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Original Paper Antihypertensive Potentials of Blue, Dutch and Swiss

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Original Paper Antihypertensive Potentials of Blue, Dutch and Swiss Milk Science Vol. 66, No. 2 2017 Original Paper Antihypertensive potentials of Blue, Dutch and Swiss cheeses containing ValProPro and IleProPro peptides Keiichi Matsuura1, Takanobu Gotou2,KyosukeKawaguchi3, Seiichi Mizuno1, Naoyuki Yamamoto4 (1Products Research & Development Laboratory, Asahi Soft Drinks Co., Ltd., Moriya-shi, Ibaraki 3020106 2R&D Section, Asahi Group Holdings Ltd., Azumabashi, Sumida-ku, Tokyo 1308602 3Core Technology Laboratories, Asahi Group Holdings Ltd., Moriya-shi, Ibaraki 3020106 4R&D Center, Asahi Group Holdings Ltd., Sagamihara-shi, Kanagawa 2520206) Abstract The antihypertensive peptides, ValProPro (VPP) and IleProPro (IPP), were ˆrst isolated from Lactobacillus helveticus fermented milk; however, there are few reports on the antihypertensive eŠects of cheese. The objective of this study was to quantify the amounts of VPP and IPP in various cheeses and to discuss the potential of these antihyperten- sive eŠects. Fifteen European-type cheeses were selected and analyzed for these two antihypertensive peptides using an LCMS analysis. The Dutch cheeses, Reypenaer and Old Amsterdam, contained high amounts of VPP/IPP, 19.9/0.9 and 10.5/0.9 mg in 100 g of cheese, respectively. The Swiss cheeses, Emmental and Gruyere, also contained VPP/IPP at 8.0/1.1 and 5.2/1.2 mg in 100 g of cheese, respectively. Notably, some French-type Blue cheeses prepared with Penicillium roqueforti contained the highest amounts of both peptides (13.3/31.0 mg in Bleu d'Auvergne and 9.9/19.2 mg in Bleu des Causses in 100 g of cheese). The ratio of VPP to IPP was higher in Dutch and Swiss cheeses than in Blue cheeses. To understand the release of these peptides in Blue cheese, proteolytic enzymes, neutral protease I (NPI) and leucine amino peptidase (LAP), previously identiˆed as crucial proteolytic enzymes for IPP processing in Aspergillus oryzae, were searched in Penicillium usingBLAST.AhomologwithsimilaritytoNPIofA. oryzae was detected in extracellular metalloproteinase4ofPenicillium subrubescens with 36 identity. Moreover, LAP of A. oryzae was identi- cal to an unknown protein of P. roqueforti. These observations suggest that proteases of Penicillium with homology to A. oryzae NPI and LAP might be involved in the processing of antihypertensive peptides during Blue cheese ripening. Key words: antihypertensive peptide, ValProPro and IleProPro, Penicillium roqueforti, Aspergillus oryzae, Lactobacillus helveticus, Blue cheese the production of amino acids and peptides and Introduction the subsequent amino acid conversion to aromatic compounds. Among the LAB, Lactobacillus helveti- Microorganisms have proteolytic systems to cus has the highest proteolytic activity and can decompose various proteins to utilize peptides and release the most peptides. In the cheese-making amino acids as nitrogen sources for their growth. process, L. helveticus is generally used in mixed Lactic acid bacteria (LAB) and mold have been starter cultures for rapid acidiˆcation and accelera- traditionally used in the manufacturing of cheese tion of cheese ripening. and yogurt to add speciˆc ‰avors and tastes via Cheese and yogurt fermented with LAB and/or mold also have nutraceutical beneˆts, such as Corresponding author: Naoyuki Yamamoto (Tel0427697811，Fax0427697842， constipation relief1) and a cholesterol-lowering E-mail: naoyuki.yamamoto＠asahigroup-holdings.com) eŠect2). Our previous study reported the release March 10, 2017 received April 24, 2017 accepted of antihypertensive peptides, ValProPro (VPP) [doi:10.11465/milk.66.97] and IleProPro (IPP),inL. helveticus fermented 第巻 milk35). These two peptides are thought to be amount of hot water, pre-heated at 60°C, was processed from casein by speciˆc proteolytic added to the precipitate and the suspension was enzymes of L. helveticus67). These peptides have vortexed. The supernatant was collected again inhibitory activities against angiotensin Iconvert- after a centrifugation at 4,000 rpm for 20 min. The ing enzyme (ACE)(kininase II; EC 3.4.15.1), supernatants were combined and ˆltered through a which plays a key role in the control of hyperten- Millipore ˆlter with a molecular sieve size of 0.45 sion8). The blood pressure lowering eŠects of mm. L. helveticus fermented milk have been reported Quantiˆcation of VPP and IPP: In cheese products, in many clinical trials on Japanese and European many kinds of peptides are released from milk subjects912). Mechanism of actions were casein by the proteolytic actions of LAB and mold. studied by pharmacokinetical13) and genetical14) Thus, the LCMS method was used to quantify approaches. Safety of these peptides were also VPP and IPP among the various peptides in cheese investigated by some studies15,16) Moreover, a products. The amounts of VPP and IPP extracted recent meta-analysis of many trials reported a by incubation in hot water (described above) were signiˆcant antihypertensive eŠect1719). analyzed according to a previously reported Many kinds of peptides are released in the method with some modiˆcations21). VPP and IPP ripening process of cheese with the involvement of were quantiˆed by the internal standard method 13 13 LAB and some molds. Speciˆcally, cheese with a VPP isotope ([ C5]Val[ C5]ProPro, m/ 13 manufactured by the ripening with L. helveticus is z 324.2) and IPP isotope (Ile[ C5]ProPro, m/z most likely to contain VPP and IPP. Moreover, 332.2) obtained from SCRUM Inc. (Tokyo, mold used in cheese ripening may have a potential Japan). The concentrations of the standards (VPP to release antihypertensive peptides. Aspergillus and IPP) were 0, 0.3, 0.6, 1.2 and 4.8 mg/mL, oryzae, a frequently used mold in the manufactur- and the internal standard (VPP isotope and IPP ing of traditional Japanese fermented foods, isotope) was 1.5 mg/mL. released a high amount of VPP and IPP from Homology search:BLAST(http:// blast.ncbi.nlm. casein20). Thus, in this study, we analyzed two nih.gov/Blast.cgi) searches were conducted using antihypertensive peptides in various cheeses sequences of NPI and LAP of A. oryzae, accession expecting to ˆnd an increase cheese ripening by numbers AAF046282222) and AF419160.123), proteolysis of LAB and mold by using the LCMS respectively. method21). Results Materials and Methods Quantiˆcation of VPP and IPP in various cheeses: Materials: Characteristics of various cheeses European cheeses, generally manufactured using including hard, semi-hard, Blue and cream-types, long ripening times to accelerate ripening, were purchased in a European market, are listed in obtained to analyze their peptide releases (Table Table 1. Information about the microorganisms 1).AsLactobacillus helveticus has the reported used in each product as starter cultures is also potential to release VPP and IPP during milk included in Table 1. fermentation, some cheeses contained high Preparation of peptides in cheese products:To amounts of VPP and IPP (Table 2). Dutch- and prepare the peptide fractions from cheese Swiss-type cheeses fermented with starter consist- products, each cheese was shredded and then ing of Lactobacillus helveticus contained relatively freeze-dried to produce cheese powder. An equal high amounts of VPP and IPP (Table 2). Amounts amount of hot water (pre-heated to 60°C) was of the two peptides in Dutch- and Swiss-type added to the cheese powder and homogenized. The cheeses were 100fold higher than that of the suspension was centrifuged at 4,000 rpm for 20 lowest one (Fromage d'a‹nois). For Dutch-type min after storing the suspension at 60°Cfor1hr. cheese, Reypenaer and Old Amsterdam, contained After collection of the supernatant, an equal VPP/IPP amounts of 19.9/0.9 and 10.5/0.9 mg in 第号 Table 1 Various kinds of cheeses for peptide analysis. Cheese Reported starter Milk Type Country, Area History Bleu d'Auvergne Penicillium roquefortii Cow Blue Auvergne, France 1850s Bleu des Causses Penicillium roquefortii Cow Blue Curuses, France 1925 Reypenaer VSOP Lactococcus lactic subsp. lactis Cow Semi-hard The Netherlands 1906 Lactococcus lactis subsp. cremoris Lactococcus lactis subsp. lactis biovar diacetylactis Leuconostoc mesenteroides subsp. cremoris Lactobacillus helveticus Lactobacillus lactis Old Amsterdam Lactococcus lactic subsp. lactis Cow Semi-hard, The Netherlands 19th Century Lactococcus lactis subsp. cremoris Gouda type Lactococcus lactis subsp. lactis biovar diacetylactis Leuconostoc mesenteroides subsp. cremoris Lactobacillus helveticus Lactobacillus lactis Emmental Streptococcus thermophilusis Cow Hard Switerland 14th Century Lactobacillus helveticus Lactobacillus bulgaricus Propionibacter freudenreichii Propionibacter shermani Gruyere Lactobacillus helveticus Cow Semi-hard Switherland 19th Century Lactobacillus casei Lactobacillus rhamnosus Fourme d'Ambert Penicillium roqueforti Cow Blue Auvergne, France 1972 Castello Blue Penicillium roqueforti Cow Blue Denmark 1893 Gouda Oud Lactococcus lactis subsp. lactis Cow Semi-hard The Netherlands Lactococcus lactis subsp. cremoris Lactococcus lactis subsp. lactis biovar diacetylactis Leuconostoc mesenteroides subsp. cremoris NSLAB Cheddar Lactococcus lactis subsp. lactis Cow Semi-hard UK 1170 Lactococcus lactis subsp. cremoris NSLAB Gouda Lactococcus lactis subsp. lactis Cow Semi-hard The Netherlands 12th Century Lactococcus lactis subsp. cremoris Lactococcus lactis subsp. lactis biovar diacetylactis Leuconostoc mesenteroides subsp. cremoris NSLAB Blue de Bresse Penicillium roqueforti (Penicillium camanberti) Cow Blue France, Bresse 1951 Stilton Penicillium glaucum Cow Blue UK 1727 Gorgonzola
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