JP7373856B2 - キシログルカン-オリゴ糖を調製する方法 - Google Patents
キシログルカン-オリゴ糖を調製する方法 Download PDFInfo
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Description
本発明は、とりわけ、食品のカロリー含有量を低下させるために、食品を甘くするために、食品の繊維含有量を増大させるために、食品の食感を改善するために、及び腸内マイクロバイオーム細菌を刺激するために、食品添加物として使用することができるオリゴ糖を調製する方法に関する。さらに、これらは、動物飼料の分野、又は他の用途で応用することができる。より具体的には、本発明は、規定のキシログルカンオリゴ糖に対するキシログルカン多糖の高温加水分解に関する。本発明はさらに、本発明の方法を用いて産生されるオリゴ糖加水分解物、並びにヒト及び/又は動物の栄養摂取における、プレバイオティックとしての又は他の用途のための該オリゴ糖加水分解物の使用に関する。さらに提供されるのは、本発明の方法及び他の用途で使用するための新規のエンドグルカナーゼである。
一般に、脂肪、油、デンプン、炭水化物、糖、及びこれらに由来する製品は、加工食品において広く利用されている。これらの成分は、食品の見た目、味、口当たり、及び他の官能特性に関して極めて重要な機能的意義を有する。しかしながら、これらは、腸を通過する間に、ヒトの体によって代謝され、したがって、そのような食品のカロリー含有量に大きく寄与することができる。最近、消費者は、ますます健康志向になってきている。したがって、多くの個人は、自身の高カロリー食品及び高レベルの脂肪を含有する食品の摂取を最小限に抑えようとしている。消費者は、従来の加工食品の低カロリー及び低脂肪バージョンを要求している。非消化性オリゴ糖を添加することにより、加工食品の官能特性を失わせることなく、糖及び脂肪の量を低下させることができる。
本発明は、請求項1記載の方法によって、問題を解決する。驚くことに、タマリンドカーネルパウダーなどのキシログルカン源の高温加水分解が低カロリー食品添加物を提供し、この食品添加物を用いて、加工食品の現在のカロリー付与含有量を代替すると同時に、官能特性に悪影響を及ぼすことなく、繊維含有量を増大させることができることが分かった。さらに驚くことに、高温手順と及び高温プロファイルを有する酵素とを使用することにより、キシログルカン-多糖加水分解が簡素化され、全体の成績が向上し、追加の精製手順が回避されることが発見された。本発明の方法は、ただ1つの酵素で実施することができるが、それは、50℃よりも高い温度でキシログルカナーゼ活性を示す慎重に選択された特異的酵素が、700g/l以上の高い基質量でさえもキシログルカン-多糖を完全に加水分解するのに十分であるからである。
好ましい実施態様において、本発明は、キシログルカン源からキシログルカンオリゴ糖(XGOS)を産生する方法であって、50℃よりも高い温度でキシログルカナーゼ活性を示す酵素による50℃よりも高い温度でのキシログルカンの酵素的加水分解を含む、方法を提供する。
・50℃よりも高い温度でキシログルカナーゼ活性を示すエンドグルカナーゼによる、50℃よりも高い温度でのキシログルカンの酵素的加水分解、
・固形物の除去、
・塩の除去、
・さらなる不純物の除去、
・任意に、加水分解物の脱色、
・例えば、凍結もしくは噴霧乾燥又は回転乾燥による加水分解物の乾燥、或いは濃縮液体製剤としての加水分解物の保存
という工程を含む。
・50.5~80℃の範囲の温度でキシログルカナーゼ活性を示すエンドグルカナーゼによる、50.5~80℃の範囲の温度でのタマリンド多糖の酵素的加水分解、
・固形物の除去、
・塩の除去、
・さらなる不純物の除去、
・任意に、加水分解物の脱色、
・例えば、凍結もしくは噴霧乾燥又は回転乾燥による加水分解物の乾燥、或いは濃縮液体製剤としての加水分解物の保存
という工程を含む。
本発明のより具体的な実施態様において、タマリンドオリゴ糖の加水分解は、次のように実施することができる。
単離されたタマリンド種子多糖の種々の用途が記載されている(Rao及びSrivastavaの文献、1973を参照)。多糖は、幅広いpH範囲にわたる糖濃度のゼリーを形成する能力を有する。これは、アイスクリーム及びマヨネーズの安定剤として食品中でも使用されている。さらに、織物産業は、綿及び人造絹糸のサイジング、仕上げ、及びプリントにタマリンド多糖を利用している。美容産業において、タマリンド多糖は、エッセンシャルオイル、シェービングクリーム、及び歯磨剤のエマルジョンを調製するために使用されている。これはまた、圧縮丸剤及び錠剤の製造における結合剤として、非油性軟膏の製造における賦形剤として、並びにコロイド状ヨウ素ゼリーの調製におけるゲル化剤として使用されている。
本発明は、配列番号1~4の推定アミノ酸配列を有するポリペプチド、並びにそのようなポリペプチドの断片、類似体、及び誘導体をさらに提供する。配列番号1~4のポリペプチドに言及する場合の「断片」、「誘導体」、及び「類似体」という用語は、キシログルカナーゼと本質的に同じ生物学的機能又は活性を保持するポリペプチドを意味する。類似体は、例えば、プロタンパク質部分の切断により活性化されて、活性のある成熟タンパク質を生じることができるプロタンパク質を含み得る。本発明のポリペプチドは、組換えポリペプチド、天然ポリペプチド、又は合成ポリペプチドであり得る。配列番号1~4のポリペプチドの断片、誘導体、及び類似体は、(i)1以上のアミノ酸残基が保存又は非保存アミノ酸残基(好ましくは、保存アミノ酸残基)と置換されており、かつそのような置換されたアミノ酸残基が遺伝暗号によってコードされているものでも、コードされていないものでもよいポリペプチド、或いは(ii)1以上のアミノ酸残基が置換基を含むポリペプチド、或いは(iii)追加のアミノ酸、例えば、リーダー配列又は分泌配列或いは成熟ポリペプチドもしくはプロタンパク質配列の精製又はその基質もしくは複合体結合に利用される配列が成熟タンパク質に融合されているポリペプチドであり得る。そのような断片、誘導体、及び類似体は、本明細書中の教示に基づいて提供することが当業者の能力の範囲内であるとみなされる。
本発明はまた、本発明のポリヌクレオチド、プロモーター、並びに転写及び翻訳終止シグナルを含む組換え発現ベクターに関する。本明細書に記載される様々な核酸及び制御配列を接続させて、そのような部位でのポリペプチドをコードするヌクレオチド配列の挿入又は置換を可能にするための1以上の(いくつかの)好都合な制限部位を含み得る組換え発現ベクターを産生することができる。或いは、本発明のポリヌクレオチド配列を、ヌクレオチド配列又は該配列を含む核酸コンストラクトを発現用の適当なベクターに挿入することにより発現させることができる。発現ベクターを作製する際に、コード配列は、該コード配列が発現のための適当な制御配列と機能的に連結されるように、ベクター中に配置される。
より好ましくは、本発明は、本発明のポリペプチド、すなわち、配列番号1~4のポリペプチドを産生する方法であって:(a)該ポリペプチドを産生する細胞を、該ポリペプチドの産生の助けとなる条件下で培養すること;及び(b)該ポリペプチドを回収することを含む、方法を提供する。好ましい態様において、該細胞は、バチルス属のものである。より好ましい態様において、該細胞は、枯草菌又はバチルス・リケニフォルミスである。
本発明はまた、本発明のポリペプチド、すなわち、配列番号1~4のポリペプチドを含む組成物に関する。好ましくは、該組成物は、そのようなポリペプチドが濃縮されている。「濃縮された」という用語は、該組成物のエンドグルカナーゼ活性が、例えば、少なくとも1.1の濃縮係数を伴って増加していることを示す。
本発明はさらに、本発明のプロセスにおけるキシログルカン多糖の加水分解で使用するための、配列番号1~4のポリペプチドを含む酵素調製物を提供する。該酵素調製物は、好ましくは、液体、粉粒体、又は凝集粉の形態のもの、より好ましくは、粉粒体又は凝集粉の形態のものである。
(実施例1:エンドグルカナーゼをコードする配列番号11~14のクローニング及び配列番号1~4の発現)
バッファー及び基質として使用される化学物質は全て、少なくとも試薬等級の市販製品であった。
配列番号1及び3のC.サーモセラムATCC27405/DSM1237由来のエンドグルカナーゼ遺伝子、並びに配列番号2及び4のハービボラックス・サクシノコラDSM101079遺伝子を有する組換え大腸菌株の流加回分発酵を、制御され、かつBiostat B Twin DCU(Sartorius AG, Gottingen, Germany)が装着された10L Uni-Vesselで実施した。発酵期間中、温度、pH、泡沫、濁度、重量、及び溶存酸素をオンラインでモニタリングした。溶存酸素(DO%)を25%(vol/vol)に設定し、撹拌を増大させ、かつ気流を一定にして維持した。泡沫の形成は、Antifoam 206(Sigma Aldrich, St. Louis, Missouri, USA)の添加により制御した。25%(vol/vol)水酸化アンモニウム溶液及び25%(vol/vol) HPO4溶液の添加により、6.9のpHを維持した。大腸菌株を、Riesenberg培地(Korzらの文献、1995)中、10Lスケールで培養した。供給溶液は、1021g/Lグリセロール、20g/L MgSO4・7H2O、13mg/L EDTA、4mg/L CoCl2・6H2O、23.5mg/L MnCl2・4H2O、2.5mg/L CuC12・2H2O、5mg/L H3BO3、4mg/L Na2MoO4×2H2O、16mg/L Zn(CH3COO)2・2H2O、40mg/Lクエン酸Fe(III)からなる(Korzらの文献、1995)。最初の炭水化物基質が消費された後、成長速度を、等式1:
大麦β-グルカン(Megazyme)などのモデル基質を使用することにより、比酵素活性を決定した。エンドグルカナーゼ活性は、モデル基質からの還元糖の生成と定義される。1単位の酵素活性は、酵素1mg当たり、60℃、1分間で生成される、マイクロモルで示した還元糖の量と定義される。酵素プロファイル並びに最適な温度及びpHを定義するために、エンドグルカナーゼ(50ng/反応)を、様々なpH(範囲4.0~8.0)を有するクエン酸バッファー(溶液A: 0.2Mクエン酸、0.1M NaCl;溶液B: 0.4M Na2HPO4、0.1M NaCl)に溶解した1%(wt/vol)大麦β-グルカンの存在下、50~80℃の範囲の温度で30分間インキュベートした。還元糖を3,5-ジニトロサリチル酸(DNSA)法により測定した: 50μLの試料を、マイクロタイタープレート中で、75μLのDNSA溶液(10g/L DNSA、200g/L K+-Na+-酒石酸塩、10g/L NaOH、0.5g/L Na2SO4、2g/Lフェノール)と混合し、95℃で5分間インキュベートし、氷上で冷却し、吸収を540nmで測定した。較正のために、0~2mg/mLのグルコース溶液を使用した。
タマリンドカーネルパウダー(TKP)及び脱脂タマリンドカーネルパウダー(dTKP)は、Tamarind Magic, Hyderabad, Phase-IV, 3rd Gate, IDA, Cherlapally, Hyderabad - 500051, Telangana, Indiaから購入した。TKPとdTKPは両方とも、約65%(wt/wt)のキシログルカンからなる(https://www.altrafine.com/tamarind-kernel-powder/)。
25g/LのTKPを60℃で脱塩水に溶解させた。酵素を700g/Lの最終基質量に関して0.05%の所望の濃度で添加した。加水分解プロセスを、250~500rpmで撹拌する3枚のセグメントインペラを備えた2Lの撹拌タンク反応器(Sartorius AG, Gottingen, Germany)中、60℃で72時間実施した。基質を、700g/lの最終基質量が達成されるまで、25g/L/hの割合で供給した。プロセスモニタリングのために、試料を様々な時点で反応器から採取した。試料を遠心分離し、上清を95℃で5分間煮沸して、残留タンパク質を変性させた。XGOSを、実施例5に記載されているアルコール沈殿により、上清由来の5mL試料中で単離し、軽量した。分析のために、上清の試料を回収し、再脱イオン水で希釈し、実施例7に記載されているHPAEC-PADにより測定した。24時間後、75%を超える加水分解度に到達させ、反応時間を72時間に延長することにより、80%超にまで一層さらに向上させた。
純粋なXGOS粉末を得るために(図3)、実施例3及び4由来の加水分解物を遠心分離により分離して、TKP/dTKPの不溶性画分を分離した(9,000rpm、20分、RT)。不溶性画分をさらに使用する1つの例は、動物飼料用のタンパク質が濃縮された高脂肪マトリックスとしてのものであり得る。上清をまず、精密濾過(接線濾過、0.2マイクロメーターフィルターカセット)により、次に、限外濾過(接線濾過、10kDaフィルターカセット)により清澄化した。残留タンパク質、ペプチド、脂肪酸、又は色素を、最大90%(vol/vol)のエタノール濃度でのエタノール沈殿及び氷上で1時間のインキュベーションにより除去した。沈殿を遠心分離により除去し、上清を濃縮し、エタノールを回転蒸発により再利用する。沈殿を、凍結乾燥、デシケーター、又は噴霧乾燥により乾燥させる。
純粋なXGOS粉末を得るために(図3)、実施例3由来の加水分解物を遠心分離により分離して、TKP/dTKPの不溶性画分を分離した(9,000rpm、20分、RT)。上清をまず、精密濾過(接線濾過、0.2μmフィルターカセット)により、次に、限外濾過(接線濾過、10kDaフィルターカセット)により清澄化する。より大きいスケール用の(逐次的)擬似移動床式クロマトグラフィー又はナノ濾過を使用することにより、DP7~DP9の濃縮を達成した。濾液又は抽出物を凍結乾燥、デシケーター、又は噴霧乾燥により乾燥させた。
HPAEC-PADによる分析のために、CarboPac(商標) PA1カラム(4×250mm)及びPA1-プレカラム(4×50mm)を装備したThermo Fisher Scientific(Waltham, USA)製のICS 3000 Dionexクロマトグラフィーシステムを使用した。このシステムは、PEEKチュービング(内径0.25mm)、GM-4勾配ミキサー(2mm)、0.25μLのチャネル容量のEDアンペリメトリーセル、pH-Ag/AgCl基準電極、0.002インチのガスケット、及び使い捨て金電極を用いて組み立てた。泳動は、30℃のカラム温度で、25μLの注入容量及び1mL/分の流速で行った。分析物の分離に使用した溶離剤勾配は、100mM NaOH及び7.5mM酢酸ナトリウム(NaOAc)を用いて、0分で開始した。後者は、100mM NaOHを維持しながら、67.5分で100mMまで直線的に増大させた。カラムを洗浄するために、NaOAcの濃度を100mM NaOHで4分間、650mMまで増大させ、その後、各々の泳動後、100mM NaOHで16.3分間再平衡化した。PADによる炭水化物検出は、2Hzに設定された「標準炭水化物四重線(quad)」波形(波形B)に基づいた。
20%(wt/wt)のTKPを、実施例3に従って、3%(wt/wt TKP)の配列番号3で24時間加水分解した。試料を、15分、30分、45分、1時間、2時間、3時間、4時間、8時間、及び24時間後に採取し、実施例7に記載されているHPAEC-PADを用いて分析した。産生されたオリゴ糖のピーク面積(nC*分)を、DP7、DP8、及びDP9オリゴ糖について個別に決定し、各々のオリゴ糖のパーセンテージを決定した。
多糖キシログルカンは、その大部分が1,6結合キシロース側鎖で置換されている、β1→4結合グルコース残基の骨格を有する。キシロース残基は、多くの場合、ガラクトースで修飾されている。単糖へのさらなるキシログルカン加水分解の可能性を解析するために、本発明者らは、特に、酵素的加水分解後の単量体グルコース及びガラクトースの含有量を分析した。
オリゴ糖の代謝安定性を、統合型全食物繊維アッセイキット(Megazyme, Ireland)を用いて評価した。XGOS試料をAOAC法2011.25に記載されている酵素で消化し、HPAEC-PADを用いる実施例7に記載されている酵素処理の後に、オリゴ糖組成を分析した。キシログルカンオリゴ糖は、ブタ膵臓アミラーゼ及びアミログルコシダーゼによる加水分解に抵抗性であり、XGOSを可溶性食物繊維とみなした。
水分活性(aW値)は、25℃でNovasina(Lachen, Switzerland)製のSprintのAW装置を用いて決定した。エタノール沈殿を伴わないで精製されたオリゴ糖の水分含有量は、0.311であった。エタノール沈殿を含めて調製されたaW XGOS値は、0.327であった。
食品及び飼料製品のために、酸安定性が必要である。酸に対するDP7~DP9 XGOSの安定性を試験するために、10%(wt/vol) XGOSを水(pH 7.0)に溶解させ、37℃で2時間インキュベートし、10mM HCl(pH 2.0)で処理され、かつ同じ条件でインキュベートされた同量のXGOSと比較した。分析は、HPAEC-PADにより行った。pH 7.0の試料とpH 2.0の試料の間のオリゴ糖組成に、違いは観察されなかった。
ペレット化、押出成形、又は低温殺菌プロセスのために、熱安定性が必要である。熱に対するDP7~DP9 XGOSの安定性を試験するために、10%(wt/vol) XGOSを水(pH 7.0)に溶解させ、97℃で10分間インキュベートし、同量の未処理XGOSと比較した。分析は、HPAEC-PADにより行った。熱処理の後、薄い沈殿が観察され、これは、XGOS溶解性に影響を及ぼさなかった。熱処理は、DP7~DP9 XGOSの組成を変化させず、熱処理試料と非熱処理試料で等量のXGOSが検出された。単糖又は二糖の増加は、検出することができなかった。10%(wt/vol) XGOS溶液を121℃及び2バールで20分間インキュベートし、80%を上回るXGOSが上清に残存した。XGOS組成は変化しなかった。さらに、単量体画分は、増加しなかった。
(態様1)
キシログルカン源からキシログルカンオリゴ糖(XGOS)を産生する方法であって、50℃よりも高い温度でキシログルカナーゼ活性を示す酵素による50℃よりも高い温度でのキシログルカンの酵素的加水分解を含み、該酵素が5mMと同じ又はそれよりも高い最終生成物阻害定数(Ki)を示すことを特徴とする、前記方法。
(態様2)
前記キシログルカン源が、タマリンド、ペパーグラス、ナタネ、リンゴ、ビルベリー、ブルーベリー、オリーブ、又はこれらの画分を含む他のキシログルカン源、例えば、タマリンドカーネルパウダー、脱脂タマリンドカーネルパウダー、タマリンド種子、並びに他の源の種子及び細胞壁である、態様1記載の方法。
(態様3)
前記酵素が、好ましくは、GHファミリー5、9、12、16、44、又は74から選択されるエンドグルカナーゼである、態様1又は2記載の方法。
(態様4)
前記酵素が、配列番号1~配列番号4から選択されるポリペプチドと少なくとも75%の配列同一性を有する、態様1~3のいずれか一項記載の方法。
(態様5)
前記酵素が宿主細胞で組換え産生され、かつ該宿主細胞が前記キシログルカン源に対する内在性キシログルカナーゼ活性を示さない、態様1~4のいずれか一項記載の方法。
(態様6)
・前記多糖のキシログルカナーゼ加水分解を促進する条件下で、配列番号1~配列番号4から選択されるポリペプチドと少なくとも75%の配列同一性を有する酵素で水溶液中のキシログルカン源を加水分解して、キシログルカン源多糖加水分解物の溶液を形成させる
:工程を含む、態様1~5のいずれか一項記載の方法。
(態様7)
・固形物の除去;
・例えば、イオン交換クロマトグラフィーによる、タンパク質及び塩の除去;
・例えば、限外濾過又はナノ濾過による、着色剤の除去;並びに
・前記溶液からの前記キシログルカン源多糖加水分解物の回収
:のうちの1以上の工程をさらに含む、態様1~6のいずれか一項記載の方法。
(態様8)
前記酵素が前記キシログルカン源の0.05%(w/w)又はそれ未満の量で存在し、かつ/又は使用される該キシログルカン源の最終量が100g/l以上である、態様1~7のいずれか一項記載の方法。
(態様9)
DP7~DP9 XGOSの混合物を含むか、該混合物から本質的になるか、又は該混合物からなるキシログルカン加水分解物が産生される、態様1~8のいずれか一項記載の方法。
(態様10)
食品、動物飼料製品、又は他の製品を産生するための、態様1~9のいずれか一項記載の方法で産生されるDP7~DP9 XGOS混合物を含む加水分解物の使用。
(態様11)
態様1~9のいずれか一項記載の方法で産生されるDP7~DP9 XGOS混合物を含む製品。
(態様12)
エンドグルカナーゼ活性を有する酵素であって、配列番号2、3、又は4によるポリペプチドと少なくとも75%のアミノ酸配列同一性を有するポリペプチドを含むか、該ポリペプチドから本質的になるか、又は該ポリペプチドからなり、ただし、該エンドグルカナーゼが配列番号1のポリペプチドではない、前記酵素。
(態様13)
態様12記載のエンドグルカナーゼをコードする核酸配列を含む核酸分子。
(態様14)
キシログルカン源からXGOSの混合物を産生するための、態様12記載の酵素の使用であって、該混合物が、DP7~DP9 XGOSを含むか、DP7~DP9 XGOSから本質的になるか、又はDP7~DP9 XGOSからなる、前記使用。
Claims (11)
- キシログルカン源からキシログルカンオリゴ糖(XGOS)を産生する方法であって、配列番号1~配列番号4から選択されるポリペプチド、又は、配列番号1~配列番号4から選択されるポリペプチドと少なくとも90%の配列同一性を有するポリペプチドである酵素による、50.5℃~80℃の範囲の温度かつ5.5~7.5の範囲のpHでのキシログルカンの酵素的加水分解を含み、該酵素が50.5℃~80℃の範囲の温度かつ5.5~7.5の範囲のpHでキシログルカナーゼ活性を示し、該酵素が5mMと同じ又はそれよりも高い最終生成物阻害定数(Ki)を示すことを特徴とする、前記方法。
- 前記キシログルカン源が、タマリンド、ペパーグラス、ナタネ、リンゴ、ビルベリー、ブルーベリー、オリーブ、又はこれらの画分を含む他のキシログルカン源である、請求項1記載の方法。
- 前記キシログルカン源が、タマリンドカーネルパウダー、脱脂タマリンドカーネルパウダー、タマリンド種子、並びに他の源の種子及び細胞壁である、請求項1又は2記載の方法。
- 前記酵素が宿主細胞で組換え産生され、かつ該宿主細胞が前記キシログルカン源に対する内在性キシログルカナーゼ活性を示さない、請求項1~3のいずれか一項記載の方法。
- ・前記キシログルカン源のキシログルカナーゼ加水分解を促進する条件下で、請求項1記載の酵素で水溶液中のキシログルカン源を加水分解して、キシログルカン源多糖加水分解物の溶液を形成させる
:工程を含む、請求項1~4のいずれか一項記載の方法。 - ・固形物の除去;
・タンパク質及び塩の除去;
・着色剤の除去;並びに
・前記溶液からのキシログルカン源多糖加水分解物の回収
:のうちの1以上の工程をさらに含む、請求項5記載の方法。 - 前記酵素が前記キシログルカン源の0.05%(w/w)又はそれ未満の量で存在し、かつ/又は使用される該キシログルカン源の最終量が100g/l以上である、請求項1~6のいずれか一項記載の方法。
- DP7~DP9 XGOSの混合物を含むか又は該混合物からなるキシログルカン加水分解物が産生される、請求項1~7のいずれか一項記載の方法。
- エンドグルカナーゼ活性を有する酵素であって、配列番号2、3又は4によるポリペプチド、又は、配列番号2、3又は4によるポリペプチドと少なくとも90%の配列同一性を有するポリペプチドからなり、ただし、該エンドグルカナーゼが配列番号1のポリペプチドではない、前記酵素。
- 請求項9記載の酵素をコードする核酸配列からなる、核酸分子。
- 50.5℃~80℃の範囲の温度かつ5.5~7.5の範囲のpHでキシログルカン源からXGOSの混合物を産生するための、請求項9記載の酵素の使用であって、該混合物が、DP7~DP9 XGOSを含むか又はDP7~DP9 XGOSからなる、前記使用。
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2017
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JP2010252789A (ja) | 2009-03-31 | 2010-11-11 | Toyota Central R&D Labs Inc | セルロース分解のためのタンパク質複合体及びその利用 |
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JP2021503953A (ja) | 2021-02-15 |
US20200362379A1 (en) | 2020-11-19 |
IN202037025779A (ja) | 2020-06-18 |
US11618913B2 (en) | 2023-04-04 |
EP3488854A1 (en) | 2019-05-29 |
CN111836625A (zh) | 2020-10-27 |
US20230407355A1 (en) | 2023-12-21 |
WO2019101648A1 (en) | 2019-05-31 |
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