Plant and bacterial proteases: A key towards improving meat tenderization, a mini review

Figures & data

Figure 1. Enzymatic mechanism of protein hydrolysis by cysteine proteases (Bekhit et al., 2014; Grzonka et al., 2007).

Table 1. pH, Temperature (⁰C) and strength of hydrolysis of myofibrillar proteins and collagen by various enzymes¹

Protease	Active pH	Optimal pH	Active range	Optimal temperature	Hydrolysis of myofibrillar proteins	Hydrolysis of collagen
Papain	4.0–9.0	4.0–6.0	50–80	65–75	Excellent	Moderate
Bromelain	4.0–7.0	5.0–6.0	50–80	65–75	Moderate	Excellent
Ficin	5.0–9.0	7.0	45–75	60–70	Moderate	Excellent
Aspergillus	5.0–9.0	7.0	50–65	55–60	Moderate	Poor
Bacillus	2.5–7.0	<6.5	40–60	55–60	Poor	Excellent

¹ Derived from Calkin and Sullivan (2007).

Table 2. The activity and application of different plant proteases

Enzymes	Activity and application as meat tenderization	References
Papain	The recommended dose of papain for meat tenderization is 0.6% with better texture and quality of meat. The dose exceeding the limit may affect the quality and texture	Abdel-Naeem and Mohamed (2016)
Papain	The addition of ginger and papain powder improved the physico-chemical and sensory properties of camel burger patties	Akpan and Omojola (2015)
Bromelain	The purified bromelain completely ruptures the myofibril tissues in meat which shows higher tenderization of meat by using scanning electron microscopy analysis	Chaurasiya et al. (2015)
Ficin	This enzyme can be inhibited by oxidizing agents and divalent metals with small strengths and this inhibition can be changed	Ramezani et al. (2003)
Actinidin	The actinidin has less tenderization property as compared to other traditional plant proteases and still not approved as GRAS by FDA	Toohey, Kerr, van de Ven, and Hopkins (2011)
Calpain	Both m-calpain and μ-calpain are cysteine proteases, and their proteolytic activity is affected by oxidation, which can influence the quality of fresh meat	Zhang et al. (2013)
Bacterial enzymes	The bacterial enzymes hydrolyses the myofibril and collagen proteins more efficiently than the papain	Ha et al. (2013)

Figure 2. Schematic diagram for the effect of papain in either active or inactive form in ante-mortem and post-mortem conditions (Bekhit et al., 2014; Dransfield & Etherington, 1981).

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