, the potential fungus was identified to the genus level by the macroscopic and microscopic methods. The growth conditions and media composition for the potential fungus were further optimized under SSF. The crude enzyme produced by the potential isolate was characterized after partial purification by acetone and ammonium sulfate precipitation. A total of 9 fungal isolates showed protease production in primary and secondary screening; however, one potential isolate (Z1BL1) was selected for further study based on its protease activity. The isolate was identified to the genus Aspergillus based on their morphological features. The maximum acid protease from the isolate Z1BL1 was obtained using fermentation media containing wheat bran as a solid substrate, 1 mL of 3.2 × 106 inoculum size, 50% moisture content, and pH 4.5 upon 120-h incubation at 30°C. The acetone-precipitated enzyme exhibited the maximum activity at 50°C and pH 5 with stability at pH 4–6 and temperature 40–60°C. Thus, the acid protease produced from Aspergillus showed suitable enzyme characteristics required in the industry and could be a candidate for application in the food industry after further purification.

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Statistical Optimization of Milk Clotting Enzyme Biosynthesis by Mucor mucedo Kp736529 and its Further Application in Cheese Production

Cited by 14 publications

References 17 publications

Optimization of media composition and growth conditions for production of milk-clotting protease (MCP) from Aspergillus oryzae DRDFS13 under solid-state fermentation

Optimization of media composition and growth conditions for production of milk-clotting protease (MCP) from Aspergillus oryzae DRDFS13 under solid-state fermentation

The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries

Production, Optimization, and Characterization of an Acid Protease from a Filamentous Fungus by Solid-State Fermentation

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