Production and Characterization of a Milk-clotting Protease Produced in Submerged Fermentation by the Thermophilic Fungus Thermomucor indicae-seudaticae N31

Silva, B. L.; Geraldes, F. M.; Murari, Cleidiane Samara; Gomes, Eleni; Silva, Roberto da

doi:10.1007/s12010-013-0655-7

Cited by 25 publications

(18 citation statements)

References 31 publications

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“…Peptidases from thermophilic fungi have been evaluated in relation to their biochemical properties (e.g. thermal stability) and industrial applications, for instance, Thermoascus aurantiacus and its hydrolytic activity on bovine casein [ 10 ], Thermomucor indicae-seudatiacea and Rhizomucor miehei in milk clotting activity [ 11 , 12 ].…”

Section: Introductionmentioning

confidence: 99%

Genome mining for peptidases in heat-tolerant and mesophilic fungi and putative adaptations for thermostability

et al. 2018

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BackgroundPeptidases (EC 3.4) consist of a large group of hydrolytic enzymes that catalyze the hydrolysis of proteins accounting for approximately 65% of the total worldwide enzyme production. Peptidases from thermophilic fungi have adaptations to high temperature that makes them adequate for biotechnological application. In the present study, we profiled the genomes of heat-tolerant fungi and phylogenetically related mesophilic species for genes encoding for peptidases and their putative adaptations for thermostability.ResultsWe generated an extensive catalogue of these enzymes ranging from 241 to 820 peptidase genes in the genomes of 23 fungi. Thermophilic species presented the smallest number of peptidases encoding genes in relation to mesophilic species, and the peptidases families with a greater number of genes were the most affected. We observed differences in peptidases in thermophilic species in comparison to mesophilic counterparts, at (i) the genome level: a great reduction in the number of peptidases encoding genes that harbored a higher number of copies; (ii) in the primary protein structure: shifts in proportion of single or groups of amino acids; and (iii) in the three-dimensional structure: reduction in the number of internal cavities. Similar results were reported for extremely thermophilic proteins, but here we show for the first time that several changes also occurred on the moderate thermophilic enzymes of fungi. In regards to the amino acids composition, peptidases from thermophilic species in relation to the mesophilic ones, contained a larger proportion of Ala, Glu, Gly, Pro, Arg and Val residues and a lower number of Cys, His, Ile, Lys, Met, Asn, Gln, Ser, Thr and Trp residues (P < 0.05). Moreover, we observed an increase in the proportion of hydrophobic and charged amino acids and a decrease in polar amino acids.ConclusionsAlthough thermophilic fungi present less genes encoding for peptidases, these have adaptations that could play a role in thermal resistance from genome to protein structure level.Electronic supplementary materialThe online version of this article (10.1186/s12864-018-4549-5) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Genome mining for peptidases in heat-tolerant and mesophilic fungi and putative adaptations for thermostability

et al. 2018

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“…(), Silva et al . () and Tubesha and Al‐Delaimy () have observed 40, 72 and 96 h as the optimal incubation period for MCE production by Nocardiopsis sp., Thermomucorindicae‐seudaticae and Mucor J20, respectively. On the other hand, P. oxalicum required even longer static incubation of 8 days (Hashem ).…”

Section: Resultsmentioning

confidence: 93%

“…between pH 4.0 and 4.5 for 24 h (Silva et al . ) and from B. subtilis K‐26, it was most stable at pH 7.5 (Rao and Mathur 1979). Some neutral and alkali proteases have also been isolated from Bacillus amyloliquefaciens FSE‐68 which were 100% stable for 60 min at 30C in the alkali range (Cho et al .…”

Section: Resultsmentioning

confidence: 99%

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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“…The values of milkclotting activity and coagulant ratio were significative to P. albidus (73.39 U/ml and 21.60, respectively). Silva et al (2014) reported milk-clotting activity ( 60.5 U/ml) and coagulant ratio (510) in Thermomucor indicae-seudaticae N31. In the study of Alecrim et al (2015), Aspergillus flavo furcatis DPUA 1493 presented milk-clotting activity of 68.61 U/ml and coagulant ratio of 1.81.…”

Section: Resultsmentioning

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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Production and Characterization of a Milk-clotting Protease Produced in Submerged Fermentation by the Thermophilic Fungus Thermomucor indicae-seudaticae N31

Cited by 25 publications

References 31 publications

Genome mining for peptidases in heat-tolerant and mesophilic fungi and putative adaptations for thermostability

Genome mining for peptidases in heat-tolerant and mesophilic fungi and putative adaptations for thermostability

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

Pleurotus albidus: A new source of milk-clotting proteases

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