Plant Milk-Clotting Enzymes for Cheesemaking

Nicosia, Fabrizio Domenico; Puglisi, Ivana; Pino, Alessandra; Caggia, Cinzia; Randazzo, Cinzia Lucia

doi:10.3390/foods11060871

Cited by 29 publications

(23 citation statements)

References 115 publications

(136 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The proteolytic activity (PA) of a clotting enzyme is an important parameter for cheese ripening; high values of proteolysis are often associated with the formation of off flavor and bitter taste due to the production of short peptides [ 7 , 23 ]. The maximum value of proteolytic activity of the aqueous extract from the pulp of kiwifruits was reached at pH 6.5, and decreased at more acidic or alkaline pHs ( Figure 6 ), in agreement with Lo Piero et al (2011) [ 16 ].…”

Section: Discussionmentioning

confidence: 99%

“…By using EPS, it is possible to obtain cheese with excellent quality [ 6 ]. However, technologies involving recombinant DNA are the subject of great debate for ethical reasons, and many countries, such as France, Germany and the Netherlands, have restricted the use of FPC [ 7 , 8 ]. Nowadays, a completely natural alternative is represented by plant-derived milk-clotting enzymes, which are commercialized and used as valid substitutes for animal rennet [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

An Easy and Cheap Kiwi-Based Preparation as Vegetable Milk Coagulant: Preliminary Study at the Laboratory Scale

Nicosia

Puglisi

Pino

et al. 2022

Foods

Self Cite

View full text Add to dashboard Cite

In the present study, a kiwifruit aqueous extract was developed and used as a coagulant enzyme in cheesemaking. In detail, polyacrylamide gel electrophoresis (SDS-PAGE) was used to investigate the presence of actinidin, the kiwifruit enzyme involved in κ-casein hydrolysis, in different tissues (pulp, peel, and whole fruit) of ripe and unripe kiwifruits. Data revealed the presence of the enzyme both in the peel and in the pulp of the fruit. Although the aqueous extract obtained from the kiwifruit peel was able to hydrolyze semi-skimmed milk, it did not break down κ-casein. The aqueous extract obtained from the pulp showed a hydrolytic activity toward both κ-casein and semi-skimmed milk. The values for milk-clotting and proteolytic activity of the kiwifruit pulp extract were evaluated at different temperatures and pH parameters in order to obtain a high value of the MCA/PA ratio; we found that a temperature of 40 °C in combination with a pH value of 5.5 allowed us to obtain the best performance. In addition, the data revealed a higher hydrolytic activity of the enzymatic preparation from ripe kiwifruits than that from unripe ones, suggesting the use of the extract from pulp of ripe kiwifruits in the laboratory-scale cheesemaking. The data showed that 3% (v/v) of the ripe kiwifruit pulp extract determined a curd yield of 20.27%, comparable to chymosin yield. In conclusion, the extraction procedure for kiwifruit aqueous extract proposed in the present study was shown to be a fast, cheap, chemical-free, and ecofriendly technology as a plant coagulant for cheese manufacturing.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An Easy and Cheap Kiwi-Based Preparation as Vegetable Milk Coagulant: Preliminary Study at the Laboratory Scale

Nicosia

Puglisi

Pino

et al. 2022

Foods

Self Cite

View full text Add to dashboard Cite

show abstract

“…Milk‐clotting enzyme is used to coagulate milk to produce cheese. The selection of specific coagulation enzymes in cheese production is an important step in the process of milk coagulation and is known to affect cheese yield, texture, and flavor (Nicosia et al, 2022). Shieh et al used B. subtilis natto Takahashi to determine the optimal culture conditions affecting the production of milk coagulase (Shieh et al, 2009).…”

Section: Functional Compounds Produced By B Subtilis Nattomentioning

confidence: 99%

Biological functions of compounds from Bacillus subtilis and its subspecies, Bacillus subtilis natto

Miyazawa

Abe

Bhaswant

et al. 2022

Food Bioengineering

View full text Add to dashboard Cite

Natto, fermented food produced by Bacillus subtilis natto (B. subtilis natto), is widely consumed around the world, and its potential health functions are attracting attention. Natto has been reported to have a variety of bioactive compounds such as levan, menaquinone‐7, nattokinase, and others. Such bioactive compounds produced by B. subtilis natto are deeply involved in the function of natto, because they are consequently contained in natto. This review summarizes bioactive compounds and its functions of (1) B. subtilis and its subspecies, (2) B. subtilis natto. Overall, natto is a natural source of bioactive compounds and is expected to be applied to functional foods.

show abstract

“…However, various plant‐derived milk‐clotting enzymes are also available for cheese‐making (Nicosia et al., 2022). Aspartic proteases, commonly known as acid proteases or aspartyl proteases, are classified as hydrolases (group 3) within subgroup 4, which can hydrolyze peptide bonds.…”

Section: Introductionmentioning

confidence: 99%

Production of a novel milk‐clotting enzyme from solid‐substrate Mucor spp. culture

Qasim

Diercks-Horn

Gerlach

et al. 2022

Journal of Food Science

View full text Add to dashboard Cite

Calf rennet has been traditionally used for cheese making all over the world since ancient times. It is primarily a type of aspartic protease. Calf rennet, also known as chymosin, is considered the best milk coagulant in cheese manufacturing. Its usage and demand are increasing day by day in the food industry; however, some ethical issues are also related since it is naturally present in the calf's stomach and obtained by the slaughtering of young animals. Therefore, researchers are trying to introduce some new and better alternatives for chymosin in the food industry. Mucor racemosus f. racemosus CBS 381, Mucor racemosus DSM 62760, and Aspergillus oryzae were cultivated by solid substrate fermentation using the design of experiment (DoE) (MODDE; Umetrics, Sweden) to optimize and analyze the various combinations of different factors and responses (milk-clotting activity, proteolytic activity, specific activity). Based on the analysis of the screening and optimization results, Mucor racemosus CBS 381 was found to be the potential strain in terms of high production of aspartic protease, as well as had high milk-clotting activity under a solid-state fermentation system. However, molasses and casein were determined to be significant carbon and nitrogen sources, respectively, under conditions such as 70% moisture content and 25 • C temperature. The molecular weight of the enzyme (Mucor CBS 381) is ∼30 KDa and it exhibits maximum activity at pH 4.8 at 45 • C. The investigated enzyme was pronounced as thermal-sensitive and lost activity completely after 10 min incubation at 55 • C. The remarkable qualities of the studied enzyme, such as cost-effective production, milk-clotting and proteolytic activity make Mucor racemosus CBS 381 a promising alternate to calf chymosin in the cheese-making industry.

show abstract

Plant Milk-Clotting Enzymes for Cheesemaking

Cited by 29 publications

References 115 publications

An Easy and Cheap Kiwi-Based Preparation as Vegetable Milk Coagulant: Preliminary Study at the Laboratory Scale

An Easy and Cheap Kiwi-Based Preparation as Vegetable Milk Coagulant: Preliminary Study at the Laboratory Scale

Biological functions of compounds from Bacillus subtilis and its subspecies, Bacillus subtilis natto

Production of a novel milk‐clotting enzyme from solid‐substrate Mucor spp. culture

Contact Info

Product

Resources

About