Production and Some Properties of Rennin-like Milk-clotting Enzyme from Penicillium citrinum

Abdelfattah, Ahmed; Mabrouk, S. S.; El-Hawwary, Nadia M.

doi:10.1099/00221287-70-1-151

Cited by 32 publications

(5 citation statements)

References 7 publications

(2 reference statements)

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“…Enhancement in presence of Mg 2+ and Fe 2+ has been reported for Amylomyces rouxii (Yu and Chou 2005). Skim milk powder and CaCl 2 , a metal ion essential for milk clotting, exhibited a synergistic effect in enhancing the production of MCP from A. niger (Channe and Shewale 1998) while having no effect from Penicillium citrinum (Abdel‐Fattah et al. 1972).…”

Section: Discussionmentioning

confidence: 99%

Role of casein on induction and enhancement of production of a bacterial milk clotting protease from an indigenously isolated Bacillus subtilis

Dutt

Meghwanshi

Gupta

et al. 2008

Lett Appl Microbiol

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Aims: To isolate and enhance the yield of a bacterial milk clotting protease (MCP) through process optimization and scale up. Materials and Results: Bacillus subtilis was isolated as MCP producer with good milk clotting activity (MCA) per proteolytic activity (PA) index. The enzyme production was inducible with casein and enhanced with fructose and ammonium nitrate resulting in 571·43 U ml−1 of enzyme. Conclusions: Medium containing 4% fructose, 0·75% casein, 0·3% NH4NO3 and 10 mmol l–1 CaCl2, pH 6·0, inoculated with 4% (v/v) inoculum, incubated at 37°C, 200 rev min−1 for 72 h gave maximum production. A 6·67‐fold increase in MCP yield with very high MCA per PA index was observed after final optimization indicating similarity to rennets. Significance and Impact of the Study: Mostly fungal MCPs have been reported. The MCA and MCA per PA index of this bacterium is comparable to that of many fungal reports and better than quite a few bacterial MCPs. Thus, this enzyme by B. subtilis has good probability of successful use in cheese production.

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Section: Discussionmentioning

confidence: 99%

Role of casein on induction and enhancement of production of a bacterial milk clotting protease from an indigenously isolated Bacillus subtilis

Dutt

Meghwanshi

Gupta

et al. 2008

Lett Appl Microbiol

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“…However, the ratio of milk-clotting activity to proteolysis activity at a wheat bran juice concentration of 18 g/100 mL was significantly higher than that at a wheat bran juice concentration of 16 g/100 mL. The ratio of milk-clotting activity to proteolysis activity is an important index for judging the suitability of an enzyme preparation for use as a rennet substitute (Abdel-Fattah et al 1972). So, a concentration of wheat bran juice of 18 g/100 mL was selected for production of the milk-clotting enzyme.…”

Section: Resultsmentioning

confidence: 99%

Screening fermentation parameters of the milk-clotting enzyme produced by newly isolated Bacillus amyloliquefaciens D4 from the Tibetan Plateau in China

Zhang

Ren

et al. 2011

Ann Microbiol

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A bacterium producing an extracellular milkclotting enzyme was isolated from yak grazing soil in the Tianzhu Tibetan autonomous county on the Tibetan Plateau and identified as Bacillus amyloliquefaciens. We used single-factor testing to study the optimum physical conditions and nutritional parameters for production of the milk-clotting enzyme, while the temperature and pH stability of the enzyme were also studied. The optimum conditions for production of the milk-clotting enzyme were: temperature, 37°C; inoculum size, 4% (1.8×10 7 CFU/mL); agitation speed, 170 rpm; and initial pH of the medium, 6.2. The maximum milk-clotting activity and milk-clotting activity per proteolysis activity were found using wheat bran juice at a concentration 18 g/100 mL, 4% (w/v) sucrose and 2% (w/v) skim milk powder. These optimized conditions resulted in a 2.68-fold increase in production of the milk-clotting enzyme. The crude enzyme exhibited good temperature and pH stability; 80% of the milk-clotting activity was retained after incubation at 40°C for 30 min and more than 70% of the activity was retained between pH 5.5 and 7.5. This B. amyloliquefaciens milk-clotting enzyme has potential as a calf rennet substitute.

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“…In any case, such retardation of milk-clotting by seed extract may be attributed to several factors. There is an insufficient amount of substrate (casein molecules) due to dilution which restricts the ability of the enzyme to act at its full capacity [ 54 ]. The increased viscosity of the solution at higher concentrations of milk diminishes the enzyme activity or it may be due to the smaller amount of hydrolyzed κ-casein when coagulation is initiated; both facts have been stated by Dalgleish [ 55 ] and Low et al [ 56 ].…”

Section: Resultsmentioning

confidence: 99%

Utility of Milk Coagulant Enzyme of Moringa oleifera Seed in Cheese Production from Soy and Skim Milks

Sánchez-Muñoz

Valdez-Solana

Avitia-Domínguez

et al. 2017

Foods

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In this study, the potential use of Moringa oleifera as a clotting agent of different types of milk (whole, skim, and soy milk) was investigated. M. oleifera seed extract showed high milk-clotting activity followed by flower extract. Specific clotting activity of seed extract was 200 times higher than that of flower extract. Seed extract is composed by four main protein bands (43.6, 32.2, 19.4, and 16.3 kDa). Caseinolytic activity assessed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and tyrosine quantification, showed a high extent of casein degradation using M. oleifera seed extract. Milk soy cheese was soft and creamy, while skim milk cheese was hard and crumbly. According to these results, it is concluded that seed extract of M. oleifera generates suitable milk clotting activity for cheesemaking. To our knowledge, this study is the first to report comparative data of M. oleifera milk clotting activity between different types of soy milk.

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Production and Some Properties of Rennin-like Milk-clotting Enzyme from Penicillium citrinum

Cited by 32 publications

References 7 publications

Role of casein on induction and enhancement of production of a bacterial milk clotting protease from an indigenously isolated Bacillus subtilis

Role of casein on induction and enhancement of production of a bacterial milk clotting protease from an indigenously isolated Bacillus subtilis

Screening fermentation parameters of the milk-clotting enzyme produced by newly isolated Bacillus amyloliquefaciens D4 from the Tibetan Plateau in China

Utility of Milk Coagulant Enzyme of Moringa oleifera Seed in Cheese Production from Soy and Skim Milks

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