Proteolysis of whey proteins by a Bacillus subtilis enzyme preparation

Castro, Serafín Novás; Peyronel, Daniel Vazquez; Cantera, Ana María B.

doi:10.1016/0958-6946(95)00024-0

Cited by 15 publications

(9 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Casein hydrolysis by purified enzyme was investigated by the method of Castro et al (1996) with slight modification. Briefly, one ml of enzyme solution was added to 5.0 ml of 1% commercial bovine a s -, b-and j-caseins in 50 mM sodium phosphate buffer (pH 6.5).…”

Section: Casein Hydrolysismentioning

confidence: 99%

“…The reaction was stopped by the addition of equal amount of 10% TCA, followed by centrifugation at 10,000g for 10 min, and absorbance estimation of supernatants at 280 nm. According to Castro et al (1996), the degree of hydrolysis (DH%) was defined as the percentage of broken peptide bonds, with an assumption that aromatic amino acids were partitioned in an equivalent manner during hydrolysis.…”

Section: Casein Hydrolysismentioning

confidence: 99%

See 1 more Smart Citation

Ginger rhizome as a potential source of milk coagulating cysteine protease

et al. 2011

View full text Add to dashboard Cite

Section: Casein Hydrolysismentioning

confidence: 99%

Section: Casein Hydrolysismentioning

confidence: 99%

Ginger rhizome as a potential source of milk coagulating cysteine protease

et al. 2011

View full text Add to dashboard Cite

“…After centrifuging for 20 min at 20,600g, absorbance was measured at 337 nm. In this case, one enzymatic unit (Uazo) was defined as the quantity of enzyme required to increase by one absorbance unit the absorbance value at 337 nm per minute in the assay conditions [18].…”

Section: Proteolytic Activity Determinationmentioning

confidence: 99%

Granulosain I, a Cysteine Protease Isolated from Ripe Fruits of Solanum granuloso -leprosum (Solanaceae)

et al. 2008

View full text Add to dashboard Cite

A new cysteine peptidase (Granulosain I) was isolated from ripe fruits of Solanum granuloso-leprosum Dunal (Solanaceae) by means of precipitation with organic solvent and cation exchange chromatography. The enzyme showed a single band by SDS-PAGE, its molecular mass was 24,746 Da (MALDI-TOF/MS) and its isoelectric point was higher than 9.3. It showed maximum activity (more than 90%) in the pH range 7-8.6. Granulosain I was completely inhibited by E-64 and activated by the addition of cysteine or 2-mercaptoethanol, confirming its cysteinic nature. The kinetic studies carried out with PFLNA as substrate, showed an affinity (Km 0.6 mM) slightly lower than those of other known plant cysteine proteases (papain and bromelain). The N-terminal sequence of granulosain I (DRLPASVDWRGKGVLVLVKNQGQC) exhibited a close homology with other cysteine proteases belonging to the C1A family.

show abstract

“…Furthermore, bacteria could be used for the clinical treatment of some food allergies, including milk hypersensitivity (Salminen and others 1998). Castro and others (1996) found that proteins in acid whey were hydrolyzed by an enzymatic preparation from B. subtilis , as a possible treatment that might reduce their allergenicity. However, no research has focused on the enzymes of bacteria from Thai traditional fermented foods in terms of hypoallergenicity.…”

Section: Introductionmentioning

confidence: 99%

Identification of Proteolytic Bacteria from Thai Traditional Fermented Foods and Their Allergenic Reducing Potentials

Phromraksa¹,

Nagano²,

Boonmars³

et al. 2008

Journal of Food Science

View full text Add to dashboard Cite

This study aimed to identify proteolytic bacteria from Thai traditional fermented foods and investigate their allergenic reducing potentials to wheat and milk allergens. Nine bacteria were isolated from fermented foods as follows: fermented soybean seeds (Thua Nao), fermented soybean paste (Thua Nao), wheat flour dough of steamed stuffed bun (Sa La Pao), and soaked rice from Thai fermented rice-noodle (Kha Nhom Jeen) processing. Both phenotypic and genotypic identifications were used in this study. It was found that all isolates were Gram-positive rods. Seven isolates were matched and identified as Bacillus subtilis by both techniques, and the remaining 2 isolates were phenotypically and genotypically identified as B. licheniformis and B. subtilis, respectively. The concentrated crude enzyme of B. subtilis DB and SR could reduce allergenicity of gliadin by hydrolyzing the allergenic gliadin fragments detected by immunoblotting. Furthermore, the enzyme of B. subtilis DB could also reduce allergenicity of beta-lactoglobulin (beta-LG) detected by hydrolyzing the major allergenic epitope of beta-LG at Gln(35)-Ser(36) position. B. subtilis DB and SR can be applied for the production of hypoallergenic wheat flour or milk food products.

show abstract

Proteolysis of whey proteins by a Bacillus subtilis enzyme preparation

Cited by 15 publications

References 18 publications

Ginger rhizome as a potential source of milk coagulating cysteine protease

Ginger rhizome as a potential source of milk coagulating cysteine protease

Granulosain I, a Cysteine Protease Isolated from Ripe Fruits of Solanum granuloso -leprosum (Solanaceae)

Identification of Proteolytic Bacteria from Thai Traditional Fermented Foods and Their Allergenic Reducing Potentials

Contact Info

Product

Resources

About