استخراج کلاژن‌های محلول در اسید و محلول در پپسین از فلس کپور معمولی (Cyprinus carpio) و تعیین ویژگی‌های آنها

نوع مقاله : مقاله پژوهشی

نویسندگان

• مرجان زرگر ¹
• بهاره شعبان پور ²
• پرستو پورعاشوری ¹
• ابراهیم ذبیحی نیشابوری ³

¹ گروه عمل‌آوری فراورده‌های شیلاتی، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران.

² گروه عمل‌آوری فراورده‌های شیلاتی، دانشگاه علوم کشاورزی و منابع طبیعی گرگان، گرگان، ایران

³ گروه فارماکولوژی، دانشگاه علوم پزشکی بابل، ایران.

https://doi.org/10.22067/ifstrj.2022.74164.1121

چکیده

کلاژن فراوان‌ترین و مهم‌ترین پروتئین ساختاری در بافت‌ همبند جانوران است که تولید آن اهمیت زیادی در زمینه‌های پزشکی و دارویی، آرایشی- بهداشتی و غذایی دارد. با توجه به محدودیت‌های مذهبی و نیز بیماری‌های مشترک بین دام و انسان، امروزه استحصال کلاژن به دیگر منابع و به‌ویژه منابع آبزی معطوف شده است. بنابراین هدف این مطالعه استخراج کلاژن به دو شیوه مرسوم اسیدی و آنزیمی از فلس کپور معمولی و تعیین ویژگی‌های آن به‌منظور استفاده بهینه از این پسماند برای تولید محصولات با ارزش افزوده و یافتن جایگزینی برای کلاژن به‌دست آمده از حیوانات خشکی می‌باشد. کلاژن محلول در اسید (Acid soluble collagen) و کلاژن محلول در پپسین (Pepsin soluble collagen) از فلس کپور معمولی (Cyprinus carpio) استخراج و خواص آنها تعیین شد. فلس‌های کپور معمولی پس از آماده‌سازی به کمک اسیداستیک 5/0 مولار و آنزیم پپسین تحت استخراج قرار گرفته در نهایت کلاژن استخراج شده، لیوفیلیزه شد و پس از محاسبه بازده استخراج، ویژگی‌های آن با استفاده از آزمون‌های الکتروفورز، طیف‌سنجی فرابنفش، پراش اشعه ایکس و تعیین نقطه ایزوالکتریک مورد بررسی قرار گرفت. یافته‌ها نشان داد که بازده استخراج ASC و PSC به‌ترتیب 9/1% و 96/2% (بر مبنای وزن خشک) بود یعنی هضم با پپسین می‌تواند تا 54/1 برابر باعث افزایش بازده کلاژن شود. نتایج آنالیز SDS-PAGE نشان داد هر دو ASC و PSC به‌عنوان کلاژن نوع I بوده و ازα₁ ، α₂ و β در ساختار زنجیره‌ای (α₁)₂α₂ تشکیل شده­اند؛ نقطه ایزوالکتریک کلاژن‌ها در دامنه pH 5- 6 قرار داشت. حداکثر پیک جذب طیف فرابنفش کلاژن‌های به‌دست آمده در 235 نانومتر مشاهده شد. اگرچه آنزیم پپسین (1% وزن خشک فلس) باعث افزایش بازده بدون تغییر معنی‌دار در ساختار کلاژن می‌شود ولی استفاده از آن برای تولید انبوه کلاژن نوع I در ایران تا رسیدن به خودکفایی و کاهش قیمت پپسین، توصیه نمی‌شود این درحالیست که استخراج کلاژن به روش اسیدی بسیار ساده بوده و تحقیق جهت طراحی خط تولید برای این روش پیشنهاد می‌شود. فلس کپور معمولی این پتانسیل را دارد که به‌عنوان منبع جایگزین کلاژن در صنایع غذایی و بهداشتی- دارویی به‌کار رود. این نتایج می‌تواند علاوه بر تولید محصول با ارزش افزوده بالا از فلس کپور معمولی، راهکاری برای کنترل ضایعات صنعت فرآوری آبزیان در ایجاد آلودگی محیط زیست ارائه دهد.

کلیدواژه‌ها

• فلس
• کپور معمولی (Cyprinus carpio)
• کلاژن محلول در اسید
• کلاژن محلول در پپسین
• ضایعات

موضوعات

• شیمی مواد غذایی

عنوان مقاله [English]

Extraction of acid-soluble and pepsin-soluble collagens from common carp scales (Cyprinus carpio) and determination of their characteristics

نویسندگان [English]

• Marjan Zargar ¹
• Bahareh Shabanpour ²
• Parastoo Pourashouri ¹
• Ebrahim Zabihi Neyshbouri ³

¹ Fisheries Products Processing Department, Gorgan University of Agricultural Sciences and Natural Resources, Gorgan, Iran.

² Fisheries Products Processing Department, Gorgan University of Agricultural Sciences and Natural Resources, Gorgan, Iran.

³ Department of Pharmacology, Babol University of Medical Sciences, Iran.

چکیده [English]

[1]Introduction: Collagen is the most abundant and important structural protein in the connective tissue of animals, the production of which is of great importance in the fields of medicine, cosmetics and food. Due to religious restrictions as well as common diseases between livestock and humans, today collagen extraction has turned to other sources, especially aquatic sources. Therefore, the aim of this study was to extract collagen by conventional acidic and enzymatic methods from common carp scales and determine its characteristics in order to make optimal use of this waste to produce valuable products and find alternatives to collagen obtained from land animals.
 
Material and Method: Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from common carp scales (Cyprinus carpio) and their properties were determined. Common carp scales were prepared with the use of 0.5 M acetic acid and pepsin enzyme. Finally, the extracted collagens were lyophilized and after calculating the extraction efficiencies, their characteristics were determined by electrophoresis tests, UV spectroscopy, X-ray diffraction and isoelectric point determination.
 
 
Results and Discussion: The results showed that the extraction efficiencies of ASC and PSC were 1.9% and 2.96% (based on dry weight), respectively, which means digestion with pepsin could increase collagen efficiency up to 1.54 times. The results of SDS-PAGE analysis showed that both ASC and PSC are type I collagen and are composed of α₁, α₂ and β in the (α₁) ₂α₂ chain structure; the isoelectric point of collagens was in the pH range of 5-6. The maximum absorption peak of the UV spectrum of collagen was observed at 235 nm. Although pepsin enzyme (1% dry weight of scales) increases efficiency without significant changes in collagen native structure, but its use for mass production of type I collagen in Iran is not recommended unless self-sufficiency and reduction of pepsin price achieved, while collagen extraction by acidic method is very simple and research to design a production line for this method is recommended. Common carp scales have the potential to be used as an alternative source of collagen in the food and health-pharmaceutical industries. These results can provide a solution to control the waste of the aquatic processing industry in creating environmental pollution, as well as producing a high value-added product from common carp scales.

کلیدواژه‌ها [English]

• Scales
• Common carp (Cyprinus carpio)
• Acid-soluble collagen
• Pepsin-soluble collagen
• Waste

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