Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family

Machalinski, C.; Pirpignani, María L.; Mariño, Cristina Giménez; Mantegazza, Adriana R.; Bonino, Mirtha Biscoglio de Jiménez

doi:10.1016/j.jbiotec.2005.12.035

Cited by 20 publications

(19 citation statements)

References 27 publications

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“…In the case of T. clypeatus milk clotting metalloprotease (AcP s ), its moderate thermostability could facilitate the reduction of other microbial contamination during cheese making. The optimum temperature is similar to that of the fungal protease from Mucor bacilliformis (45°C) (Machalinski, Pirpignani, Marino, Mantegazza, & de Bonino, 2006). The purified AcP had sequence homology with the predicted protein of P. trichocarpa (Supplementary Tables 1a and 1b).…”

Section: Discussionmentioning

confidence: 74%

“…(Preetha & Boopathy, 1994) and Mucor sp. (Arima, Yu, Iwasaki, & Tamura, 1968;Arima et al, 1970;Machalinski, Pirpignani, Marino, Mantegazza, & de Bonino, 2006;Merheb-Dini et al, 2010;Yegin, Fernandez-Lahore, Guvenc, & Goksungur, 2010) have been studied in the past, much less is known on the applications of the proteinase obtained from Termitomyces sp. Therefore the aim of the present study was to purify and characterise the metalloprotease produced by the fungus in submerged fermentation and elucidate its milk-clotting potency.…”

Section: Discussionmentioning

confidence: 99%

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Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091

2015

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Section: Discussionmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091

2015

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“…Pro23 and hydrophobic residues, e.g., Val18 and Val20, are also well conserved when comparing primary sequences between proteinases. Machalinski et al (2006) reported the structural aspects of aspartic proteinases obtained from a mesophilic M. bacilliformis strain. The molecular weight of the proteinase was close to 32 kDa.…”

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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“…The worldwide increase in cheese consumption and the reduction in natural rennet supply has induced to look for new alternative sources of milk coagulants such as those obtained from microbial fermentation or genetically modified microorganisms. Some specific genera such as Mucor baciliformis and Rhizomucor miehei can produce, by fermentation, chymosin-like enzymes with similar milk-clotting properties (Chitpinityol and Crabbe, 1998;Machalinski et al 2006). On the other hand, genetically modified organisms (e.g., Aspergillus nigger, Kluyveromyces lactis and E. coli carrying the calf chymosin gene) have been used to obtain recombinant chymosin (Barbano and Rasmussen, 1992; Kappeler et al 2006; Mazorra-Manzano et al 2013a).…”

Section: Introductionmentioning

confidence: 99%

EXPLORING THE MILK-CLOTTING PROPERTIES OF EXTRACTS FROM Bromelia pinguin FRUIT

Moreno-Hernández¹,

Pérez²,

Osuna-Ruíz³

et al. 2017

J microb biotech food sci

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Plants represent an attractive source of milk-clotting proteases with potential use for chymosin substitution in cheesemaking process. A crude enzymatic extract from B. pinguin fruit showed capacity to clot milk efficiently in a short time. It showed a maximum milk-clotting activity around 4 U/mL in the range of 70-80 ºC. This value indicated that one mL of the extract was capable to clot around 400 mL of milk in 40 min at the specified condition. B. pinguin extract presented only 25% of its maximum activity under standard temperature (30-35 ºC) for cheese-making. Proteases inhibitors indicated that cysteine and serine proteases were present in the extract and could be responsible for the milk-clotting activity found. SDS-PAGE analysis of casein hydrolysis indicated that proteases in B. pinguin extract were more proteolytic than chymosin. The high presence of milk-clotting proteases in B. pinguin fruit offers an alternative new source of proteases for biotechnological processes.

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Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family

Cited by 20 publications

References 27 publications

Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091

Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091

Aspartic proteinases from Mucor spp. in cheese manufacturing

EXPLORING THE MILK-CLOTTING PROPERTIES OF EXTRACTS FROM Bromelia pinguin FRUIT

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