Purification and Characterization of a Chymosin from Rhizopus microsporus var. rhizopodiformis

Sun, Qian; Wang, Xiping; Yan, Qiaojuan; Chen, Wei; Jiang, Zhengqiang

doi:10.1007/s12010-014-1044-6

Cited by 22 publications

(16 citation statements)

References 42 publications

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“…However, at 50–60C, they retained only 10–20% of its activity after 30 min (Rao and Mathur 1979; Sun et al . ). No changes were observed in the protease activity of Rhizomucor miehei between 55 and 62C, where it retained ∼80% activity.…”

Section: Resultsmentioning

confidence: 97%

Optimization of Upstream Process Parameters for Enhanced Production of Thermostable Milk Clotting Enzyme from Bacillus Subtilis MTCC 10422

Narwal

Bhushan

Pal

et al. 2016

J Food Process Engineering

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The process protocol of high titer milk clotting enzyme (MCE) production from Bacillus subtilis was delineated through optimizing different energy sources and growth conditions like incubation period, temperature and pH. The culture broth showed maximum production of MCE at pH 6.0 and temperature 40C after 48 h of incubation with the yield of 191.55 U/mL. Quantitative comparison of MCE activity before and after optimization revealed 7.46-fold increase in MCE production after the process conditions were standardized. The characteristics of MCE viz. broad pH and temperature stability could make it useful as a new source of milk coagulant in dairy processing. PRACTICAL APPLICATIONSEach microbial strain is unique in its molecular, biochemical and metabolic enzyme production properties. These production characteristics would have to offer competitive advantages over the existing products of un-optimized medium. This warrants thorough study of isolated microbial species under variable growth conditions. Fungal MCEs have been widely reported. The Milk Clotting Activity (MCA) and MCA per Proteolytic Activity (PA) index of the bacterium under study are comparable to that of many fungal reports and better than quite a few bacterial MCEs. Bacillus subtilis can be a promising microorganism for MCE production and has a good probability of successful use in cheese production.

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Section: Resultsmentioning

confidence: 97%

Optimization of Upstream Process Parameters for Enhanced Production of Thermostable Milk Clotting Enzyme from Bacillus Subtilis MTCC 10422

Narwal

Bhushan

Pal

et al. 2016

J Food Process Engineering

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“…1E), and it decreased at higher speeds due to increased mechanical shear force that was not conducive to cell growth (Hashem, 2000;Narwal et al, 2017). Proper agitation of culture would facilitate MCA by letting in more air, therefore oxygen, but some other studies presented otherwise different results, that still culture would yield a higher MCA (Hashem, 2000;Narwal et al, 2017;Sun et al, 2014), which was possible due to the differences in the nature of strains. He et al (2012) indicated that the initial pH of growth medium strongly affected enzyme reaction and transport of various components across the cell membrane, thus the MCA of B. methanolicus LB-1.…”

Section: Resultsmentioning

confidence: 97%

Production, purification and characterization of a milk clotting enzyme from Bacillus methanolicus LB-1

Zheng

Zhao

et al. 2019

Food Sci Biotechnol

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Bacillus methanolicus LB-1 isolated from traditional rice wine was found to produce a milk clotting enzyme (MCE), and its fermentation conditions were optimized using response surface methodology. Then the MCE was produced by ethanol precipitation, and further chromatography separation resulted in a 10.46-fold purification with a 59.28% recovery. The MCA (milk clotting activity) of the purified MCE reached 597,310 ± 0.13 SU/ g. The optimal temperature of the MCE was determined to be 50°C and it was stable in the low temperature range of 40-45°C. The MCE had an optimum pH of 6.5, and it was stable under neutral conditions. Calcium chloride at the concentration of 25 mM was found to be the most effective stimulus. The MCE was identified by LC-MS to be a putative protein (ID I3EB99) containing 759 amino acids with a molecular weight of 80.37 kDa and a pI of 9.23.

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“…Milk-clotting enzymes from other fungi as Rhizopus oryzae (Kumar et al, 2005), Penicillium oxalicum (Hashem, 1999) and Rhizopus microsporus var. rhizopodiformis (Sun et al, 2014) also presented optimum activity at 60°C. According to Dybowska and Fujio (1996) at high values of temperature, the process of coagulation is decreased.…”

Section: Al (2015)mentioning

confidence: 94%

“…Sun et al (2014) showed that Zn 2+ ions raised the milk-clotting enzyme activity from R. microsporus var. rhizopodiformis.…”

Section: Al (2015)mentioning

confidence: 99%

Pleurotus albidus: A new source of milk-clotting proteases

Martim¹,

Silva²,

Souza³

et al. 2017

Afr. J. Microbiol. Res.

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Researches have been done to discover new sources of microbial proteases with milk-clotting activity to replace the traditional rennet from calves. The aim of this study was to select a species of edible mushroom as milk-clotting enzymes producer using the submerged fermentation technology. From the six species evaluated, Pleurotus albidus was the one that expressed the highest value of coagulant ratio (21.60). The milk-clotting enzymes showed maximum activity at 60°C and pH 6.0. Iodoacetic acid presented the highest inhibition in proteolytic activity suggesting the presence of cysteine proteases in the crude extract from P. albidus. The enzymes did not present toxic action against human fibroblasts (MRC5) in the analyzed conditions and, for that reason, can be suitable to applications in food industry. This is the first report of milk-clotting enzymes production by the edible mushroom P. albidus

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Purification and Characterization of a Chymosin from Rhizopus microsporus var. rhizopodiformis

Cited by 22 publications

References 42 publications

Optimization of Upstream Process Parameters for Enhanced Production of Thermostable Milk Clotting Enzyme from Bacillus Subtilis MTCC 10422

Optimization of Upstream Process Parameters for Enhanced Production of Thermostable Milk Clotting Enzyme from Bacillus Subtilis MTCC 10422

Production, purification and characterization of a milk clotting enzyme from Bacillus methanolicus LB-1

Pleurotus albidus: A new source of milk-clotting proteases

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