Acid protease recovery from a solid-state fermentation system

Fernández-Lahore, Hector Marcelo; Fraile, Elda R.; Cascone, Osvaldo

doi:10.1016/s0168-1656(98)00048-0

Cited by 52 publications

(50 citation statements)

References 22 publications

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“…In any case, unit operations based on chromatography and adsorption may be required in order to produce an adequate separation between the product and other "contaminants," which are not necessarily proteins. Fernandez-Lahore et al (1998) recovered the milk-clotting enzyme from M. bacilliformis from SSF crude extracts with 46% yield by employing ethanol (or acetone) precipitation at optimized pH values (e.g., ranging from 4.0 to 5.0). Areces et al (1992) further purified such aspartic proteinase by employing ion exchange chromatography.…”

Section: Recovery and Purification Of Mucor Spp Aspartic Proteinasesmentioning

confidence: 99%

“…strains (Belyauskaite et al 1980;Fraile et al 1981;Handel and Fraile 1984;Fernandez-Lahore et al 1998;Andrade et al 2002). Fraile et al (1978) performed a pioneering study on the ability of Mucor spp.…”

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confidence: 99%

“…An additional advantage is the facilitated recovery of the products, e.g., an enzyme can be leached out in a concentrated solution. Moreover, SSF helps to prevent phenomena that adversely influence the biosynthesis of aspartic proteinase as in the cases of catabolite repression by glucose or the case of biosynthesis inhibition by amino acids and ammonia (Fernandez-Lahore et al 1998). Several types of aspartic proteinases have been successfully produced by this technique (Preetha and Boopathy 1994;Pandey et al 2000;.…”

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confidence: 99%

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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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Section: Recovery and Purification Of Mucor Spp Aspartic Proteinasesmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Aspartic proteinases from Mucor spp. in cheese manufacturing

Yeğin

Fernández‐Lahore

Salgado

et al. 2010

Appl Microbiol Biotechnol

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“…Moreover, protein -protein association may lead to unexpected protein chromatographic behaviour or to multilayer formation [4,5]. The nature of the feedstock can also have an influence on protein separation due to its interaction with low molecular weight components and polymers in the mixture [6]. Some additional structural characteristics of the macromolecules to be separated, as is the case for the glycosylation type, also have the potential to impact chromatographic behaviour [7].…”

Section: Introductionmentioning

confidence: 99%

Tailoring orthogonal proteomic routines to understand protein separation during ion exchange chromatography

Cabrera¹,

Zhelyazkova²,

Galvis³

et al. 2008

J of Separation Science

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Original PaperTailoring orthogonal proteomic routines to understand protein separation during ion exchange chromatography Surface charge, molecular weight, and folding state are known to influence protein chromatographic behaviour onto ion exchangers. Experimentally, information related to such factors can be gathered via 2-DE methods. The application of 2-D PAGE under denaturing/reducing conditions was already shown to reveal separation trends within a large protein population from cell extracts. However, ion-exchange chromatography normally runs under native conditions. A tailored protocol consisting in a first separation based on IEF on Immobiline TM strips under native conditions followed by a second dimension SDS-PAGE run was adopted. The chromatographic versus electrophoretic separation behaviours of two model proteins, thaumatin (TAU) and BSA, were compared to better understand which proteomic routine would be better suited to anticipate IEX chromatographic separations. It was observed that the information contained in the pI value obtained with the adapted 2-DE protocol showed better correlation with the IEX chromatographic behaviour. On the other hand, chromatographic separations performed in the presence of urea as a denaturant have demonstrated the potential influence of hydrodynamic radius/ conformation on protein separation. Moreover, the information provided by such 2-D system correlated well with the chromatographic behaviour of an additional set of pure proteins. An initial prediction of protein ion-exchange chromatographic behaviour could be possible utilizing an experimental approach based on 2-DE running under milder chemical conditions. This technique provides information that more closely resembles the separation behaviour observed with a complex biotechnological feedstock.

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“…Distilled or tap water alone or with glycerin or sodium chloride was found to be best for amyloglucosidase extraction from moldywheat bran [9], whereas alcoholic solvents were found to be less effi cient than aqueous solvents. Fernandez-Lahore et al [20] found that 0.5 M sodium chloride was more suitable for acid protease recovery than distilled water. For this reason, subsequent experiments were carried out with only water for further optimization.…”

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confidence: 99%

Optimization of extraction of β-endoglucanase from the fermented bran of Aspergillus niger

2010

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A local isolate of Aspergillus niger was cultivated under optimal growth conditions on wheat bran in solid state fermentation. β-endoglucanase from fermented bran was separately extracted with different solvents to test recovery of enzyme. Among solvents tested, distilled water served the best leachate. Conditions were further optimized with this leachate. Two washes of fermented bran with the leachate for 30 min each under shaking conditions in a ratio of 1 g of wheat bran : 4 ml of distilled water together yielded maximum recovery of 16.7 U/g of wheat bran.

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Acid protease recovery from a solid-state fermentation system

Cited by 52 publications

References 22 publications

Aspartic proteinases from Mucor spp. in cheese manufacturing

Aspartic proteinases from Mucor spp. in cheese manufacturing

Tailoring orthogonal proteomic routines to understand protein separation during ion exchange chromatography

Optimization of extraction of β-endoglucanase from the fermented bran of Aspergillus niger

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