Evaluating each statement

A. “It produces large amount of recombinant protein.” – Correct

Pichia pastoris grows to very high cell densities and uses strong, inducible promoters (like AOX1), often giving high yields of recombinant proteins suitable for industrial production.

B. “It has the property of secreting proteins into the medium.” – Correct

With an appropriate signal peptide (e.g., α‑factor signal), Pichia can secrete expressed proteins into the culture medium, simplifying downstream purification and reducing host‑cell contaminants.

C. “It allows the formation of disulphide bonds similar to those in humans.” – Correct

As a eukaryotic yeast with a functional endoplasmic reticulum and oxidative folding machinery, Pichia forms disulfide bonds in secretory proteins in a way much more similar to mammalian cells than bacteria do, enabling proper folding of many human proteins.

D. “It carries out protein glycosylations identical to those found in humans.” – Incorrect

Pichia performs N‑linked and O‑linked glycosylation, but the patterns are yeast‑type (e.g., high‑mannose, hyperglycosylated), not identical to human complex glycans.
For many therapeutics, this difference can affect half‑life or immunogenicity, and glyco‑engineering is often needed to “humanize” its glycosylation.

Why option (2) is correct

• A, B, and C describe genuine advantages of Pichia pastoris as a host for human therapeutic proteins.

• D is false because Pichia’s glycosylation is not identical to human glycosylation.

Thus, the correct combination is A, B and C only (option 2).