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Author: search.filters.author.Nalinanon, SitthipongSubject: search.filters.subject.Antidiabetic

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    Alpha-amylase inhibitory activity of collagen hydrolysate from Asian bullfrog skin and its application in dark chocolate
    (2024-01-01)
    Indriani, Sylvia
    ;
    Benjakul, Soottawat
    ;
    Sitanggang, Azis Boing
    ;
    Karnjanapratum, Supatra
    ;
    Nalinanon, Sitthipong
    The present study aimed to investigate the in-vitro antidiabetic activity of collagen hydrolysate (CH) from Asian bullfrog skin and its application as a bioactive compound in dark chocolate bars. Papain (3% [w/w]) was used to obtain CH with a simultaneous conjunction of ultrasound. CH possessed α-amylase inhibitory activity with an IC<inf>50</inf> value of 3.60 mg/mL, while results from inhibition reaction kinetics revealed that CH inhibited α-amylase in a non-competitive mode. Different concentrations (0.5, 1.0, and 2.0% [w/w]) of CH were then fortified into dark chocolate bars, and the physicochemical characteristics, breaking strength, and rheological behaviour of the resulting chocolate were investigated and compared with a control (without CH addition). A higher level of CH significantly enhanced antidiabetic activity against α-amylase (p ≤ 0.05) in chocolate bar. Chocolate bar with 2% CH complied with the nutritional claim requirement for ‘source of protein’ with lower fat content and energy value, while sensory evaluation revealed good organoleptic properties.
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    Structural characteristic and molecular docking simulation of fish protein-derived peptides: Recent updates on antioxidant, anti-hypertensive and anti-diabetic peptides
    (2023-03-30)
    Prakash Nirmal, Nilesh
    ;
    Singh Rajput, Mithun
    ;
    Bhojraj Rathod, Nikheel
    ;
    Mudgil, Priti
    ;
    Pati, Siddhartha
    Over the decade, fish protein-derived peptides (FPDP) have been evaluated for various biological activities including their mechanism of action through structure–activity relationship (SAR) and molecular simulation. SAR studies are known to provide the basic structural information of the active site which can be used for designing synthetic bioactive peptides for application in therapeutics and medicinal purposes. In light of the above discussion, this review discusses the mechanism of action and SAR of the FPDP with a focus on three widely studied bioactive properties including antioxidant, antihypertensive and anti-diabetic activities. The emphasis is given to the recently purified and identified FPDP from various seafood resources. A brief discussion has been made on their structural characteristics and mechanism of action towards antioxidant, angiotensin-I converting enzyme (ACE) inhibition, and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities. Additionally, the importance and future perspective of SAR of food-derived bioactive peptides have been addressed.