Aᴅɪᴛʏᴀ Pʀᴜsʜᴏᴛᴛᴀᴍ

XII-C

Bᴜʀɴᴘᴜʀ Rɪᴠᴇʀsɪᴅᴇ Sᴄʜᴏᴏʟ,

Bᴜʀɴᴘᴜʀ -713325

Pᴀsᴄʜɪᴍ Bᴀʀᴅʜᴀᴍᴀɴ

Wᴇsᴛ Bᴇɴɢᴀʟ
 𝕮 𝖔 𝖓 𝖙 𝖊 𝖓 𝖙 𝖘 :-
SERIAL TOPIC:- PAGE Remarks/
No. No. signature
01.

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03. 𝓐𝓲𝓶

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06.
𝒯𝒽ℯℴ𝓇𝓎:-

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08. 𝕺𝖇𝖘𝖊𝖗𝖛𝖆𝖙𝖎𝖔𝖓s:-

09. 𝕽𝖊𝖘𝖚𝖑𝖙𝖘 :-
10. 𝓟𝓻𝓮𝓬𝓪𝓾𝓽𝓲𝓸𝓷𝓼:-
11. 𝕭𝖎𝖇𝖑𝖎𝖔𝖌𝖗𝖆𝖕𝖍𝖞
 𝕭𝖚𝖗𝖓𝖕𝖚𝖗 𝕽𝖎𝖛𝖊𝖗𝖘𝖎𝖉𝖊 𝕾𝖈𝖍𝖔𝖔𝖑
𝕭𝖚𝖗𝖓𝖕𝖚𝖗-713325
𝖂𝖊𝖘𝖙 𝕭𝖊𝖓𝖌𝖆𝖑

-:𝕮𝖍𝖊𝖒𝖎𝖘𝖙𝖗𝖞 𝕯𝖊𝖕𝖆𝖗𝖙𝖒𝖊𝖓𝖙:-
𝐓𝐡𝐢𝐬 𝐢𝐬 𝐭𝐨 𝐜𝐞𝐫𝐭𝐢𝐟𝐲 𝐭𝐡𝐚𝐭 𝐀𝐝𝐢𝐭𝐲𝐚 𝐏𝐫𝐮𝐬𝐡𝐨𝐭𝐭𝐚𝐦 𝐨𝐟 𝐜𝐥𝐚𝐬𝐬
𝐗𝐈𝐈(𝐂) ,𝐑𝐨𝐥𝐥 𝐍𝐨:-________𝐬tu𝐝𝐲𝐢𝐧𝐠 𝐢𝐧 𝐭𝐡𝐢𝐬 𝐢𝐧𝐬𝐭𝐢𝐭𝐮𝐭𝐢𝐨𝐧,
𝐡𝐚𝐬 𝐬𝐮𝐜𝐜𝐞𝐬𝐬𝐟𝐮𝐥𝐥𝐲 𝐜𝐨𝐦𝐩𝐥𝐞𝐭𝐞𝐝 𝐓𝐇𝐄 𝐈𝐍𝐕𝐄𝐒𝐓𝐈𝐆𝐀𝐓𝐎𝐑𝐘
𝐏𝐑𝐎𝐉𝐄𝐂𝐓, 𝐞𝐧𝐭𝐢𝐭𝐥𝐞𝐝:-"𝐃𝐄𝐓𝐄𝐑𝐌𝐈𝐍𝐀𝐓𝐈𝐎𝐍 𝐎𝐅 𝐐𝐔𝐀𝐍𝐓𝐈𝐓𝐘
𝐎𝐅 𝐂𝐀𝐒𝐄𝐈𝐍 𝐏𝐑𝐄𝐒𝐄𝐍𝐓 𝐈𝐍 𝐃𝐈𝐅𝐅𝐄𝐑𝐄𝐍𝐓 𝐒𝐀𝐌𝐏𝐋𝐄𝐒 𝐎𝐅
𝐌𝐈𝐋𝐊" ,𝐛𝐚𝐬𝐞𝐝 𝐨𝐧 𝐂𝐁𝐒𝐄 𝐆𝐔𝐈𝐃𝐄𝐋𝐈𝐍𝐄𝐒 𝟐𝟎𝟐𝟐-𝟐𝟑 𝐚𝐧𝐝 𝐡𝐚𝐬
𝐠𝐢𝐯𝐞𝐧 𝐚 𝐬𝐚𝐭𝐢𝐬𝐟𝐚𝐜𝐭𝐨𝐫𝐲 𝐚𝐜𝐜𝐨𝐮𝐧𝐭 𝐨𝐟 𝐢𝐭 𝐢𝐧 𝐭𝐡𝐢𝐬 𝐫𝐞𝐩𝐨𝐫𝐭 . 𝐓𝐡𝐢𝐬
𝐩𝐫𝐨𝐣𝐞𝐜𝐭 𝐰𝐢𝐥𝐥 𝐩𝐚r𝐭𝐢𝐚𝐥𝐥𝐲 𝐟𝐮𝐥𝐟𝐢𝐥 𝐭𝐡𝐞 𝐩𝐮𝐫𝐩𝐨𝐬𝐞 𝐨𝐟
𝐂𝐇𝐄𝐌𝐈𝐒𝐓𝐑𝐘 𝐏𝐑𝐀𝐂𝐓𝐈𝐂𝐀𝐋 𝐄𝐗𝐀𝐌𝐈𝐍𝐀𝐓𝐈𝐎𝐍.

𝐈 𝐰𝐢𝐬𝐡 𝐡𝐢𝐦 𝐬𝐮𝐜𝐜𝐞𝐬𝐬 𝐢𝐧 𝐟𝐮𝐭𝐮𝐫𝐞...

𝐃𝐚𝐭𝐞 :-
Mr.𝐏𝐫𝐚𝐛𝐡𝐚t 𝐃𝐮𝐭𝐭𝐚
(𝐃𝐞𝐩𝐚𝐫𝐭𝐦𝐞𝐧𝐭 𝐨𝐟
𝐂𝐡𝐞𝐦𝐢𝐬𝐭𝐫𝐲)
𝑨𝒄𝒌𝒏𝒐𝒘𝒍𝒆𝒅𝒈𝒆𝒎𝒆𝒏𝒕 :-
ℑ 𝔞𝔪 𝔳𝔢𝔯𝔶 𝔤𝔯𝔞𝔱𝔢𝔣𝔲𝔩 𝔱𝔬 𝔐𝔯. S.K. S𝔦𝔫𝔥𝔞,
𝔥𝔬𝔫𝔬𝔲𝔯𝔞𝔟𝔩𝔢 P𝔯𝔦𝔫𝔠𝔦𝔭𝔞𝔩 & 𝔇𝔦𝔯𝔢𝔠𝔱𝔬𝔯 𝔰𝔦𝔯 𝔣𝔬𝔯 𝔞𝔩𝔩
𝔱𝔥𝔦𝔰 𝔥𝔢𝔩𝔭 𝔞𝔫𝔡 𝔪𝔬𝔱𝔦𝔳𝔞𝔱𝔦𝔬. ℑ 𝔬𝔴𝔢 𝔪𝔲𝔠𝔥 𝔱𝔬
𝔐𝔯. P𝔯𝔞𝔟𝔥𝔞𝔱 𝔇𝔲𝔱𝔱𝔞 𝔣𝔬𝔯 𝔥𝔦𝔰 𝔰𝔲𝔭𝔭𝔬𝔯𝔱 𝔞𝔫𝔡
𝔤𝔲𝔦𝔡𝔞𝔫𝔠𝔢. ℑ 𝔴𝔬𝔲𝔩𝔡 𝔞𝔩𝔰𝔬 𝔩𝔦k𝔢 𝔱𝔬 𝔱𝔥𝔞𝔫k 𝔪y
𝔭𝔞𝔯𝔢𝔫𝔱𝔰 𝔞𝔫𝔡 𝔣𝔯𝔦𝔢𝔫𝔡𝔰 𝔣𝔬𝔯 𝔱𝔥𝔢𝔦𝔯 𝔥𝔢𝔩𝔭 𝔞𝔫𝔡
𝔞𝔰𝔰𝔦𝔰𝔱𝔞𝔫𝔠𝔢.

_________________________________
-: 𝓐𝓲𝓶:-
Tᴏ Sᴛᴜᴅʏ Tʜᴇ Aᴍᴏᴜɴᴛ Oғ Cᴀseɪɴ
Pʀᴇsᴇɴᴛ Iɴ Dɪғғᴇʀᴇɴᴛ Sᴀᴍᴘʟᴇs Oғ
Mɪʟᴋ……
𝕴𝖓𝖙𝖗𝖔𝖉𝖚𝖈𝖙𝖎𝖔𝖓
𝐶𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑡𝑕𝑒 𝑑𝑜𝑚𝑖𝑛𝑎𝑛𝑡 𝑝𝑟𝑜𝑡𝑒𝑖𝑛 𝑔𝑟𝑜𝑢𝑝 𝑖𝑛 𝑏𝑜𝑣𝑖𝑛𝑒 𝑚𝑖𝑙𝑘 𝑎𝑛𝑑 𝑖𝑠 𝑡𝑕𝑒
𝑚𝑎𝑗𝑜𝑟 𝑓𝑢𝑛𝑐𝑡𝑖𝑜𝑛𝑎𝑙 𝑐𝑜𝑛𝑡𝑟𝑖𝑏𝑢𝑡𝑜𝑟 𝑡𝑜 𝑎 𝑓𝑎𝑚𝑖𝑙𝑦 𝑜𝑓 𝑑𝑎𝑖𝑟𝑦 𝑖𝑛𝑔𝑟𝑒𝑑𝑖𝑒𝑛𝑡𝑠
𝑤𝑕𝑖𝑐𝑕 𝑎𝑟𝑒 𝑢𝑠𝑒𝑑 𝑢𝑏𝑖𝑞𝑢𝑖𝑡𝑜𝑢𝑠𝑙𝑦 𝑖𝑛 𝑡𝑕𝑒 𝑓𝑜𝑜𝑑 𝑖𝑛𝑑𝑢𝑠𝑡𝑟𝑦. 𝑇𝑕𝑒 𝑐𝑎𝑠𝑒𝑖𝑛𝑠 𝑎𝑟𝑒
𝑛𝑎𝑡u𝑟𝑒-𝑑𝑒𝑠𝑖𝑔𝑛𝑒𝑑 𝑡𝑜 𝑏𝑒 𝑑𝑖𝑠𝑝𝑒𝑟𝑠𝑒𝑑 𝑖𝑛 𝑎𝑛 𝑎𝑞𝑢𝑒𝑜𝑢𝑠 𝑠𝑜𝑙𝑣𝑒𝑛𝑡, 𝑐𝑎𝑟𝑟𝑦
𝑟𝑒𝑙𝑎𝑡𝑖𝑣𝑒𝑙𝑦 𝑙𝑎𝑟𝑔𝑒 𝑞𝑢𝑎𝑛𝑡𝑖𝑡𝑖𝑒𝑠 𝑜𝑓 𝑐𝑎𝑙𝑐𝑖𝑢𝑚 𝑎𝑛𝑑 𝑐𝑎𝑙𝑐𝑖𝑢𝑚 𝑝𝑕𝑜𝑠𝑝𝑕𝑎𝑡𝑒 𝑎𝑛𝑑
𝑠𝑡𝑖𝑙𝑙 𝑚𝑎𝑖𝑛𝑡𝑎𝑖𝑛 𝑎 𝑙𝑜𝑤 𝑣𝑖𝑠𝑐𝑜𝑠𝑖𝑡𝑦 𝑎𝑡 ∼ 2.5% (𝑤/𝑤) 𝑐𝑜𝑛𝑐𝑒𝑛𝑡𝑟𝑎𝑡𝑖𝑜𝑛. 𝑇𝑕𝑒
𝑔𝑒𝑛𝑒𝑟𝑎𝑙 𝑐𝑜𝑚𝑝𝑜𝑠𝑖𝑡𝑖𝑜𝑛 𝑜𝑓 𝑏𝑜𝑣𝑖𝑛𝑒 𝑚𝑖𝑙𝑘 𝑖𝑠 𝑜𝑢𝑡𝑙𝑖𝑛𝑒𝑑 𝑖𝑛 𝑇𝑎𝑏𝑙𝑒 2.1. 𝐷𝑢𝑒 𝑡𝑜
𝑡𝑕𝑒 𝑙𝑖𝑞𝑢𝑖𝑑 𝑛𝑎𝑡𝑢𝑟𝑒 𝑜𝑓 𝑏𝑜𝑣𝑖𝑛𝑒 𝑚𝑖𝑙𝑘, 𝑡𝑕𝑒 𝑑𝑎𝑖𝑟𝑦 𝑖𝑛𝑑𝑢𝑠𝑡𝑟𝑦 𝑕𝑎𝑠 𝑡𝑕𝑒
𝑐𝑎𝑝𝑎𝑏𝑖𝑙𝑖𝑡𝑦 𝑜𝑓 𝑓𝑟𝑎𝑐𝑡𝑖𝑜𝑛𝑎𝑡𝑖𝑛𝑔 𝑡𝑕𝑒 𝑐𝑜𝑚𝑝𝑜𝑛𝑒𝑛𝑡𝑠 𝑟𝑒𝑠𝑢𝑙𝑡𝑖𝑛𝑔 𝑖𝑛 𝑎𝑛 𝑎𝑟𝑟𝑎𝑦
𝑜𝑓 𝑓𝑢𝑛𝑐𝑡𝑖𝑜𝑛𝑎𝑙 𝑖𝑛𝑔𝑟e𝑑𝑖𝑒𝑛𝑡𝑠 𝑓𝑜𝑟 𝑎𝑝𝑝𝑙𝑖𝑐𝑎𝑡𝑖𝑜𝑛 𝑖𝑛 𝑡𝑕𝑒 𝑓𝑜𝑜𝑑 𝑖𝑛𝑑𝑢𝑠𝑡𝑟𝑦. 𝑇𝑕𝑖𝑠
𝑐𝑕𝑎𝑝𝑡𝑒𝑟 𝑤𝑖𝑙𝑙 𝑐𝑜𝑛𝑐𝑒𝑛𝑡𝑟𝑎𝑡𝑒 𝑜𝑛 𝑡𝑕𝑒 𝑚𝑒𝑡𝑕𝑜𝑑𝑠 𝑜𝑓 𝑠𝑒𝑝𝑎𝑟𝑎𝑡𝑖𝑜𝑛 𝑜𝑓 𝑡𝑕𝑒 𝑐𝑎𝑠𝑒𝑖𝑛
𝑐𝑜𝑚𝑝𝑜𝑛𝑒𝑛𝑡𝑠 𝑓𝑟𝑜𝑚 𝑏𝑜𝑣𝑖𝑛𝑒 𝑚𝑖𝑙𝑘 𝑎𝑛𝑑 𝑡𝑕𝑒 𝑚𝑎𝑛𝑦 𝑓𝑢𝑛𝑐𝑡𝑖𝑜𝑛𝑎𝑙 𝑎𝑡𝑡𝑟𝑖𝑏𝑢𝑡𝑒𝑠
𝑡𝑕𝑎𝑡 𝑐𝑎𝑛 𝑏𝑒 𝑔𝑒𝑛𝑒𝑟𝑎𝑡𝑒𝑑 𝑏𝑦 𝑖𝑛𝑐𝑙𝑢𝑠𝑖𝑜𝑛 𝑜𝑓 𝑡𝑕𝑒 ca𝑠𝑒𝑖𝑛-𝑏𝑎𝑠𝑒𝑑 𝑖𝑛𝑔𝑟𝑒𝑑𝑖𝑒𝑛𝑡𝑠
𝑖𝑛 𝑓𝑜𝑜𝑑 𝑠𝑦𝑠𝑡𝑒𝑚𝑠.

𝐶𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑡𝑕𝑒 𝑚𝑜𝑠𝑡 𝑖𝑚𝑝𝑜𝑟𝑡𝑎𝑛𝑡 𝑝𝑟𝑜𝑡𝑒𝑖𝑛 𝑐𝑜𝑚𝑝𝑜𝑛𝑒𝑛𝑡 𝑖n 𝑚𝑖𝑙𝑘, 𝑏𝑜𝑡𝑕

𝑞𝑢𝑎𝑛𝑡𝑖𝑡𝑎𝑡𝑖𝑣𝑒𝑙𝑦 𝑎𝑛𝑑 𝑛𝑢𝑡𝑟𝑖𝑡𝑖𝑜𝑛𝑎𝑙𝑙𝑦, 𝑎𝑐𝑐𝑜𝑢𝑛𝑡𝑖𝑛𝑔 𝑓𝑜𝑟 𝑎𝑏𝑜𝑢𝑡 80% 𝑜𝑓
𝑚𝑖𝑙𝑘’𝑠 𝑡𝑜𝑡𝑎𝑙 𝑛𝑖𝑡𝑟𝑜𝑔𝑒𝑛. 𝐼𝑡 𝑤𝑎𝑠 𝑢𝑠𝑒𝑑 𝑖𝑛 𝑖𝑛𝑑𝑢𝑠𝑡𝑟𝑖𝑒𝑠 𝑝𝑟𝑜𝑑𝑢𝑐𝑖𝑛𝑔 𝑝𝑎𝑝𝑒𝑟,
𝑡𝑒x𝑡𝑖𝑙𝑒𝑠, 𝑝𝑎𝑖𝑛𝑡, 𝑙𝑒𝑎𝑡𝑕𝑒𝑟, 𝑓𝑖𝑏𝑒𝑟, 𝑎𝑛𝑑 𝑜𝑡𝑕𝑒𝑟 𝑚𝑎𝑡𝑒𝑟𝑖𝑎𝑙𝑠. 𝐸d𝑖𝑏𝑙𝑒 𝑐𝑎𝑠𝑒𝑖𝑛 𝑎𝑛𝑑
𝑐𝑎𝑠𝑒𝑖𝑛𝑎𝑡𝑒𝑠 𝑎𝑟𝑒 𝑎𝑙𝑠𝑜 𝑙𝑜𝑛𝑔 𝑒𝑠𝑡𝑎𝑏𝑙𝑖𝑠𝑕𝑒𝑑 𝑑𝑎𝑖𝑟𝑦 𝑏𝑦𝑝𝑟𝑜𝑑𝑢𝑐𝑡𝑠 𝑤𝑖𝑡𝑕 𝑢𝑠𝑒𝑠 𝑖𝑛
𝑚𝑎𝑛𝑦 𝑓𝑜𝑜𝑑𝑠. 𝐶𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑎 𝑣𝑒𝑟𝑦 𝑟𝑖𝑐𝑕 𝑠𝑜𝑢𝑟𝑐𝑒 𝑜𝑓 𝑒𝑠𝑠𝑒𝑛𝑡𝑖𝑎𝑙 𝑎𝑚𝑖𝑛𝑜 𝑎𝑐𝑖𝑑𝑠,
𝑤𝑖𝑡𝑕 𝑡𝑕𝑒 𝑜𝑛𝑙𝑦 𝑝𝑜𝑠𝑠𝑖𝑏𝑙𝑒 𝑒𝑥𝑐𝑒𝑝𝑡𝑖𝑜𝑛 𝑜𝑓 𝑐𝑦𝑠𝑡𝑒𝑖𝑛𝑒. 𝐼𝑡 𝑖𝑠 𝑎 𝑝𝑕𝑜𝑠𝑝𝑕𝑜𝑟𝑦𝑙𝑎𝑡𝑒𝑑
𝑎𝑛𝑑 𝑔𝑙𝑦𝑐𝑜𝑠𝑖𝑙𝑎𝑡e𝑑 𝑐𝑜𝑚𝑝𝑙𝑒𝑥 𝑠𝑦𝑛𝑡𝑕𝑒𝑠𝑖𝑧𝑒𝑑 𝑏𝑦 𝑚𝑎𝑚𝑚𝑎𝑟𝑦 𝑔𝑙𝑎𝑛𝑑𝑠. 𝐼𝑡 𝑖𝑠
𝑐𝑜𝑛𝑠𝑡𝑖𝑡𝑢𝑡𝑒𝑑 𝑜𝑓 𝑡𝑕𝑟𝑒𝑒 𝑑𝑖𝑓𝑓𝑒𝑟𝑒𝑛𝑡 𝑝𝑜𝑙𝑦𝑝𝑒𝑝𝑡𝑖𝑑𝑒 𝑐𝑕𝑎𝑖𝑛𝑠 (𝛼𝑠1, 𝛼𝑠2, 𝑎𝑛𝑑 ß)
𝑕𝑒𝑙𝑑 𝑡𝑜𝑔𝑒𝑡𝑕𝑒𝑟 𝑏𝑦 𝑛𝑜𝑛𝑐𝑜𝑣𝑎𝑙𝑒𝑛𝑡 𝑖𝑛𝑡𝑒𝑟𝑎𝑐𝑡𝑖𝑜𝑛𝑠. 𝐶𝑎𝑠𝑒𝑖𝑛 𝑓𝑟𝑎𝑐𝑡𝑖𝑜𝑛𝑠 𝑎𝑟𝑒
𝑜𝑟𝑔𝑎𝑛𝑖𝑧𝑒𝑑 𝑖𝑛 𝑚𝑖𝑐𝑒𝑙𝑙𝑎𝑟 𝑎𝑔𝑔𝑟𝑒𝑔𝑎𝑡𝑒𝑠 𝑡𝑕𝑎𝑡 𝑎𝑙𝑠𝑜 𝑐𝑜𝑛𝑡𝑎𝑖𝑛 𝑏𝑖𝑣𝑎𝑙𝑒𝑛𝑡 𝑐𝑎𝑡𝑖𝑜𝑛𝑠
(𝑐𝑎𝑙𝑐𝑖𝑢𝑚 𝑎𝑛𝑑 𝑠𝑚𝑎𝑙𝑙𝑒𝑟 𝑎𝑚𝑜𝑢𝑛𝑡𝑠 𝑜𝑓 𝑚𝑎𝑔𝑛e𝑠𝑖𝑢𝑚), 𝑟𝑎𝑛𝑔𝑖𝑛𝑔 20–300 𝑛𝑚
𝑖𝑛 𝑑𝑖𝑎𝑚𝑒𝑡𝑒𝑟. 𝑇𝑕𝑖𝑠 𝑠𝑡𝑟𝑢𝑐𝑡𝑢𝑟𝑒 𝑎𝑙𝑙𝑜𝑤𝑠 𝑕𝑖𝑔𝑕𝑙𝑦 𝑠𝑡𝑎𝑏𝑙𝑒 𝑑𝑖𝑠𝑝𝑒𝑟𝑠𝑖𝑜𝑛 𝑜𝑓
𝑕𝑦𝑑𝑟𝑜𝑝𝑕𝑜𝑏𝑖𝑐 𝑓𝑟𝑎𝑐𝑡𝑖𝑜𝑛𝑠 𝑖𝑛 𝑎 𝑐𝑜𝑙𝑙𝑜𝑖𝑑𝑎𝑙 𝑠𝑡𝑎𝑡𝑒 𝑏𝑦 𝑡𝑕𝑒 𝑎𝑐𝑡𝑖𝑜𝑛 𝑜𝑓
𝑕𝑦𝑑𝑟𝑜𝑝𝑕𝑖𝑙𝑖𝑐 𝑏𝑜𝑛𝑑𝑠.
𝑇𝑕𝑒 𝑎𝑚𝑜𝑢𝑛𝑡 𝑜𝑓 𝑐𝑎𝑠𝑒𝑖𝑛 𝑖𝑛 𝑤𝑕𝑜𝑙𝑒 𝑚i𝑙𝑘 𝑣𝑎𝑟𝑖𝑒𝑠 𝑎𝑐𝑐𝑜𝑟𝑑𝑖𝑛𝑔 𝑡𝑜 𝑡𝑕𝑒 𝑎𝑛𝑖𝑚𝑎𝑙
𝑏𝑟𝑒𝑒𝑑 𝑎𝑛𝑑 𝑠𝑡𝑎𝑔𝑒 𝑜𝑓 𝑙𝑎𝑐𝑡𝑎𝑡𝑖𝑜𝑛. 𝐼𝑡 𝑖𝑠 𝑔𝑒𝑛𝑒𝑟𝑎𝑙𝑙𝑦 𝑖𝑛 𝑡𝑕𝑒 𝑟𝑎𝑛𝑔𝑒 24–29 𝑔 𝑙−
1. 𝐶𝑎𝑠𝑒𝑖𝑛 𝑐𝑜n𝑡𝑎𝑖𝑛𝑠 0.7–0.9% 𝑝𝑕𝑜𝑠𝑝𝑕𝑜𝑟𝑢𝑠, 𝑐𝑜𝑣𝑎𝑙𝑒𝑛t𝑙𝑦 𝑏𝑜𝑢𝑛𝑑 𝑡𝑜 𝑡𝑕𝑒
𝑝𝑟𝑜𝑡𝑒𝑖𝑛 𝑏𝑦 𝑎 𝑠𝑒𝑟𝑖𝑛𝑒 𝑒𝑠𝑡𝑒𝑟 𝑙𝑖𝑛𝑘𝑎𝑔𝑒. 𝐶𝑜𝑛𝑠𝑒𝑞𝑢𝑒𝑛𝑡𝑙𝑦, 𝑐𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑘𝑛𝑜𝑤𝑛 𝑎𝑠
𝑎 𝑝𝑕𝑜𝑠𝑝𝑕𝑜p𝑟𝑜𝑡𝑒𝑖𝑛. 𝐴𝑙𝑙 𝑡𝑕𝑒 𝑎𝑚i𝑛𝑜 𝑎𝑐𝑖𝑑𝑠 𝑡𝑕𝑎𝑡 𝑎𝑟𝑒 𝑒𝑠𝑠𝑒𝑛𝑡𝑖𝑎𝑙 𝑓𝑜𝑟 𝑕𝑢𝑚𝑎𝑛𝑠
𝑎𝑟𝑒 𝑝𝑟𝑒𝑠𝑒𝑛𝑡 𝑖𝑛 𝑐𝑎𝑠𝑒𝑖𝑛 𝑖𝑛 𝑕𝑖𝑔𝑕 𝑝𝑟𝑜𝑝𝑜𝑟𝑡𝑖𝑜𝑛𝑠, 𝑤𝑖𝑡𝑕 𝑡𝑕𝑒 𝑝𝑜𝑠𝑠𝑖𝑏𝑙𝑒
𝑒𝑥𝑐𝑒𝑝𝑡𝑖𝑜𝑛 𝑜𝑓 𝑐𝑦𝑠𝑡𝑒𝑖𝑛𝑒. 𝑇𝑕𝑢𝑠, 𝑐𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑐𝑜𝑛𝑠𝑖𝑑𝑒𝑟𝑒𝑑 𝑡𝑜 𝑏𝑒 𝑎 𝑕𝑖𝑔𝑕𝑙𝑦
𝑛𝑢𝑡𝑟𝑖𝑡𝑖𝑜𝑢𝑠 𝑝𝑟𝑜𝑡𝑒𝑖𝑛. 𝐼𝑡 𝑒𝑥𝑖𝑠𝑡𝑠 𝑖𝑛 𝑚𝑖𝑙𝑘 𝑖𝑛 𝑐𝑜𝑚𝑝𝑙𝑒𝑥 𝑔𝑟𝑜𝑢𝑝𝑠 𝑜𝑓 𝑚𝑜𝑙𝑒𝑐𝑢𝑙𝑒𝑠
𝑐𝑎𝑙𝑙𝑒𝑑 𝑎𝑠 𝑚𝑖𝑐𝑒𝑙𝑙𝑒𝑠. 𝑇𝑕𝑒 𝑚𝑖𝑐𝑒𝑙𝑙𝑒𝑠 𝑐𝑜𝑛𝑠𝑖𝑠𝑡 𝑜𝑓 𝑐𝑎𝑠𝑒𝑖𝑛 𝑚o𝑙𝑒𝑐𝑢𝑙𝑒𝑠, 𝑐𝑎𝑙𝑐𝑖𝑢𝑚,
𝑖𝑛𝑜𝑟𝑔𝑎𝑛𝑖𝑐 𝑝𝑕𝑜s𝑝𝑕𝑎𝑡𝑒, 𝑎𝑛𝑑 𝑐𝑖𝑡𝑟𝑎𝑡𝑒 𝑖𝑜𝑛𝑠, 𝑎𝑛𝑑 𝑡𝑕𝑒𝑦 𝑕𝑎𝑣𝑒 𝑎 𝑡𝑦𝑝𝑖𝑐𝑎𝑙
𝑚𝑜𝑙𝑒𝑐𝑢𝑙𝑎𝑟 𝑤𝑒𝑖𝑔𝑕𝑡 𝑜𝑓 𝑠𝑒𝑣𝑒𝑟𝑎𝑙 𝑕𝑢𝑛𝑑𝑟𝑒𝑑 𝑚𝑖𝑙𝑙𝑖𝑜𝑛 𝑑a𝑙𝑡𝑜𝑛𝑠.
𝐼𝑛 𝑡𝑒𝑟𝑚𝑠 𝑜𝑓 𝑝𝑕𝑦𝑠𝑖𝑐𝑎𝑙 𝑐𝑕𝑒𝑚𝑖𝑠𝑡𝑟𝑦, 𝑡𝑕𝑒 𝑐𝑎𝑠𝑒𝑖𝑛 𝑚𝑖𝑐𝑒𝑙𝑙𝑒𝑠 𝑒𝑥𝑖𝑠𝑡 𝑖𝑛 𝑚𝑖𝑙𝑘 𝑎𝑠 𝑎
𝑣𝑒𝑟𝑦 𝑠𝑡𝑎𝑏𝑙𝑒 𝑐𝑜𝑙𝑙𝑜𝑖𝑑𝑎𝑙 𝑑𝑖𝑠𝑝𝑒𝑟𝑠𝑖𝑜𝑛. 𝐴𝑠 𝑎 𝑝𝑟𝑜𝑡𝑒𝑖𝑛, 𝑐𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑚𝑎𝑑𝑒 𝑢𝑝 𝑜𝑓
𝑕𝑢𝑛𝑑𝑟𝑒𝑑𝑠 𝑜𝑓 𝑖n𝑑𝑖𝑣𝑖𝑑𝑢𝑎𝑙 𝑎𝑚𝑖𝑛𝑜 𝑎𝑐𝑖𝑑𝑠, 𝑒𝑎𝑐𝑕 𝑜𝑓 𝑤𝑕𝑖𝑐𝑕 𝑚𝑎𝑦 𝑕𝑎𝑣𝑒 𝑎
𝑝𝑜𝑠𝑖𝑡𝑖𝑣𝑒 𝑜𝑟 𝑎 𝑛𝑒𝑔𝑎𝑡𝑖𝑣𝑒 𝑐𝑕𝑎𝑟𝑔𝑒, 𝑑𝑒𝑝𝑒𝑛𝑑𝑖𝑛𝑔 𝑜𝑛 𝑡𝑕𝑒 𝑝𝐻 𝑜𝑓 𝑡𝑕𝑒 𝑚𝑖𝑙𝑘
𝑠𝑦𝑠𝑡𝑒𝑚. 𝐴𝑡 𝑠𝑜𝑚𝑒 𝑝𝐻 𝑣a𝑙𝑢𝑒, 𝑎𝑙𝑙 𝑡𝑕𝑒 𝑝𝑜𝑠i𝑡𝑖𝑣𝑒 𝑐𝑕𝑎𝑟𝑔𝑒𝑠 𝑎𝑛𝑑 𝑎𝑙𝑙 𝑡𝑕𝑒
𝑛𝑒𝑔𝑎𝑡𝑖𝑣𝑒 𝑐𝑕𝑎𝑟𝑔𝑒𝑠 𝑜𝑛 𝑡𝑕𝑒 𝑐𝑎𝑠𝑒𝑖𝑛 𝑟𝑒𝑚𝑎𝑖𝑛 𝑖𝑛 𝑏𝑎𝑙𝑎𝑛𝑐𝑒 (𝑖.𝑒., 𝑡𝑕𝑒 𝑛𝑒𝑡
𝑐𝑕𝑎𝑟𝑔𝑒 𝑜𝑛 𝑡𝑕𝑒 𝑝𝑟𝑜𝑡𝑒𝑖𝑛 𝑖𝑠 𝑧𝑒𝑟𝑜); 𝑡𝑕𝑖𝑠 𝑝𝐻 𝑣𝑎𝑙u𝑒 𝑖𝑠 𝑘𝑛𝑜𝑤𝑛 𝑎𝑠 𝑡𝑕𝑒
𝑖𝑠𝑜𝑒𝑙𝑒𝑐𝑡𝑟𝑖𝑐 𝑝𝑜𝑖𝑛𝑡 (𝐼𝐸𝑃), 𝑤𝑕𝑖𝑐𝑕 𝑖𝑠 4.6 𝑓𝑜𝑟 𝑐𝑎𝑠𝑒𝑖𝑛. 𝑇𝑕𝑒 𝐼𝐸𝑃 𝑖𝑠 𝑡𝑕𝑒 𝑝𝐻 𝑎𝑡
𝑤𝑕𝑖𝑐𝑕 𝑡𝑕𝑒 𝑝𝑟𝑜𝑡𝑒𝑖𝑛 𝑖𝑠 𝑙𝑒𝑎𝑠𝑡 𝑠𝑜𝑙𝑢𝑏𝑙𝑒. 𝑀𝑖𝑙𝑘 𝑕𝑎𝑠 𝑎 𝑝𝐻 𝑣𝑎𝑙𝑢𝑒 𝑜𝑓 𝑎𝑏𝑜u𝑡 6.6,
𝑎𝑡 𝑤𝑕𝑖𝑐𝑕 𝑡𝑕𝑒 𝑐𝑎𝑠𝑒𝑖𝑛 𝑚𝑖𝑐𝑒𝑙𝑙𝑒𝑠 𝑕𝑎𝑣𝑒 𝑎 𝑛𝑒𝑡 𝑛𝑒𝑔𝑎𝑡i𝑣𝑒 𝑐𝑕𝑎𝑟𝑔𝑒 𝑎𝑛𝑑 𝑎𝑟𝑒
𝑞𝑢𝑖𝑡𝑒 𝑠𝑡𝑎𝑏𝑙𝑒. 𝐶𝑎𝑠𝑒𝑖𝑛 𝑐𝑜𝑛𝑠𝑖𝑠𝑡𝑠 𝑜𝑓 𝑠𝑒𝑣𝑒𝑟𝑎𝑙 𝑖𝑛𝑑𝑖𝑣𝑖𝑑𝑢𝑎𝑙 𝑐𝑎𝑠𝑒𝑖𝑛
𝑐𝑜𝑚𝑝𝑜𝑛𝑒𝑛𝑡𝑠 (𝛼𝑠1-, 𝛼𝑠2-, 𝛽-, 𝑎𝑛𝑑 𝜅-𝑐𝑎𝑠𝑒𝑖𝑛), 𝑒𝑎𝑐𝑕 𝑕𝑎𝑣𝑖𝑛𝑔 𝑠𝑙𝑖𝑔𝑕𝑡𝑙𝑦
𝑑𝑖𝑓𝑓𝑒r𝑒𝑛𝑡 𝑝𝑟𝑜𝑝𝑒𝑟𝑡𝑖𝑒𝑠.
𝐶𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑝𝑟𝑒𝑐𝑖𝑝𝑖𝑡𝑎𝑡𝑒𝑑 𝑓𝑟𝑜𝑚 𝑠𝑘𝑖𝑚 𝑚𝑖𝑙𝑘 𝑏𝑦 𝑎𝑐𝑖𝑑𝑖𝑓𝑦𝑖𝑛𝑔 𝑖𝑡 𝑡𝑜 𝑝𝑟𝑜𝑑𝑢𝑐𝑒
𝑎𝑐𝑖𝑑 𝑐𝑎𝑠𝑒𝑖𝑛, 𝑜𝑟 𝑡𝑕𝑒 𝑚𝑖𝑙𝑘 𝑖𝑠 𝑡𝑟𝑒𝑎𝑡𝑒𝑑 𝑤𝑖𝑡𝑕 𝑟𝑒𝑛𝑛𝑒𝑡 𝑡𝑜 𝑝𝑟𝑜𝑑𝑢𝑐𝑒 𝑟𝑒𝑛𝑛𝑒𝑡
𝑐𝑎𝑠𝑒𝑖𝑛. 𝑇𝑕𝑒 𝑝𝑟𝑒𝑐𝑖𝑝𝑖𝑡𝑎𝑡𝑒𝑑 𝑐𝑎𝑠𝑒𝑖𝑛 𝑐𝑢𝑟𝑑 𝑖𝑠 𝑠𝑒𝑝𝑎𝑟𝑎𝑡𝑒𝑑 𝑓𝑟𝑜𝑚 𝑡𝑕𝑒 𝑤𝑕𝑒𝑦,
𝑤𝑎𝑠𝑕𝑒𝑑, 𝑎𝑛𝑑 𝑑𝑟𝑖𝑒𝑑. 𝑇𝑕𝑒 𝑤𝑎t𝑒𝑟-𝑠𝑜𝑙𝑢𝑏𝑙𝑒 𝑑𝑒r𝑖𝑣𝑎𝑡𝑖𝑣𝑒𝑠 𝑜𝑓 𝑎𝑐𝑖𝑑 𝑐𝑎𝑠𝑒𝑖𝑛𝑠,
𝑝𝑟𝑜𝑑𝑢𝑐e𝑑 𝑏𝑦 𝑟𝑒𝑎𝑐𝑡𝑖𝑜𝑛 𝑤𝑖𝑡𝑕 𝑎𝑙𝑘𝑎𝑙𝑖𝑠, 𝑎𝑟𝑒 𝑐𝑎𝑙𝑙𝑒𝑑 𝑐𝑎𝑠𝑒𝑖𝑛𝑎𝑡𝑒𝑠. 𝐸𝑑𝑖𝑏𝑙𝑒
𝑐𝑎𝑠𝑒𝑖𝑛 𝑖𝑠 𝑎 𝑙𝑜𝑛𝑔-𝑒𝑠𝑡𝑎𝑏𝑙𝑖𝑠𝑕𝑒𝑑 𝑑𝑎𝑖𝑟𝑦 𝑏𝑦𝑝𝑟𝑜𝑑𝑢𝑐𝑡 𝑢𝑠𝑒𝑑 𝑎𝑠 𝑎𝑛 𝑖𝑛𝑔𝑟𝑒𝑑𝑖𝑒𝑛𝑡
𝑖𝑛 𝑚𝑎𝑛𝑦 𝑓𝑜𝑜𝑑 𝑝𝑟𝑜𝑑𝑢𝑐𝑡𝑠, 𝑖𝑛𝑐𝑙𝑢𝑑𝑖𝑛𝑔 𝑑𝑎𝑖𝑟𝑦 𝑝𝑟𝑜𝑑𝑢𝑐𝑡𝑠. 𝑇𝑕𝑒 𝑔𝑒𝑛𝑒𝑟𝑎𝑙
𝑑𝑒𝑣𝑒𝑙𝑜𝑝𝑚𝑒𝑛𝑡 𝑜𝑓 𝑓𝑜𝑜𝑑 𝑡𝑒𝑐𝑕𝑛𝑜𝑙𝑜𝑔𝑖𝑒𝑠 𝑎𝑛𝑑 𝑡𝑕𝑒𝑖𝑟 𝑎𝑝𝑝𝑙𝑖𝑐𝑎𝑡𝑖𝑜𝑛𝑠 𝑕𝑎𝑠
𝑖𝑛c𝑟𝑒𝑎𝑠𝑒𝑑 𝑡𝑕𝑒 𝑝𝑟𝑜𝑑𝑢𝑐𝑡𝑖𝑜𝑛 𝑜𝑓 𝑎𝑛𝑑 𝑑𝑒𝑚𝑎n𝑑 𝑓𝑜𝑟 𝑐𝑎𝑠𝑒𝑖𝑛. 𝐼𝑡𝑠
𝑚𝑎𝑛𝑢𝑓𝑎𝑐𝑡𝑢𝑟𝑒 𝑑𝑖𝑓𝑓𝑒𝑟𝑠 𝑓𝑟𝑜𝑚 𝑡𝑕𝑎𝑡 𝑜𝑓 𝑛𝑜𝑛𝑒𝑑𝑖𝑏𝑙𝑒 𝑐𝑎𝑠𝑒𝑖𝑛 (𝑎𝑙𝑠𝑜 𝑐𝑎𝑙𝑙𝑒𝑑
𝑖𝑛𝑑𝑢𝑠𝑡𝑟𝑖𝑎𝑙 𝑐𝑎𝑠𝑒𝑖𝑛) 𝑖𝑛 𝑡𝑕𝑎𝑡 𝑐𝑎𝑠𝑒𝑖𝑛 𝑓𝑜𝑟 𝑓𝑜𝑜𝑑 𝑖𝑠 𝑝𝑟𝑜𝑑𝑢𝑐𝑒𝑑 𝑢𝑛𝑑𝑒𝑟
𝑠𝑎𝑛𝑖𝑡𝑎𝑟𝑦 𝑐𝑜𝑛𝑑𝑖𝑡𝑖𝑜𝑛𝑠. 𝐹𝑢𝑟𝑡𝑕𝑒𝑟, 𝑑𝑢𝑟𝑖𝑛𝑔 𝑖𝑡𝑠 𝑚𝑎𝑛𝑢𝑓𝑎𝑐𝑡u𝑟𝑒, 𝑓𝑜𝑜𝑑-𝑔𝑟𝑎𝑑𝑒
𝑐𝑕𝑒𝑚𝑖𝑐𝑎𝑙𝑠 𝑎𝑟𝑒 𝑢𝑠𝑒𝑑 𝑎𝑛𝑑 𝑠𝑢𝑓𝑓𝑖𝑐𝑖𝑒𝑛𝑡𝑙𝑦 𝑕𝑒𝑎𝑡-𝑡𝑟𝑒𝑎𝑡𝑒𝑑 𝑡𝑜 𝑚𝑎𝑘𝑒 𝑡𝑕𝑒
𝑐𝑎𝑠𝑒𝑖𝑛 𝑠𝑎𝑓𝑒 𝑓𝑜𝑟 𝑕𝑢𝑚𝑎𝑛 𝑐𝑜𝑛𝑠𝑢𝑚𝑝𝑡𝑖𝑜𝑛. 𝑇𝑕𝑒 𝑖𝑛𝑡𝑒𝑛𝑠𝑖𝑣𝑒 𝑖𝑛𝑣𝑒𝑠𝑡𝑖𝑔𝑎𝑡𝑖𝑜𝑛
𝑖𝑛t𝑜 𝑚𝑎𝑛𝑢𝑓𝑎𝑐𝑡𝑢𝑟𝑖𝑛𝑔 𝑡𝑒𝑐𝑕𝑛𝑜𝑙𝑜𝑔𝑖𝑒𝑠 𝑜𝑣𝑒𝑟 𝑡𝑕𝑒 𝑦𝑒𝑎𝑟𝑠 𝑎𝑛𝑑 𝑡𝑕𝑒
𝑖𝑛𝑡𝑟𝑜𝑑𝑢𝑐𝑡𝑖𝑜𝑛 𝑜𝑓 𝑒𝑓𝑓𝑖𝑐𝑖𝑒𝑛𝑡 𝑝𝑙𝑎𝑛𝑡 𝑑𝑒𝑠𝑖𝑔𝑛𝑠 𝑕𝑎𝑣𝑒 𝑖𝑚𝑚𝑒𝑛𝑠𝑒𝑙𝑦 𝑖𝑚𝑝𝑟𝑜𝑣𝑒𝑑
𝑡𝑕𝑒 𝑡𝑒𝑐𝑕𝑛𝑜𝑙𝑜𝑔𝑦 𝑓𝑜𝑟 𝑒𝑑𝑖𝑏𝑙𝑒 𝑐𝑎𝑠𝑒𝑖𝑛 𝑝𝑟𝑜𝑑𝑢𝑐𝑡𝑖𝑜𝑛.
A𝖕𝖕𝖆𝖗𝖆𝖙𝖚s &
𝕮𝖍𝖊𝖒𝖎𝖈𝖆𝖑𝖘
𝕽𝖊𝖖𝖚𝖎𝖗𝖊𝖉 :-

𝖥𝗎𝗇𝗇𝖾𝗅, 𝖥𝗎𝗇𝗇𝖾𝗅 𝖲𝗍𝖺𝗇 , 𝖦𝗅𝖺𝗌𝗌 𝖱𝗈𝖽, 𝖥𝗂𝖻𝗋𝖾

𝖯𝖺𝗉𝖾𝗋 , 𝖶𝖾𝗂g𝗁𝗍 𝖡𝗈𝗑, 𝖳𝖾𝗌𝗍 𝖳𝗎𝖻𝖾, 𝖯𝖾𝗌𝗍𝖾𝗅 𝖺𝗇𝖽
𝖬𝗈𝗋𝗍𝖺𝗋
𝗂)𝖣𝗂𝖿𝖿𝖾𝗋𝖾𝗇𝗍 𝖲𝖺𝗆𝗉𝗅𝖾𝗌 𝖮𝖿 𝖬𝗂𝗅𝗄
𝗂𝗂)𝖲𝖺𝗍𝗎𝗋𝖺𝗍𝖾𝖽 𝖠𝗆𝗆𝗈𝗇𝗂𝗎𝗆 𝖲𝗎𝗅𝗉𝗁𝖺𝗍𝖾 𝖲𝗈𝗅𝗎𝗍𝗂𝗈𝗇
𝗂𝗂𝗂)𝟣% 𝖠𝖼𝖾𝗍𝗂𝖼 𝖠𝖼𝗂𝖽 𝖲𝗈𝗅𝗎𝗍𝗂𝗈𝗇
𝒯𝒽ℯℴ𝓇𝓎:-

Mɪʟᴋ ᴄᴏɴᴛᴀɪɴs 3 ᴛᴏ 4 % Cᴀsᴇɪɴ

sᴜsᴘᴇɴᴅᴇᴅ ɪɴ ᴡᴀᴛᴇʀ ɪɴ ᴛʜᴇ
ᴄᴏʟʟᴏɪᴅᴀʟ ғᴏʀᴍ .
Iᴛ ɪs ᴘʀᴇᴄɪᴘɪᴛᴀᴛᴇᴅ ɪɴ ᴡᴇᴀᴋʟʏ
ᴀᴄɪᴅɪᴄ sᴏʟᴜᴛɪᴏɴ.
𝓟𝓻𝓸𝓬𝓮𝓭𝓾𝓻𝓮:-
1) 𝑾𝒂𝒔𝒉 𝒕𝒉𝒆 𝒃𝒆𝒂𝒌𝒆𝒓 (500 𝒎𝒍) 𝒘𝒊𝒕𝒉 𝒅𝒊𝒔𝒕𝒊𝒍𝒍𝒆𝒅 𝒘𝒂𝒕𝒆𝒓
𝒂𝒏𝒅 𝒅𝒓𝒚 𝒊𝒕.
2) 𝑻𝒂𝒌𝒆 200 𝒎𝒍 𝒐𝒇 𝒃𝒖𝒇𝒇𝒂𝒍𝒐❜𝒔 𝒎𝒊𝒍𝒌 𝒊𝒏 𝒕𝒉𝒆 500 𝒎𝒍
𝒃𝒆𝒂𝒌𝒆𝒓 𝒂𝒏𝒅 𝒓𝒆𝒄𝒐𝒓𝒅 𝒊𝒕𝒔 𝒘𝒆𝒊𝒈𝒉𝒕
3) 𝑨𝒅𝒅 20 𝒎𝒍 𝒐𝒇 𝒔𝒂𝒕𝒖𝒓𝒂𝒕𝒆𝒅 𝒔𝒐𝒍𝒖𝒕𝒊𝒐𝒏 𝒐𝒇 𝑨𝒎𝒎𝒐𝒏𝒊𝒖𝒎
𝑺𝒖𝒍𝒑𝒉𝒂𝒕𝒆 𝒔𝒍𝒐𝒘𝒍𝒚 𝒘𝒊𝒕𝒉 𝒔𝒕𝒐𝒓𝒊𝒏 .𝑭𝒂𝒕
𝒂𝒏𝒅 𝑪𝒂𝒔𝒆𝒊𝒏 𝒘𝒊𝒍𝒍 𝒔𝒆𝒑𝒂𝒓𝒂𝒕𝒆 𝒐𝒖𝒕 𝒂𝒔 𝒑𝒓𝒆𝒄𝒊𝒑𝒊𝒕𝒂𝒕𝒆 .
4)F𝒊𝒍𝒕𝒆𝒓 𝒕𝒉𝒆 𝒂𝒃𝒐𝒗𝒆 𝒔𝒐𝒍𝒖𝒕𝒊𝒐𝒏 𝒂𝒏𝒅 𝒕𝒓𝒂𝒏𝒔𝒇𝒆𝒓 𝒕𝒉𝒆
𝒑𝒓𝒆𝒄𝒊𝒑𝒊𝒕𝒂𝒕𝒆 𝒊𝒏 𝒂𝒏𝒐𝒕𝒉𝒆𝒓 𝒃𝒆𝒂𝒌𝒆𝒓.
5)T𝒓𝒆𝒂𝒕 𝒕𝒉𝒆 𝒂𝒃𝒐𝒗𝒆 𝒑𝒓𝒆𝒄𝒊𝒑𝒊𝒕𝒂𝒕𝒆 𝒘𝒊𝒕𝒉 30 𝒎𝒍 𝒅𝒊𝒔𝒕𝒊𝒍𝒍𝒆𝒅
𝒘𝒂𝒕𝒆𝒓. 𝑪𝒂𝒔𝒆𝒊𝒏 𝒅𝒊𝒔𝒔𝒐𝒍𝒗𝒆𝒔 𝒊𝒏 𝒘𝒂𝒕𝒆𝒓 𝒇𝒐𝒓𝒎𝒊𝒏𝒈 𝒂 𝒎𝒊𝒍𝒌𝒚
𝒔𝒐𝒍𝒖𝒕𝒊𝒐𝒏 𝒘𝒉𝒆𝒓𝒆𝒂𝒔 𝒇𝒂𝒕 𝒓𝒆𝒎𝒂𝒊𝒏𝒔 𝒂𝒔 𝒔𝒖𝒄𝒉.
6)W𝒂𝒓𝒎 𝒕𝒉𝒆 𝒂𝒃𝒐𝒗𝒆 𝒄𝒐𝒏𝒕𝒆𝒏𝒕𝒔 𝒐𝒇 𝒕𝒉𝒆 𝒃𝒆𝒂𝒌𝒆𝒓 𝒕𝒐 40-
45°𝑪 𝒐𝒏 𝒂 𝒍𝒐𝒘 𝒇𝒍𝒂𝒎𝒆. 𝑵𝒐𝒘, 𝒂𝒅𝒅 1% 𝑨𝒄𝒆𝒕𝒊𝒄 𝑨𝒄𝒊d
s𝒐𝒍𝒖𝒕𝒊𝒐𝒏 𝒔𝒕𝒊𝒓𝒓𝒊𝒏𝒈 𝒅𝒓𝒐𝒑𝒘𝒊𝒔𝒆 𝒘𝒉𝒆𝒏 𝒄𝒂𝒔𝒆𝒊𝒏 𝒈𝒆𝒕𝒔
𝒑𝒓𝒆𝒄𝒊𝒑𝒊𝒕𝒂𝒕𝒆𝒅.
7) F 𝒊𝒍𝒕𝒆𝒓 𝒕𝒉𝒆 𝒑𝒓𝒆𝒄𝒊𝒑𝒊𝒕𝒂𝒕𝒆𝒅 𝑪𝒂𝒔𝒆𝒊𝒏 𝒂𝒏𝒅 𝒘𝒂𝒔𝒉 𝒘𝒊𝒕𝒉
𝒅𝒊𝒔𝒕𝒊𝒍𝒍𝒆𝒅 𝒘𝒂𝒕e𝒓 𝒂𝒏𝒅 𝒅𝒓𝒚 𝒊𝒕.
8) F 𝒊𝒏𝒅 𝒕𝒉𝒆 𝒘𝒆𝒊𝒈𝒉𝒕 𝒐𝒇 𝒕𝒉𝒆 𝒅𝒓𝒚 𝒑𝒓𝒆𝒄𝒊𝒑𝒊𝒕𝒂t𝒆.
9)R𝒆𝒑𝒆𝒂𝒕 𝒕𝒉𝒆 𝒘𝒉𝒐𝒍𝒆 𝒆𝒙𝒑𝒆𝒓𝒊𝒎𝒆𝒏𝒕 𝒘𝒊𝒕𝒉 𝒄𝒐𝒘❜𝒔 𝒎𝒊𝒍𝒌,
𝒈𝒐𝒂𝒕❜𝒔 𝒎𝒊𝒍𝒌.
𝕺𝖇𝖘𝖊𝖗𝖛𝖆𝖙𝖎𝖔𝖓s:-
𝑉𝑜𝑙𝑢𝑚𝑒 𝑜𝑓 𝑒𝑎𝑐𝑕 𝑚𝑖𝑙𝑘 𝑠𝑎𝑚𝑝𝑙𝑒 𝑖𝑠 200 𝑚𝑙

𝑆𝑎𝑚𝑝𝑙𝑒 𝑆𝑜𝑢𝑟𝑐𝑒 𝐶𝑜𝑛𝑡𝑒𝑛𝑡𝑠 𝘈𝘮𝘰𝘶𝘯𝘵 % 𝑂𝑓

𝑁𝑢𝑚𝑏𝑒𝑟 𝑜𝑓 𝘖𝘧 𝐶𝑎𝑠𝑒𝑖𝑛
𝑃𝑟𝑜𝑡𝑒𝑖𝑛 𝘊𝘢𝘴𝘦𝘪𝘯 (𝑔/𝑚𝑙)
(𝘨/𝘮𝘭)
01. 𝐶𝑜𝑤'𝑠 0.60𝘨 𝟎.𝟓 𝟓
𝑀𝑖𝑙𝑘
02. 𝐺𝑜𝑎𝑡'𝑠 0.65𝘨 𝟎.𝟒 𝟑.𝟐𝟓
𝑀𝑖𝑙𝑘
03. 𝐵𝑢𝑓𝑓𝑎𝑙𝑜'𝑠 0.85𝘨 𝟎.𝟑𝟒 𝟒.𝟐𝟎
𝑀𝑖𝑙𝑘
𝕽𝖊𝖘𝖚𝖑𝖙𝖘 :-
𝐴𝑐𝑐𝑜𝑟𝑑𝑖𝑛𝑔 𝑡𝑜 𝑜𝑢𝑟 𝑎𝑛𝑎𝑙𝑦𝑠𝑖𝑠
𝑜𝑓 𝑣𝑎𝑟𝑖𝑜𝑢𝑠 𝑠𝑎𝑚𝑝𝑙𝑒𝑠 𝑜𝑓 𝑚𝑖𝑙𝑘 ,
𝑤𝑒 𝑐𝑜𝑛𝑐𝑙𝑢𝑑𝑒 𝑡𝑕𝑎𝑡 :-

𝐶𝑜𝑤 𝑚𝑖𝑙𝑘 𝑐𝑜𝑛𝑡𝑎𝑖ns 5%

𝐶𝑎𝑠𝑒𝑖𝑛

𝐺𝑜𝑎𝑡 𝑚𝑖𝑙𝑘 𝑐𝑜𝑛𝑡𝑎𝑖ns 3.25%

𝐶𝑎𝑠𝑒𝑖𝑛
𝐵𝑢𝑓𝑓𝑎𝑙𝑜 𝑚𝑖𝑙𝑘 𝑐𝑜𝑛𝑎𝑡𝑖ns 4.2%
𝐶𝑎𝑠𝑒𝑖𝑛

-:𝓟𝓻𝓮𝓬𝓪𝓾𝓽𝓲𝓸𝓷𝓼:-
1. 𝐻𝑎𝑛𝑑𝑙𝑒 𝑡𝑕𝑒 𝐴𝑝𝑝𝑎𝑟𝑎𝑡𝑢𝑠 𝑎𝑛𝑑 𝐶𝑕𝑒𝑚𝑖𝑐𝑎𝑙𝑠
𝑐𝑎𝑟𝑒𝑓𝑢𝑙𝑙𝑦

2.𝐴𝑑𝑑 𝐴𝑚𝑚𝑜𝑛𝑖𝑢𝑚 𝑆𝑢𝑙𝑝𝑕𝑎𝑡𝑒 𝑆𝑜𝑙𝑢𝑡𝑖𝑜𝑛𝑠

𝑣𝑒𝑟𝑦 𝑐𝑎𝑟𝑒𝑓𝑢𝑙𝑙𝑦

3.𝑆𝑡𝑖𝑟 𝑚𝑖𝑙𝑘 𝑤𝑕𝑖𝑙𝑒 𝑎𝑑𝑑𝑖𝑛𝑔 𝑐𝑕𝑒𝑚𝑖𝑐𝑎𝑙𝑠.

4.𝐷𝑜 𝑛𝑜𝑡 𝑑𝑖𝑠𝑡𝑢𝑟𝑏 𝑚𝑖𝑙𝑘 𝑎𝑓𝑡𝑒𝑟 𝑎𝑑𝑑𝑖𝑛𝑔

𝑎𝑚𝑚𝑚𝑜𝑖𝑛𝑢𝑚 𝑠𝑢𝑙𝑝𝑕𝑎𝑡𝑒 𝑠𝑜𝑙𝑢𝑡𝑖𝑜𝑛 𝑎𝑛𝑑
𝑤𝑎𝑖𝑡 𝑓𝑜r 𝑠𝑜𝑚𝑒 𝑡𝑖𝑚𝑒 𝑓𝑜𝑟 𝐹𝑎𝑡 𝑎𝑛𝑑 𝐶𝑎𝑠𝑒𝑖𝑛
𝑡𝑜 𝑝𝑟𝑒𝑐𝑖𝑝𝑖𝑡𝑎𝑡𝑒 𝑜𝑢𝑡.

5.𝑇𝑎𝑘𝑒 𝑡𝑕𝑒 𝑎𝑚𝑜𝑢𝑛𝑡 𝑟𝑒𝑎𝑑𝑖𝑛𝑔𝑠 𝑐𝑎𝑟𝑒𝑓𝑢𝑙𝑙𝑦

𝑤𝑖𝑡𝑕 𝑑𝑖𝑔𝑖𝑡𝑎𝑙 𝑤𝑒𝑖𝑔𝑕𝑖𝑛𝑔 𝑚𝑎𝑐𝑕𝑖𝑛𝑒 𝑜𝑛𝑙𝑦
 -:𝕭𝖎𝖇𝖑𝖎𝖔𝖌𝖗𝖆𝖕𝖍𝖞:-
✪ 𝔚𝔦k𝔦𝔭𝔢𝔡𝔦𝔞.𝔬𝔯𝔤
✪ ℭ𝔥𝔢𝔪𝔦𝔭𝔯𝔬𝔧𝔢𝔠𝔱𝔰.𝔟𝔩𝔬𝔤𝔰𝔭𝔬𝔱.𝔦𝔫
✪ 𝔖𝔠𝔯𝔦𝔟𝔡.𝔠𝔬𝔪

•••⁗…⁗…⁗…⁗…⁗…⁗…⁗…⁗…⁗•••
•✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽✽•

❗❗❗𝙏𝙝𝙖𝙣𝙠 𝙔𝙤𝙪 ❗❗❗

𝘼𝙇𝙇 𝙍𝙄𝙂𝙃𝙏𝙎 𝙍𝙀𝙎𝙀𝙍𝙑𝙀𝘿 © 𝘽𝙔

✪ 𝘽𝙐𝙍𝙉𝙋𝙐𝙍 𝙍𝙄𝙑𝙀𝙍𝙎𝙄𝘿𝙀 𝙎𝘾𝙃𝙊𝙊𝙇

(𝙝𝙩𝙩𝙩𝙥𝙨://𝙬𝙬𝙬.𝙗𝙧𝙨𝙗𝙪𝙧𝙣𝙥𝙪𝙧.𝙘𝙤𝙢)

✪ 𝘾𝙀𝙉𝙏𝙍𝘼𝙇 𝘽𝙊𝘼𝙍𝘿 𝙊𝙁 𝙎𝙀𝘾𝙊𝙉𝘿𝘼𝙍𝙔 𝙀𝘿𝙐𝘾𝘼𝙏𝙄𝙊𝙉

(𝙬𝙬𝙬.𝙘𝙗𝙨𝙚.𝙣𝙞𝙘.𝙞𝙣)