Production and properties of a soymilk-clotting enzyme system from a microorganism.

Park, Yang Won; Kusakabe, Isao; Kobayashi, Hideyuki; Murakami, Kazuo

doi:10.1271/bbb1961.49.3215

Cited by 6 publications

(6 citation statements)

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“…Bromelain attacked the basic subunit of 11S globulin and converted them to low molecular weight fragments (LMWF), and aggregation developed with an increase of the fragments. Some microorganisms were reported to secrete an enzyme with a clotting activity of soybean milk (13). Recently, it was reported that a novel serine proteinase of Bacillus pumilus showed the coagulating activity of soybean milk and that it degraded the acidic subunit in glycinin and R′-, R-, and β-subunits in β-conglycinin but not the basic subunit of glycinin (14).…”

Section: Introductionmentioning

confidence: 99%

“…On the other hand, the reaction mechanism has been studied extensively in the case of the coagulation of milk casein induced by chymosin or pepsin (production of cheese) ( − ) and that of fibrin induced by thrombin (blood clotting) ( − ). However, there are only a few reports on the protease-induced coagulation of soy protein ( − ). It was reported that heat-induced water-soluble soybean proteins prepared from defatted soybean meal showed aggregation and gelation by treatment with stem bromelain ().…”

Section: Introductionmentioning

confidence: 99%

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Coagulation of Soy Protein Isolates Induced by Subtilisin Carlsberg

Inouye

Nagai

Takita

2002

J. Agric. Food Chem.

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The coagulation of soy protein isolates (SPI) induced by subtilisin Carlsberg was studied. The proteins were digested to fragments of 16 kDa or less in the early stage of the reaction, followed by coagulation. The time-course of the coagulation measured by turbidity was separated into three phases. The turbidity decreased from the initial level observed at time zero to the minimum level (OD1) at time T1 (15-20 min) in the first phase. Then, it increased drastically to reach the maximum (OD2) at time T2 (60-70 min) in the second phase, which was followed by a slight decrease in the third phase. The coagulation was terminated at T2, where 30-35% of the weight of the SPI proteins was in coagula. Proteins in the coagula were degraded slowly in the prolonged incubation, and the protein content in the coagula was finally 15-20% of the weight. The time-course of the turbidity agreed well with that of the weight of the precipitates formed, indicating that the turbidity reflects the progress of the coagulation. The turbidity change (OD1 to OD2) from the start to the end of the coagulation increased proportionally to the SPI concentration (4.9-11 mg/mL), although the time (T1 to T2) needed for the coagulation was independent of the concentration. The growth of the coagula is promoted by increasing the SPI concentration and is rate-limiting in the coagulation.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Coagulation of Soy Protein Isolates Induced by Subtilisin Carlsberg

Inouye

Nagai

Takita

2002

J. Agric. Food Chem.

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“…It is not yet a viable alternative to dairy foods. For that reason, the commercial use of enzymes such as bromelain, ficin, and papain for the curdling of soybean milk has been unsuccessful [20][21][22]. The authors have reported that physical properties of soy protein modified by enzyme reactions such as germinated proteolysis in soybeans.…”

Section: Soy Milk Curdling Yeast and Characteristics Of Curdling Enzymentioning

confidence: 99%

New Cheese-Like Food Production from Soy Milk — Utility of Soy Milk Curdling Yeast

Kanauchi¹,

Hatanaka²,

Shimoyamada³

2015

Food Production and Industry

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Soybeans are a traditional food in eastern Asia, particularly in Japan and China. They were eaten in 100 BC in China. The beans can be processed into Tofu, soy milk, fermented seasonings, soy sauce or Miso paste, and Natto and green beans. Soybeans have rich nutrition, protein lipid, and other functional substances such as isoflavones. However, soybeans are difficult to process for use as food because of tissue and cell wall hardness. Therefore, soybeans are conducted to do some treatments, e.g., boiling, steaming, roasting, crushing/grinding, and some enzyme treating, to eat soy protein easily. Soy storage proteins mainly comprise two proteins as 7S globulin composed with β-conglycinin and 11S globulin containing glycinin composed of 5 subunits. β-Conglycinin, included in 7S globulin, is composed of three subunits. To modify the physical properties of soy protein, a new type of enzyme for curdling soybean milk enzyme was purified as an extract from yeast. Yeast producing curdling soybean milk enzyme, the SCY003 strain, was isolated from 1345 yeast strains. According to the morphology, physiology, and molecular and characteristics, SCY003 was identified as Saccharomyces bayanus. The soy milk curdling enzyme having proteolytic activity was approximately 45 kDa and monomer protein. The optimum pH for the protease activity was pH 7.5; the optimum temperature was 50°C. The enzyme cleaved the β-conglycinin as α-, α′-, and part of glycinin as A 3 A 4 , A 1b , and A 2 in soy protein by endoproteolysis. Soybean protein became loosely curdled with the addition of other proteases from microorganisms or plants. Soybean milk curdled after cleaving endoproteolysis enzyme in SCY003 strain.

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“…For that reason, the commercial use of enzymes such as bromelain, ficin, and papain for the curdling of soybean milk has not been successful (Arima et al 1968;Khan et al 1979;Nouani et al 2009). Thus, it is not yet a viable alternative to dairy foods (Park et al 1985;Park et al 1989;Qua et al, 1981).…”

Section: Introductionmentioning

confidence: 99%

Characteristics and Purification of Soybean Milk Curdling Enzyme-Producing Yeast Saccharomyces bayanus SCY003

Hatanaka

Maegawa

Kanauchi

et al. 2014

FSTR

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Soybeans and the processed food, soybean milk, have important health functions. A cheese-like food produced from soybean milk resembles casein protein in its mouthfeel and physical properties. The intracellular soybean milk curdling enzyme-producing Saccharomyces bayanus SCY003 strain was screened. The curdling enzyme is an intracellular protease, a 45 kDa monomer protein that degrades soy protein subunits, produced by this strain.The optimum temperature and pH of enzyme activity are 50℃ and pH 7.5, respectively. The protease degrades β-conglycinin and parts of glycinin in soy protein to α', α and β subunits. The rheological characteristics of the resultant curd were assessed, and revealed that elasticity differed from curd produced by glucono δ-lactone, which is used in tofu production. A new soy protein food having health-supporting functions will be developed using this protease.

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Production and properties of a soymilk-clotting enzyme system from a microorganism.

Cited by 6 publications

References 0 publications

Coagulation of Soy Protein Isolates Induced by Subtilisin Carlsberg

Coagulation of Soy Protein Isolates Induced by Subtilisin Carlsberg

New Cheese-Like Food Production from Soy Milk — Utility of Soy Milk Curdling Yeast

Characteristics and Purification of Soybean Milk Curdling Enzyme-Producing Yeast Saccharomyces bayanus SCY003

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