Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein

Rajagopalan, Anusha; Singh, Maheshwari Kumari; Sukumaran, Bindhu Omana

doi:10.1007/s00217-014-2177-0

Cited by 44 publications

(35 citation statements)

References 25 publications

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“…In order to detect the optimum of activity, different comparison studies were carried out between extracts of different parts in the same plant. Results of Anusha et al [3] revealed that the highest clotting activity was observed in the extract of latex followed by extracts of stems, leaves, and flowers of Calotropis gigantea, in descending order. This is in contradiction with extracts of C. cardunculus, whose clotting activity is concentrated mainly on flowers, because of the predominance of coagulating enzymes (cardosins) in this part of the plant.…”

Section: Evaluation Of Enzymatic Activities Of Plant Rennetsmentioning

confidence: 97%

“…However, the worldwide increase in cheese production, coupled with reduced supply and increasing prices of calf rennet, has led to search for alternative milk-clotting enzymes, as appropriate rennet substitutes. [3,4] Apart from this, some religious factors (Islam and Judaism) and others related to vegetarism of some consumers have greatly limited their use. [4] Several milk-clotting enzymes of microbial origin have been commercialised and used in cheese making, such as aspartic proteases (APs) obtained from Rhizomucor miehei, Rhizomucor pusillus, and Cryphonectria parasitica.…”

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

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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: Evaluation Of Enzymatic Activities Of Plant Rennetsmentioning

confidence: 97%

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

View full text Add to dashboard Cite

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“…However, most of the enzyme preparations from the above sources were found unsuitable because they produced cheese with low yield and bitter taste due to the low ratio of milk‐clotting/proteolytic activities (Anusha et al. ; Shah et al. ).…”

Section: Introductionmentioning

confidence: 99%

“…Consequently, much research interest has been focused on the discovering milk-clotting enzymes from other sources, and, as a result, several enzyme preparations of animal, microbial, and plant origin have been discovered (Jacob et al 2011). However, most of the enzyme preparations from the above sources were found unsuitable because they produced cheese with low yield and bitter taste due to the low ratio of milk-clotting/ proteolytic activities (Anusha et al 2014;Shah et al 2014). Therefore, the search for a rennet substitute from plant sources having a high ratio of milk-clotting/proteolytic activity is extremely needed to be used for the production of cheese with better quality.…”

Section: Introductionmentioning

confidence: 99%

Characterization of partially purified milk‐clotting enzyme from sunflower (Helianthus annuus) seeds

Nasr

Ahmed

Hamid

2016

Food Science & Nutrition

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This study was aimed to extract milk-clotting enzyme from sunflower seeds and to determine its potentiality for manufacturing white soft cheese from cows and goats milk. The seeds were blended and extracted using two types of buffers and milk-clotting and proteolytic activities were evaluated. The enzyme was partially purified using ammonium sulfate fractionation techniques. Results indicated that sunflower seeds extracted with 5% NaCl in 50 mmol/L acetate buffer, pH 5.0, had the highest milk-clotting activity (MCA) and lowest coagulation time compared to that extracted with only acetate buffer (pH 5.0). Ammonium sulfate at 30-50% saturation purified the enzyme to 4.3 folds with MCA of 241.0 U/mL and final enzyme yield of 10.9%. The partially purified enzyme was characterized by SDS-PAGE that showed two bands with molecular weight of 120 and 62 kDa. When compared with other plant enzymes, the partially purified sunflower enzyme was found to have higher milk-clotting activity and lower proteolytic activity. Also, both milk sources and enzyme types significantly affected the cheese yield and curd formation time. The cheese made from cow milk using sunflower enzyme had higher yield compared to that obtained using commercial rennet, whereas the opposite was observed when using goat milk. 734

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“…The first and the most widely coagulating enzyme preparation, used in cheese processing, was calf rennet. However, the worldwide increases in cheese production, along with reduced supply of calf rennet and higher prices, have led to search for alternative milk-clotting enzymes, as appropriate rennet substitutes [1,2]. Aspartic proteases extracted from plants have become a subject of growing interest in dairy technology [3], due to their easy availability and their efficient purification processes.…”

Section: Introductionmentioning

confidence: 99%

Identification of proteins from wild cardoon flowers (Cynara cardunculus L.) by a proteomic approach

et al. 2016

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Proteomic approach was applied to identify total proteins, particularly the enzymatic content, from wild cardoon flowers. As the selection of an appropriate sample preparation method is the key for getting reliable results, two different extraction/precipitation methods (trichloroacetic acid and phenol/ammonium acetate) were tested on fresh and lyophilized flowers. After two-dimensional electrophoresis (2D-E) separations, a better protein pattern was obtained after phenol extraction from lyophilized flowers. Only 46 % of the total analyzed spots resulted in a protein identification by mass spectrometry MALDI-TOF. Four proteases (cardosins A, E, G, and H), which have become a subject of great interest in dairy technology, were identified. They presented molecular weights and isoelectric points very close and high levels of homology between matched peptides sequences. The absence of the other cardosins (B, C, D, and F) could be an advantage, as it reduces the excessive proteolytic activity that causes bitter flavors and texture defects, during cheese making.

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Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein

Cited by 44 publications

References 25 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

Characterization of partially purified milk‐clotting enzyme from sunflower (Helianthus annuus) seeds

Identification of proteins from wild cardoon flowers (Cynara cardunculus L.) by a proteomic approach

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