Further characterization and kinetic parameter determination of a milk-clotting protease fromMucor bacilliformis

Venera, Graciela Delia; Machalinski, C.; Zumarraga, H.; Biscoglio, Mirtha J.; Bonino, De Jimenez

doi:10.1007/bf02785991

Cited by 18 publications

(12 citation statements)

References 9 publications

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“…7). Similar results have been reported for milk-clotting enzyme from Mucor miehe [44] and Mucor baciliformis [45]. Lin et al [41] also found the same result on a milkclotting agent from lao-chao with Rhizopus oryzae.…”

Section: Ph Optima and Ph Stabilitysupporting

confidence: 89%

Purification and partial characterization of milk-clotting enzyme extracted from glutinous rice wine mash liquor

Wang

Cheng

Ahmed

et al. 2009

Korean J. Chem. Eng.

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Glutinous rice wine mash liquor is a traditional food of south of China and its ability to coagulate the milk has been proved. The aim of this work was to extract milk-clotting enzyme from glutinous rice wine mash liquor. A partial purified extract of enzyme was obtained by fractional precipitation with (NH 4 ) 2 SO 4 . The fractions obtained by precipitation, 40-90% possessed the milk-clotting activity (MCA) (145.72 U/mg). The 40-90% (NH 4 ) 2 SO 4 fraction was further purified by sephadex G-100 and DEAE-sephadex A-50 with MCA (4,360±50 U/mg), which was confirmed by SDS-PAGE that showed only one band with a molecular mass of 36.0 kDa. Highest MCA was attained at 36 o C. The enzyme was completely inactivated by heating for 20 min at 60 o C. The MCA increased with the decreasing of milk pH from 8.0 to 5.5, and it was active at the wide range of pH 1 to 7. The metal ions Mg 2+ , Ca 2+ , Ba 2+ , Mn 2+ , Al 3+ , Fe 2+ had a very clear function to accelerate milk coagulation whereas Na + and K + decelerated the activity slightly. The curd effect of the milk-clotting enzyme has primarily been studied.

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Section: Ph Optima and Ph Stabilitysupporting

confidence: 89%

Purification and partial characterization of milk-clotting enzyme extracted from glutinous rice wine mash liquor

Wang

Cheng

Ahmed

et al. 2009

Korean J. Chem. Eng.

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“…5). The result is in accordance with Venera et al (1997), who observed an optimum pH of 5.5 for MCA from Mucor baciliformis. Hashem (2000) also observed that an increase in the pH of the reaction mixture was associated with a gradual loss of MCA, but at pH 7, 86.79% of the enzyme activity of Penicillium oxalicum was lost and it exhibited a maximum activity at pH 4.…”

Section: Effect Of Ph On Milk Clotting Activity and Stabilitysupporting

confidence: 80%

“…Among those bacterial and fungal rennin substitutes, those from Mucor miehei (Seker et al, 1998), Penicillium oxalicum (Hashem, 2000), Myxococcus xanthus (Petit and Guespin, 1992), Bacillus mesentericus (Stoeva and Mesrob, 1977), Nocardiopsis sp. (Cavalcanti et al, 2004), and Mucor baciliformis (Venera et al, 1997) are the most widely known.…”

Section: Introductionmentioning

confidence: 99%

Fermentation parameter and partial biochemical characterisation of milk clotting enzyme from Chinese distiller’s yeast

Chen

2008

Ann. Microbiol.

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A strain F34 producing milk clotting enzyme with high yield was obtained from Chinese distiller's yeast, using casein plate prescreening and fermentation reselection. The optimum fermentation medium for milk clotting enzyme production was as follows: 5.0% rice flour and bran digest, 5.0% bean flour digest, 0.5% CaCl 2 , 0.5% KCl, initial pH 4.5. The optimal fermentation parameters was at 34 °C for 60 h. The enzyme action was optimal at 50 °C and at about pH 5.5. In the absence of substrate the enzyme showed good stability at 40 °C and pH 3.5. Ca 2+ , Zn 2+ , Fe 3+ and Fe 2+ showed stimulation on the milk clotting activity; K + and Mg 2+ showed weak stimulation; Na + , Cu 2+ , Co 2+ and Li 2+ showed inhibition. The results indicate that this milk clotting enzyme may partially substitute calf rennet in the cheese manufacture.

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“…Figure 3 shows the predicted 3D ribbontype computational representation models for M. circinelloides and M. bacilliformis (online homology modeling with Geno3D was used to create structural models). Venera et al (1997) performed a detailed biochemical and kinetic study on the milk-clotting proteinase from M. bacilliformis. An extinction coefficient, ε 278 cm = 1.61 ml mg −1 cm −1 , a molecular mass of 35.4 kDa, and pI of 5.2 were determined for the protein under study.…”

Section: Recovery and Purification Of Mucor Spp Aspartic Proteinasesmentioning

confidence: 99%

“…and (b) rennin-like enzymes produced by Mucor spp. (Fraile et al 1981;Venera et al 1997;Fernandez-Lahore et al 1999;Neelakantan et al 1999;Andrade et al 2002;Machalinski et al 2006), Rhizomucor spp. (Thakur et al 1990;Escobar and Barnett 1993;Silveira et al 2005;De Lima et al 2008), and Endothia parasitica (Sardinas 1968).…”

mentioning

confidence: 99%

Aspartic proteinases from Mucor spp. in cheese manufacturing

Yeğin

Fernández‐Lahore

Salgado

et al. 2010

Appl Microbiol Biotechnol

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Filamentous fungi belonging to the order of Mucorales are well known as producers of aspartic proteinases depicting milk-clotting activity. The biosynthesis level, the biochemical characteristics, and the technological properties of the resulting proteinases are affected by the producer strain and the mode of cultivation. While the milk-clotting enzymes produced by the Rhizomucor spp. have been extensively studied in the past, much less is known on the properties and potential applications of the aspartic proteinases obtained for Mucor spp. Indeed, several Mucor spp. strains have been reported as a potential source of milk-clotting enzymes having unique technological properties. Both submerged fermentation and solid substrate cultivation are proven alternatives for the production of Mucor spp. aspartic proteinases. This review provides an overview on the bioprocessing routes to obtain large amounts of these enzymes, on their structural characteristics as related to their functional properties, and on their industrial applications with focus on cheese manufacturing.

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Further characterization and kinetic parameter determination of a milk-clotting protease fromMucor bacilliformis

Cited by 18 publications

References 9 publications

Purification and partial characterization of milk-clotting enzyme extracted from glutinous rice wine mash liquor

Purification and partial characterization of milk-clotting enzyme extracted from glutinous rice wine mash liquor

Fermentation parameter and partial biochemical characterisation of milk clotting enzyme from Chinese distiller’s yeast

Aspartic proteinases from Mucor spp. in cheese manufacturing

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