Progress in the field of aspartic proteinases in cheese manufacturing: structures, functions, catalytic mechanism, inhibition, and engineering

Yeğin, Sırma; Dekker, P.

doi:10.1007/s13594-013-0137-2

Cited by 56 publications

(56 citation statements)

References 118 publications

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“…[53,54] The hydrolysis of caseins in cheese by residual coagulant produces essential substrates for some bacterial microflora, whose degradation allows flavour development during ripening. [6] However, the intensity of these effects on cheese quality depends on the type of plant coagulant, its dose, and its enzymatic activities.…”

Section: Citrus Aurantiummentioning

confidence: 99%

“…Several studies have reported the reduction of the thermo-stability of microbial enzymes by applying chemical modifications to preparations of rennet or by using genetic engineering tools on the microbial organism. [6] Nowadays, some of the best rennets available are of microbial origin. Nonetheless, this does not exclude the fact that there is no place for plant-derived rennet, most certainly in scientific research.…”

Section: Introductionmentioning

confidence: 99%

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Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Amira

Besbes

Attia

et al. 2017

International Journal of Food Properties

104

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Plant rennets hold an important position among various coagulants used in cheese technology. The selection of a suitable plant coagulant is important due to the increasing global demands of cheese alongside reduced supply of calf rennet. Thus, a literature synthesis is presented to investigate recent achievements on their functional properties and enzymatic role in cheese making. Efforts have also been done to compare certain rheological and sensory properties of final products, arising from some plant-and animalbased rennets. In fact, some coagulants such as actinidin or dubiumin produce cheeses with sensory qualities similar to those produced by animal rennet. Others, like ginger, cucumisin, or hieronymain proteases contribute to develop very different textures and flavours, due to excessive proteolytic activity and production of bitter peptides. For milk-clotting enzymes with high non-specific action, several improved strategies have been developed to produce cheeses with sensory properties close to those of animal rennet. For example, the mixture of coagulants (cardosins/chymosin), the selection of appropriate milk or its ultrafiltration, as well as the increase of salting time of cheese during ripening could be efficient ways to improve texture and reduce bitterness. Concerning cheeses with high yield loss, the whey could be used for a traditional production of whey cheese. To conclude, the selection of appropriate plant rennet with high milk-clotting activity/proteolytic activity ratio and the optimisation of all coagulation parameters play a central role in manufacturing cheese with superior rheological and sensory properties.

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Section: Citrus Aurantiummentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Amira

Besbes

Attia

et al. 2017

International Journal of Food Properties

104

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“…Although it is well known that aspartic proteases are the most suitable enzymes used as milk clotting agents for the manufacture of cheese [9,10], some serine proteases from different sources have been used recently as natural rennets [11][12][13][14][15]. Therefore, it is important to study casein micelle coagulation by P7 in the presence of different mineral salts of interest to the dairy industry.…”

Section: Introductionmentioning

confidence: 99%

Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool

Lombardi

Spelzini

Corrêa

et al. 2016

Colloids and Surfaces B: Biointerfaces

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Structural changes of casein micelles and their aggregation induced by a novel enzymatic pool isolated from Bacillus spp. in the presence of calcium, magnesium or zinc were investigated. The effect of cations on milk protein structure was studied using fluorescence and dynamic light scattering. In the presence of cations, milk protein structure rearrangements and larger casein micelle size were observed. The interaction of milk proteins with zinc appears to be of a different nature than that with calcium or magnesium. Under the experimental conditions assayed, the affinity of each cation for some groups present in milk proteins seems to play an important role, besides electrostatic interaction. On the other hand, the lowest aggregation times were achieved at the highest calcium and zinc concentrations (15 mM and 0.25 mM, respectively). The study found that the faster the aggregation of casein micelles, the less compact the gel matrix obtained. Cation concentrations affected milk protein aggregation kinetics and the structure of the aggregates formed.

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“…Phylogenetic analysis is able to provide deeper insights into the evolution of a new clade. The phylogenetic tree showed that Tl APA1 largely differed with other homologs in terms of the amino acid sequence, indicating that Tl APA1 potentially had distinct enzyme characteristics and special applications like the mucorpepsin subgroup, a unique clade in the evolutionary process and an important class of proteases, widely used as milk coagulating agents (39). The evolution of A1 family has been well studied, which has contributed to an indepth understanding of fungal aspartic protease evolution (40).…”

Section: Discussionmentioning

confidence: 99%

A novel thermostable aspartic protease fromTalaromyces leycettanusand its specific autocatalytic activation through an intermediate transition state

Guo

Ren

et al. 2019

Preprint

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ABSTRACTAspartic proteases exhibit optimum enzyme activity under acidic condition and have been extensively used in food, fermentation and leather industries. In this study, a novel aspartic protease precursor (proTlAPA1) from Talaromyces leycettanus was identified and successfully expressed in Pichia pastoris. Subsequently, the auto-activation processing of the zymogen proTlAPA1 was studied by SDS-PAGE and N-terminal sequencing, under different processing conditions. TlAPA1 shared the highest identity of 70.3 % with the aspartic endopeptidase from Byssochlamys spectabilis (GAD91729) and was classified into a new subgroup of the aspartic protease A1 family, based on evolutionary analysis. Mature TlAPA1 protein displayed an optimal activity at 60 °C and remained stable at temperatures of 55 °C and below, indicating the thermostable nature of TlAPA1 aspartic protease. During the auto-activation processing of proTlAPA1, a 45 kDa intermediate was identified that divided the processing mechanism into two steps: formation of intermediates, and activation of the mature protein (TlAPA1). The former step was completely induced by pH of the buffer, while the latter process depended on protease activity. The discovery of the novel aspartic protease TlAPA1 and study of its activation process will contribute to a better understanding of the mechanism of aspartic proteases auto-activation.IMPORTANCEThe novel aspartic protease TlAPA1 was identified from T. leycettanus and expressed as a zymogen (proTlAPA1) in P. pastoris. Enzymatic characteristics of the mature protein were studied and the specific pattern of zymogen conversion was described. The auto-activation processing of proTlAPA1 proceeded in two stages and an intermediate was identified in this process. These results describe a new subgroup of aspartic protease A1 family and provide insights into a novel mode of activation processing in aspartic proteases.

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Progress in the field of aspartic proteinases in cheese manufacturing: structures, functions, catalytic mechanism, inhibition, and engineering

Cited by 56 publications

References 118 publications

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool

A novel thermostable aspartic protease fromTalaromyces leycettanusand its specific autocatalytic activation through an intermediate transition state

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